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Journal articles on the topic 'Myristylation'

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Published: 4 June 2021
Last updated: 7 February 2022

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1

Garber, E. A., F. R. Cross, and H. Hanafusa. "Processing of p60v-src to its myristylated membrane-bound form." Molecular and Cellular Biology 5, no. 10 (1985): 2781–88. http://dx.doi.org/10.1128/mcb.5.10.2781.

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p60src of wild-type Rous sarcoma virus is myristylated at its N-terminal glycine residue. We have shown previously that this myristylation is necessary for p60src membrane association and for cell transformation by using src mutants with alterations within the N-terminal 30 kilodaltons of p60src. In this study we analyzed the process of p60src myristylation in wild type- and mutant-infected cells. All myristylated src proteins examined lack the initiator methionine, but two mutant src proteins lacking the initiator methionine are not myristylated, indicating that removal of the initiator methionine and myristylation are not obligatorily coupled. Analysis of the kinetics of myristylation and the association of p60src with cellular proteins p50 and p90 indicated that myristylation occurs before p60src becomes membrane associated and that transient association with p50 and p90 occurs regardless of myristylation. Myristylation is required for stable association of p60src with the plasma membrane but is not sufficient for membrane association. A mutant with an src deletion of amino acids 169 through 264 has an src protein that is myristylated but not membrane bound, remaining stably associated with p50 and p90. This mutant is transformation defective. Several N-terminal deletion mutants possessing tyrosine kinase activity have myristylated and membrane-bound src proteins but are not fully active in cell transformation, suggesting that additional N-terminal functional domains exist.
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2

Garber, E. A., F. R. Cross, and H. Hanafusa. "Processing of p60v-src to its myristylated membrane-bound form." Molecular and Cellular Biology 5, no. 10 (1985): 2781–88. http://dx.doi.org/10.1128/mcb.5.10.2781-2788.1985.

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p60src of wild-type Rous sarcoma virus is myristylated at its N-terminal glycine residue. We have shown previously that this myristylation is necessary for p60src membrane association and for cell transformation by using src mutants with alterations within the N-terminal 30 kilodaltons of p60src. In this study we analyzed the process of p60src myristylation in wild type- and mutant-infected cells. All myristylated src proteins examined lack the initiator methionine, but two mutant src proteins lacking the initiator methionine are not myristylated, indicating that removal of the initiator methionine and myristylation are not obligatorily coupled. Analysis of the kinetics of myristylation and the association of p60src with cellular proteins p50 and p90 indicated that myristylation occurs before p60src becomes membrane associated and that transient association with p50 and p90 occurs regardless of myristylation. Myristylation is required for stable association of p60src with the plasma membrane but is not sufficient for membrane association. A mutant with an src deletion of amino acids 169 through 264 has an src protein that is myristylated but not membrane bound, remaining stably associated with p50 and p90. This mutant is transformation defective. Several N-terminal deletion mutants possessing tyrosine kinase activity have myristylated and membrane-bound src proteins but are not fully active in cell transformation, suggesting that additional N-terminal functional domains exist.
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3

Clark, B., and U. Desselberger. "Myristylation of Rotavirus Proteins." Journal of General Virology 69, no. 10 (1988): 2681–86. http://dx.doi.org/10.1099/0022-1317-69-10-2681.

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4

Kaplan, J. M., G. Mardon, J. M. Bishop, and H. E. Varmus. "The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant." Molecular and Cellular Biology 8, no. 6 (1988): 2435–41. http://dx.doi.org/10.1128/mcb.8.6.2435.

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The transforming protein of Rous sarcoma virus, pp60v-src, is covalently coupled to myristic acid by an amide linkage to glycine 2. Myristylation promotes the association of pp60v-src with cellular membranes, and this subcellular location is essential for transforming activity. The findings presented here, in conjunction with the previous reports of others, imply that the seventh amino acid encoded by v-src might be important in the myristylation reaction. Replacement of lysine 7 by asparagine greatly reduced the myristylation, membrane association, and transforming activity of pp60v-src. In contrast, substitution of arginine at residue 7 had no effect on any of these properties of pp60v-src. Addition of amino acids 1 to 7 encoded by v-src was sufficient to cause myristylation of a src-pyruvate kinase fusion protein. We conclude that the recognition sequence for myristylation of pp60v-src comprises amino acids 1 to 7 and that lysine 7 is a critical component of this sequence.
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5

Kaplan, J. M., G. Mardon, J. M. Bishop, and H. E. Varmus. "The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant." Molecular and Cellular Biology 8, no. 6 (1988): 2435–41. http://dx.doi.org/10.1128/mcb.8.6.2435-2441.1988.

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The transforming protein of Rous sarcoma virus, pp60v-src, is covalently coupled to myristic acid by an amide linkage to glycine 2. Myristylation promotes the association of pp60v-src with cellular membranes, and this subcellular location is essential for transforming activity. The findings presented here, in conjunction with the previous reports of others, imply that the seventh amino acid encoded by v-src might be important in the myristylation reaction. Replacement of lysine 7 by asparagine greatly reduced the myristylation, membrane association, and transforming activity of pp60v-src. In contrast, substitution of arginine at residue 7 had no effect on any of these properties of pp60v-src. Addition of amino acids 1 to 7 encoded by v-src was sufficient to cause myristylation of a src-pyruvate kinase fusion protein. We conclude that the recognition sequence for myristylation of pp60v-src comprises amino acids 1 to 7 and that lysine 7 is a critical component of this sequence.
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6

Kamata, N., and J. T. Holt. "Inhibitory effect of myristylation on transrepression by FBR (Gag-Fos) protein." Molecular and Cellular Biology 12, no. 2 (1992): 876–82. http://dx.doi.org/10.1128/mcb.12.2.876.

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The myristylated v-fos product, FBR murine sarcoma virus (Gag-Fos) protein, exhibits a lower level of transrepression of the serum response element (SRE) than does c-fos protein (Fos). Mutation of the N-terminal myristylation site in FBR protein restored SRE transrepression. Replacement of N-terminal viral Gag sequences with the Fos N terminus also restored this activity, providing additional evidence that myristylation inhibits transrepression by FBR protein. However, the myristylated Gag domain did not inhibit SRE transrepression when fused to Fos, indicating that myristylation of a fos protein is not by itself sufficient to prevent SRE transrepression and that C-terminal mutation is necessary to inhibit transrepression by N myristylation. Comparison of transfection results with Fos C-terminal deletion mutants and the Fos/FBR chimeric mutant revealed that the FBR C terminus retained the potential for transrepression despite deletion of the normal Fos C terminus, whereas similar Fos deletion mutants did not. These results indicate that both N- and C-terminal mutations are required to inhibit transrepression by FBR protein and that multiple structural mutations accompanied by posttranslational protein modification alter gene regulation by FBR protein.
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7

Kamata, N., and J. T. Holt. "Inhibitory effect of myristylation on transrepression by FBR (Gag-Fos) protein." Molecular and Cellular Biology 12, no. 2 (1992): 876–82. http://dx.doi.org/10.1128/mcb.12.2.876-882.1992.

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The myristylated v-fos product, FBR murine sarcoma virus (Gag-Fos) protein, exhibits a lower level of transrepression of the serum response element (SRE) than does c-fos protein (Fos). Mutation of the N-terminal myristylation site in FBR protein restored SRE transrepression. Replacement of N-terminal viral Gag sequences with the Fos N terminus also restored this activity, providing additional evidence that myristylation inhibits transrepression by FBR protein. However, the myristylated Gag domain did not inhibit SRE transrepression when fused to Fos, indicating that myristylation of a fos protein is not by itself sufficient to prevent SRE transrepression and that C-terminal mutation is necessary to inhibit transrepression by N myristylation. Comparison of transfection results with Fos C-terminal deletion mutants and the Fos/FBR chimeric mutant revealed that the FBR C terminus retained the potential for transrepression despite deletion of the normal Fos C terminus, whereas similar Fos deletion mutants did not. These results indicate that both N- and C-terminal mutations are required to inhibit transrepression by FBR protein and that multiple structural mutations accompanied by posttranslational protein modification alter gene regulation by FBR protein.
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8

Kamata, N., R. M. Jotte, and J. T. Holt. "Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein." Molecular and Cellular Biology 11, no. 2 (1991): 765–72. http://dx.doi.org/10.1128/mcb.11.2.765.

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FBR murine sarcoma virus (gag-fos) protein, a virally transduced Fos protein, exhibits decreased gene transactivation in comparison with the cellular Fos protein. Biochemical analysis suggests that myristylation of the virally encoded N-terminal gag region results in decreased DNA binding and transcriptional activation without affecting heterodimerization with Jun protein. These findings demonstrate that protein myristylation can modulate gene regulation by a DNA-binding protein.
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9

Kamata, N., R. M. Jotte, and J. T. Holt. "Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein." Molecular and Cellular Biology 11, no. 2 (1991): 765–72. http://dx.doi.org/10.1128/mcb.11.2.765-772.1991.

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FBR murine sarcoma virus (gag-fos) protein, a virally transduced Fos protein, exhibits decreased gene transactivation in comparison with the cellular Fos protein. Biochemical analysis suggests that myristylation of the virally encoded N-terminal gag region results in decreased DNA binding and transcriptional activation without affecting heterodimerization with Jun protein. These findings demonstrate that protein myristylation can modulate gene regulation by a DNA-binding protein.
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10

Loh, Ying-Tsu, Jianmin Zhou, and Gregory B. Martin. "The Myristylation Motif of Pto Is Not Required for Disease Resistance." Molecular Plant-Microbe Interactions® 11, no. 6 (1998): 572–76. http://dx.doi.org/10.1094/mpmi.1998.11.6.572.

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The tomato Pto kinase confers resistance to bacterial speck disease caused by strains of Pseudomonas syringae pv. tomato that express the avirulence gene avrPto. Pto contains a putative myristylation site at its amino terminus that was hypothesized to play a role in localizing Pto in the plant cell. Site-directed mutagenesis was used to change the invariant glycine residue in the myristylation motif to an alanine. Transgenes encoding the mutant Pto(G2A) and wild-type Pto were placed behind the cauliflower mosaic virus 35S promoter and transformed into tomato plants that are susceptible to bacterial speck disease. Both the mutant and wild-type forms of Pto conferred resistance to a strain of P. syringae pv. tomato expressing avrPto. These results indicate that the myristylation motif of Pto is not required for bacterial speck disease resistance.
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11

Kaplan, J. M., H. E. Varmus, and J. M. Bishop. "The src protein contains multiple domains for specific attachment to membranes." Molecular and Cellular Biology 10, no. 3 (1990): 1000–1009. http://dx.doi.org/10.1128/mcb.10.3.1000.

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The proteins encoded by the oncogene v-src and its cellular counterpart c-src (designated generically here as pp60src) are tightly associated with both plasma membranes and intracellular membranes. This association is due in part to the amino-terminal myristylation of pp60src, but several lines of evidence suggest that amino-terminal portions of the protein itself are also involved. We now report that pp60src contains at least three domains which, in conjunction with myristylation, are capable of mediating attachment to membranes and determining subcellular localization. We identified these domains by fusing various portions of pp60src to pyruvate kinase, which is normally a cytoplasmic protein. Amino acids 1 to 14 of pp60src are sufficient to mediate both myristylation and the attachment of pyruvate kinase to cytoplasmic granules. In contrast, amino acids 38 to 111 mediate association with the plasma membrane and perinuclear membranes, whereas amino acids 204 to 259 mediate association primarily with perinuclear membranes. We conclude that pp60src contains independent domains that target the protein to distinctive subcellular locations and thus may facilitate diverse biological functions of the protein.
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12

Kaplan, J. M., H. E. Varmus, and J. M. Bishop. "The src protein contains multiple domains for specific attachment to membranes." Molecular and Cellular Biology 10, no. 3 (1990): 1000–1009. http://dx.doi.org/10.1128/mcb.10.3.1000-1009.1990.

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The proteins encoded by the oncogene v-src and its cellular counterpart c-src (designated generically here as pp60src) are tightly associated with both plasma membranes and intracellular membranes. This association is due in part to the amino-terminal myristylation of pp60src, but several lines of evidence suggest that amino-terminal portions of the protein itself are also involved. We now report that pp60src contains at least three domains which, in conjunction with myristylation, are capable of mediating attachment to membranes and determining subcellular localization. We identified these domains by fusing various portions of pp60src to pyruvate kinase, which is normally a cytoplasmic protein. Amino acids 1 to 14 of pp60src are sufficient to mediate both myristylation and the attachment of pyruvate kinase to cytoplasmic granules. In contrast, amino acids 38 to 111 mediate association with the plasma membrane and perinuclear membranes, whereas amino acids 204 to 259 mediate association primarily with perinuclear membranes. We conclude that pp60src contains independent domains that target the protein to distinctive subcellular locations and thus may facilitate diverse biological functions of the protein.
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13

Buss, J. E., C. J. Der, and P. A. Solski. "The six amino-terminal amino acids of p60src are sufficient to cause myristylation of p21v-ras." Molecular and Cellular Biology 8, no. 9 (1988): 3960–63. http://dx.doi.org/10.1128/mcb.8.9.3960.

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We have used oligonucleotide-directed mutagenesis to replace the N-terminal amino acids of p21v-ras with residues which mimic the amino terminus of p60v-src. p21v-ras protein possessing only the first five amino acids of p60src was not myristylated, while substitution of residue 6 (serine) produced a protein p21(GSSKS) which incorporated [3H]myristic acid that was stable to hydroxylamine, sensitive to inhibitors of protein synthesis, and found in both the normally nonacylated precursor and mature forms of p21(GSSKS). This defines the minimum framework of the p60v-src myristylation signal (glycine 2 and serine 6) and identifies serine 6 as a crucial part of that signal for myristylation of a protein in vivo.
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14

Buss, J. E., C. J. Der, and P. A. Solski. "The six amino-terminal amino acids of p60src are sufficient to cause myristylation of p21v-ras." Molecular and Cellular Biology 8, no. 9 (1988): 3960–63. http://dx.doi.org/10.1128/mcb.8.9.3960-3963.1988.

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We have used oligonucleotide-directed mutagenesis to replace the N-terminal amino acids of p21v-ras with residues which mimic the amino terminus of p60v-src. p21v-ras protein possessing only the first five amino acids of p60src was not myristylated, while substitution of residue 6 (serine) produced a protein p21(GSSKS) which incorporated [3H]myristic acid that was stable to hydroxylamine, sensitive to inhibitors of protein synthesis, and found in both the normally nonacylated precursor and mature forms of p21(GSSKS). This defines the minimum framework of the p60v-src myristylation signal (glycine 2 and serine 6) and identifies serine 6 as a crucial part of that signal for myristylation of a protein in vivo.
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15

Bouamr, Fadila, Suzanne Scarlata, and Carol Carter. "Role of Myristylation in HIV-1 Gag Assembly†." Biochemistry 42, no. 21 (2003): 6408–17. http://dx.doi.org/10.1021/bi020692z.

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16

Silverman, L., and M. D. Resh. "Lysine residues form an integral component of a novel NH2-terminal membrane targeting motif for myristylated pp60v-src." Journal of Cell Biology 119, no. 2 (1992): 415–25. http://dx.doi.org/10.1083/jcb.119.2.415.

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Association of pp60v-src with the plasma membrane is fundamental to generation of the transformed phenotype. Although myristylation of pp60v-src is required for interaction with a membrane-bound receptor, the importance of NH2-terminal amino acids in receptor binding has not yet been uncoupled from their role in signaling myristylation. Using chimeric src proteins, peptides identical or related to the NH2 terminus of src, and site-directed mutagenesis, we demonstrate that NH2-terminal lysines in conjunction with myristate are essential for membrane localization. Subsequent to NH2-terminal interaction with the "src receptor," internal regions of the src protein also participate in membrane binding. This novel NH2-terminal motif and internal contact mechanism may direct other members of the src family of tyrosine kinases to their membrane receptors.
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17

Chen, Steve S. L. "Myristylation of the Envelope Glycoprotein of Vesicular Stomatitis Virus." Intervirology 32, no. 3 (1991): 193–97. http://dx.doi.org/10.1159/000150199.

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18

Jotte, R. M., and J. T. Holt. "Myristylation of FBR v-fos dictates the differentiation pathways in malignant osteosarcoma." Journal of Cell Biology 135, no. 2 (1996): 457–67. http://dx.doi.org/10.1083/jcb.135.2.457.

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Myristylation of FBR v-fos, a c-fos retroviral homologue that causes osteosarcomas in mice, determines many of its transcriptional properties in vitro. To determine whether myristylation of FBR v-fos contributes to in vivo tumorigenicity, we examined its transforming capability in comparison to a nonmyristylated FBR v-fos (G2A-R). Retroviral infections with FBR v-fos and G2A-R transform BALB/c-3T3 cells. The number, size, and cellular morphology of foci generated by both FBR and G2A-R are indistinguishable. However, marked biological differences were found in transgenic mice expressing either the myristylated FBR v-fos or the nonmyristylated G2A-R. 11 of 26 FBR v-fos transgenic mice died as a result of gross tumor burden. None of the 28 G2A-R transgenic mice died from tumor burden, and only two of the G2A-R mice developed bone tumors. Histologic examination of the tumors reveals that the FBR v-fos bone tumors contain malignant cells with features of four cell lineages (osteocytes, chondrocytes, myocytes, and adipocytes) in an environment rich in extracellular matrix (ECM). However, the G2A-R tumors exist in an environment devoid of ECM and display malignant cells with features of adipocytes. Masson staining reveals that the ECM of the FBR tumors stains strongly for collagen. Immunohistochemical staining with collagen III antibody demonstrates an abundance of collagen III expression in this ECM. While NH2-terminal myristylation is not required for FBR immortalization and transformation, it is essential in determining the degree of differentiation and tumorigenicity of malignant cells.
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19

Ono, Akira, and Eric O. Freed. "Binding of Human Immunodeficiency Virus Type 1 Gag to Membrane: Role of the Matrix Amino Terminus." Journal of Virology 73, no. 5 (1999): 4136–44. http://dx.doi.org/10.1128/jvi.73.5.4136-4144.1999.

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ABSTRACT Binding of the human immunodeficiency virus type 1 (HIV-1) Gag protein precursor, Pr55Gag, to membrane is an indispensable step in virus assembly. Previously, we reported that a matrix (MA) residue 6 substitution (6VR) imposed a virus assembly defect similar to that observed with myristylation-defective mutants, suggesting that the 6VR change impaired membrane binding. Intriguingly, the 6VR mutation had no effect on Gag myristylation. The defective phenotype imposed by 6VR was reversed by changes at other positions in MA, including residue 97. In this study, we use several biochemical methods to demonstrate that the residue 6 mutation, as well as additional substitutions in MA amino acids 7 and 8, reduce membrane binding without affecting N-terminal myristylation. This effect is observed in the context of Pr55Gag, a truncated Gag containing only MA and CA, and in MA itself. The membrane binding defect imposed by the 6VR mutation is reversed by second-site changes in MA residues 20 and 97, both of which, when present alone, increase membrane binding to levels greater than those for the wild type. Both reduced and enhanced membrane binding imposed by the MA substitutions depend upon the presence of the N-terminal myristate. The results support the myristyl switch model recently proposed for the regulation of Gag membrane binding, according to which membrane binding is determined by the degree of exposure or sequestration of the N-terminal myristate moiety. Alternatively, insertion of the myristate into the lipid bilayer might be a prerequisite event for the function of other distinct MA-encoded membrane binding domains.
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20

Kuroki, K., R. Russnak, and D. Ganem. "Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum." Molecular and Cellular Biology 9, no. 10 (1989): 4459–66. http://dx.doi.org/10.1128/mcb.9.10.4459.

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The preS1 surface glycoprotein of hepatitis B virus is targeted to the endoplasmic reticulum (ER) and is retained in this organelle when expressed in the absence of other viral gene products. The protein is also acylated at its N terminus with myristic acid. Sequences responsible for its ER retention have been identified through examination of mutants bearing lesions in the preS1 coding region. These studies reveal that such sequences map to the N terminus of the molecule, between residues 6 and 19. Molecules in which this region was present remained in the ER; those in which it had been deleted were secreted from the cell. Although all deletions which allowed efficient secretion also impaired acylation of the polypeptide, myristylation alone was not sufficient for ER retention: point mutations which eliminated myristylation did not lead to secretion. These data indicate that an essential element for ER retention resides in a 14-amino-acid sequence that is unrelated to previously described ER retention signals.
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21

Kuroki, K., R. Russnak, and D. Ganem. "Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum." Molecular and Cellular Biology 9, no. 10 (1989): 4459–66. http://dx.doi.org/10.1128/mcb.9.10.4459-4466.1989.

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The preS1 surface glycoprotein of hepatitis B virus is targeted to the endoplasmic reticulum (ER) and is retained in this organelle when expressed in the absence of other viral gene products. The protein is also acylated at its N terminus with myristic acid. Sequences responsible for its ER retention have been identified through examination of mutants bearing lesions in the preS1 coding region. These studies reveal that such sequences map to the N terminus of the molecule, between residues 6 and 19. Molecules in which this region was present remained in the ER; those in which it had been deleted were secreted from the cell. Although all deletions which allowed efficient secretion also impaired acylation of the polypeptide, myristylation alone was not sufficient for ER retention: point mutations which eliminated myristylation did not lead to secretion. These data indicate that an essential element for ER retention resides in a 14-amino-acid sequence that is unrelated to previously described ER retention signals.
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22

Chow, M., J. F. E. Newman, D. Filman, J. M. Hogle, D. J. Rowlands, and F. Brown. "Myristylation of picornavirus capsid protein VP4 and its structural significance." Nature 327, no. 6122 (1987): 482–86. http://dx.doi.org/10.1038/327482a0.

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23

De Falco, S., M. Ruvo, A. Verdoliva, et al. "N-terminal myristylation of HBV preS1 domain enhances receptor recognition." Journal of Peptide Research 57, no. 5 (2001): 390–400. http://dx.doi.org/10.1034/j.1399-3011.2001.00848.x.

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24

Niklinska, B. B., D. Hou, C. June, A. M. Weissman, and J. D. Ashwell. "CD45 tyrosine phosphatase activity and membrane anchoring are required for T-cell antigen receptor signaling." Molecular and Cellular Biology 14, no. 12 (1994): 8078–84. http://dx.doi.org/10.1128/mcb.14.12.8078.

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T cells that lack the CD45 transmembrane tyrosine phosphatase have a variety of T-cell receptor (TCR) signaling defects that are corrected by reexpression of wild-type CD45 or its intracytoplasmic domains. In this study, a chimeric molecule containing the myristylation sequence of Src and the intracellular portion of CD45, previously shown to restore function in CD45- T cells, was mutagenized to determine if membrane-associated CD45 tyrosine phosphatase activity is required to restore TCR-mediated signaling in CD45- T cells. Abolition of enzymatic activity by substitution of a serine for a critical cysteine in the first catalytic domain resulted in failure of this molecule to restore TCR signaling. Another mutation, in which a single amino acid substitution destroyed the myristylation site, resulted in failure of the chimeric molecule to partition to the plasma membrane. Although expressed at high levels and enzymatically active, this form of intracellular CD45 also failed to restore normal signaling in CD45- T cells. These findings strongly suggest that CD45's function in TCR signaling requires its proximity to membrane-associated tyrosine phosphatase substrates.
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Niklinska, B. B., D. Hou, C. June, A. M. Weissman, and J. D. Ashwell. "CD45 tyrosine phosphatase activity and membrane anchoring are required for T-cell antigen receptor signaling." Molecular and Cellular Biology 14, no. 12 (1994): 8078–84. http://dx.doi.org/10.1128/mcb.14.12.8078-8084.1994.

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T cells that lack the CD45 transmembrane tyrosine phosphatase have a variety of T-cell receptor (TCR) signaling defects that are corrected by reexpression of wild-type CD45 or its intracytoplasmic domains. In this study, a chimeric molecule containing the myristylation sequence of Src and the intracellular portion of CD45, previously shown to restore function in CD45- T cells, was mutagenized to determine if membrane-associated CD45 tyrosine phosphatase activity is required to restore TCR-mediated signaling in CD45- T cells. Abolition of enzymatic activity by substitution of a serine for a critical cysteine in the first catalytic domain resulted in failure of this molecule to restore TCR signaling. Another mutation, in which a single amino acid substitution destroyed the myristylation site, resulted in failure of the chimeric molecule to partition to the plasma membrane. Although expressed at high levels and enzymatically active, this form of intracellular CD45 also failed to restore normal signaling in CD45- T cells. These findings strongly suggest that CD45's function in TCR signaling requires its proximity to membrane-associated tyrosine phosphatase substrates.
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26

Gervais, F. G., and A. Veillette. "The unique amino-terminal domain of p56lck regulates interactions with tyrosine protein phosphatases in T lymphocytes." Molecular and Cellular Biology 15, no. 5 (1995): 2393–401. http://dx.doi.org/10.1128/mcb.15.5.2393.

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The catalytic activity of p56lck is repressed by phosphorylation of a conserved carboxy-terminal tyrosine residue (tyrosine 505). Accumulating data show that this phosphorylation is mediated by the tyrosine protein kinase p50csk and that it is reversed by the transmembrane tyrosine protein phosphatase CD45. Recent studies have indicated that dephosphorylation of tyrosine 505 in resting T cells is necessary for the initiation of antigen-induced T-cell activation. To better understand this phenomenon, we have characterized the factors regulating tyrosine 505 phosphorylation in an antigen-specific T-cell line (BI-141). As is the case for other T-cell lines, Lck molecules from unstimulated BI-141 cells exhibited a pronounced dephosphorylation of the inhibitory carboxyl-terminal tyrosine. This state could be corrected by incubation of cells with the tyrosine protein phosphatase inhibitor pervanadate, suggesting that it reflected the unrestricted action of tyrosine protein phosphatases. In structure-function analyses, mutation of the site of Lck myristylation (glycine 2) partially restored phosphorylation at tyrosine 505 in BI-141 cells. Since the myristylation-defective mutant also failed to stably associate with cellular membranes, this effect was most probably the consequence of removal of p56lck from the vicinity of membrane phosphatases like CD45. Deletion of the unique domain of Lck, or its replacement by the equivalent sequence from p59fyn, also increased the extent of tyrosine 505 phosphorylation in vivo. This effect was unrelated to changes in Lck membrane association and therefore was potentially related to defects in crucial protein-protein interactions at the membrane. In contrast, deletion of the SH3 or SH2 domain, or mutation of the phosphotransfer motif (lysine 273) or the site of autophosphorylation (tyrosine 394), had no impact on phosphate occupancy at tyrosine 505. In combination, these results indicated that the hypophosphorylation of the inhibitory tyrosine of p56(lck) in T lymphocytes is likely the result of the predominant action of tyrosine protein phosphatases. Moreover, they showed that both the amino-terminal myristylation signal and the unique domain of p56(lck) play critical roles in this process.
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27

Paillart, Jean-Christophe, and Heinrich G. Göttlinger. "Opposing Effects of Human Immunodeficiency Virus Type 1 Matrix Mutations Support a Myristyl Switch Model of Gag Membrane Targeting." Journal of Virology 73, no. 4 (1999): 2604–12. http://dx.doi.org/10.1128/jvi.73.4.2604-2612.1999.

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ABSTRACT Targeting of the human immunodeficiency virus type 1 (HIV-1) Gag precursor Pr55 gag to the plasma membrane, the site of virus assembly, is primarily mediated by the N-terminal matrix (MA) domain. N-myristylation of MA is essential for the stable association of Pr55 gag with membranes and for virus assembly. We now show that single amino acid substitutions near the N terminus of MA can dramatically impair assembly without compromising myristylation. Subcellular fractionation demonstrated that Gag membrane binding was compromised to a similar extent as in the absence of the myristyl acceptor site, indicating that the myristyl group was not available for membrane insertion. Remarkably, the effects of the N-terminal modifications could be completely suppressed by second-site mutations in the globular core of MA. The compensatory mutations enhanced Gag membrane binding and increased viral particle yields above wild-type levels, consistent with an increase in the exposure of the myristyl group. Our results support a model in which the compact globular core of MA sequesters the myristyl group to prevent aberrant binding to intracellular membranes, while the N terminus is critical to allow the controlled exposure of the myristyl group for insertion into the plasma membrane.
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28

Alland, L., S. M. Peseckis, R. E. Atherton, L. Berthiaume, and M. D. Resh. "Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization." Journal of Biological Chemistry 269, no. 24 (1994): 16701–5. http://dx.doi.org/10.1016/s0021-9258(19)89447-4.

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29

Zhang, Ping, Feng Ye, Adam C. Bastidas, et al. "An Isoform-Specific Myristylation Switch Targets Type II PKA Holoenzymes to Membranes." Structure 23, no. 9 (2015): 1563–72. http://dx.doi.org/10.1016/j.str.2015.07.007.

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30

Prange, R., A. Clemen, and R. E. Streeck. "Myristylation is involved in intracellular retention of hepatitis B virus envelope proteins." Journal of Virology 65, no. 7 (1991): 3919–23. http://dx.doi.org/10.1128/jvi.65.7.3919-3923.1991.

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31

Schultz, A., L. Henderson, S. Oroszlan, E. Garber, and H. Hanafusa. "Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein." Science 227, no. 4685 (1985): 427–29. http://dx.doi.org/10.1126/science.3917576.

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32

Risinger, Mary A., Catherine Korsgren, and Carl M. Cohen. "Role ofN-Myristylation in Targeting of Band 4.2 (Pallidin) in Nonerythroid Cells." Experimental Cell Research 229, no. 2 (1996): 421–31. http://dx.doi.org/10.1006/excr.1996.0387.

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33

Deichaite, I., L. P. Casson, H. P. Ling, and M. D. Resh. "In vitro synthesis of pp60v-src: myristylation in a cell-free system." Molecular and Cellular Biology 8, no. 10 (1988): 4295–301. http://dx.doi.org/10.1128/mcb.8.10.4295.

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Covalent attachment of myristic acid to pp60v-src, the transforming protein of Rous sarcoma virus, was studied in a cell-free system. Using a synthetic peptide containing the first 11 amino acids of the mature pp60v-src polypeptide sequence as a substrate, we probed lysates from a variety of cells and tissues for N-myristyl transferase (NMT) activity. Nearly every eucaryotic cell type tested contained NMT, including avian, mammalian, insect, and plant cells. Since NMT activity was detected in rabbit reticulocyte lysates, we took advantage of the translational capability of these lysates to determine the precise point during translation at which myristate is attached to pp60v-src. src mRNA, transcribed from cloned v-src DNA, was translated in reticulocyte lysates which had been depleted of endogenous myristate. Addition of [3H]myristate to lysates 10 min after the start of synchronized translation resulted in a dramatic decrease in the incorporation of radiolabeled myristate into pp60v-src polypeptide chains. These results imply that although myristate can be attached posttranslationally to synthetic peptide substrates, myristylation in vivo is apparently a very early cotranslational event which occurs before the first 100 amino acids of the nascent polypeptide chain are polymerized.
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34

da Silva, A. M., and C. Klein. "A rapid posttranslational myristylation of a 68-kD protein in D. discoideum." Journal of Cell Biology 111, no. 2 (1990): 401–7. http://dx.doi.org/10.1083/jcb.111.2.401.

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Cells incubated with [3H]myristate were shown to rapidly and specifically acylate a 68-kD protein, p68, in a developmentally-regulated manner. The fatty acid incorporated into p68 was identified as myristate, and is linked to the protein via an amide bond, apparently to an NH2-terminal glycine. The acylation of p68 in D. discoideum displays some unusual properties. Unexpectedly, myristylation of p68 is a posttranslational event and occurs in the presence of inhibitors of protein synthesis. Another unusual finding was that although p68 is a stable protein, the acyl moiety is removed with a half time of approximately 15 min.
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35

Resh, Marilyn D. "Myristylation and palmitylation of Src family members: The fats of the matter." Cell 76, no. 3 (1994): 411–13. http://dx.doi.org/10.1016/0092-8674(94)90104-x.

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36

Jotte, R. M., N. Kamata, and J. T. Holt. "Myristylation-dependent transactivation by FBR v-fos is regulated by C/EBP." Journal of Biological Chemistry 269, no. 23 (1994): 16383–96. http://dx.doi.org/10.1016/s0021-9258(17)34019-x.

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37

Deichaite, I., L. P. Casson, H. P. Ling, and M. D. Resh. "In vitro synthesis of pp60v-src: myristylation in a cell-free system." Molecular and Cellular Biology 8, no. 10 (1988): 4295–301. http://dx.doi.org/10.1128/mcb.8.10.4295-4301.1988.

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Covalent attachment of myristic acid to pp60v-src, the transforming protein of Rous sarcoma virus, was studied in a cell-free system. Using a synthetic peptide containing the first 11 amino acids of the mature pp60v-src polypeptide sequence as a substrate, we probed lysates from a variety of cells and tissues for N-myristyl transferase (NMT) activity. Nearly every eucaryotic cell type tested contained NMT, including avian, mammalian, insect, and plant cells. Since NMT activity was detected in rabbit reticulocyte lysates, we took advantage of the translational capability of these lysates to determine the precise point during translation at which myristate is attached to pp60v-src. src mRNA, transcribed from cloned v-src DNA, was translated in reticulocyte lysates which had been depleted of endogenous myristate. Addition of [3H]myristate to lysates 10 min after the start of synchronized translation resulted in a dramatic decrease in the incorporation of radiolabeled myristate into pp60v-src polypeptide chains. These results imply that although myristate can be attached posttranslationally to synthetic peptide substrates, myristylation in vivo is apparently a very early cotranslational event which occurs before the first 100 amino acids of the nascent polypeptide chain are polymerized.
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38

Andrawiss, Mariam, Yasuhiro Takeuchi, Lindsay Hewlett, and Mary Collins. "Murine Leukemia Virus Particle Assembly Quantitated by Fluorescence Microscopy: Role of Gag-Gag Interactions and Membrane Association." Journal of Virology 77, no. 21 (2003): 11651–60. http://dx.doi.org/10.1128/jvi.77.21.11651-11660.2003.

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ABSTRACT In order to track the assembly of murine leukemia virus (MLV), we used fluorescence microscopy to visualize particles containing Gag molecules fused to fluorescent proteins (FPs). Gag-FP chimeras budded from cells to produce fluorescent spots, which passed through the same pore-size filters and sedimented at the same velocity as authentic MLV. N-terminal myristylation of Gag-FPs was necessary for particle formation unless wild-type Gag was coexpressed. By labeling nonmyristylated Gag with yellow FP and wild-type Gag with cyan FP, we could quantitate the coincorporation of two proteins into single particles. This experiment showed that nonmyristylated Gag was incorporated into mixed particles at approximately 50% the efficiency of wild-type Gag. Mutations that inhibit Gag-Gag interactions (K. Alin and S. P. Goff, Virology 216:418-424, 1996; K. Alin and S. P. Goff, Virology 222:339-351, 1996) were then introduced into the capsid (CA) region of Gag-FPs. The mutations P150L and R119C/P133L inhibited fluorescent particle formation by these Gag-FPs, but Gag-FPs containing these mutations could be efficiently incorporated into particles when coexpressed with wild-type Gag. When these mutations were introduced into nonmyristylated Gag-FPs, no incorporation into particles in the presence of wild-type Gag was detected. These data suggest that two independent mechanisms, CA interactions and membrane association following myristylation, cooperate in MLV Gag assembly and budding.
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39

Abraham, N., and A. Veillette. "Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation." Molecular and Cellular Biology 10, no. 10 (1990): 5197–206. http://dx.doi.org/10.1128/mcb.10.10.5197.

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Mutation of the major site of in vivo tyrosine phosphorylation of p56lck (tyrosine 505) to a phenylalanine constitutively enhances the p56lck-associated tyrosine-specific protein kinase activity. The mutant polypeptide is extensively phosphorylated in vivo at the site of in vitro Lck autophosphorylation (tyrosine 394) and is capable of oncogenic transformation of rodent fibroblasts. These observations have suggested that phosphorylation at Tyr-505 down regulates the tyrosine protein kinase activity of p56lck. Herein we have attempted to examine whether other posttranslational modifications may be involved in regulation of the enzymatic function of p56lck. The results indicated that activation of p56lck by mutation of Tyr-505 was prevented by a tyrosine-to-phenylalanine substitution at position 394. Furthermore, activation of p56lck by mutation of the carboxy-terminal tyrosine residue was rendered less efficient by substituting an alanine residue for the amino-terminal glycine. This second mutation prevented p56lck myristylation and stable membrane association and was associated with decreased in vivo phosphorylation at Tyr-394. Taken together, these findings imply that lack of phosphorylation at Tyr-505 may be insufficient for enhancement of the p56lck-associated tyrosine protein kinase activity. Our data suggest that activation of p56lck may be dependent on phosphorylation at Tyr-394 and that this process may be facilitated by myristylation, membrane association, or both.
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40

Sada, Kiyonao, Juan Zhang та Reuben P. Siraganian. "SH2 domain–mediated targeting, but not localization, of Syk in the plasma membrane is critical for FcεRI signaling". Blood 97, № 5 (2001): 1352–59. http://dx.doi.org/10.1182/blood.v97.5.1352.

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Aggregation of the high-affinity IgE receptor induces the tyrosine phosphorylation of subunits of the receptor and the subsequent association with the receptor of the cytosolic protein tyrosine kinase Syk. The current experiments examined the functional importance of membrane association of Syk and the role of the SH2 domain in receptor-mediated signal transduction. Wild-type Syk and chimeric Syk molecules with the c-Src myristylation sequence at the amino-terminus were expressed in a Syk-negative mast cell line. Chimeric Syk with the myristylation sequence was membrane associated, and a small fraction was constitutively colocalized with FcεRI, Lyn, and LAT (linker for T-cell activation) in the glycolipid-enriched microdomains or rafts. However, even under these conditions, the tyrosine phosphorylation of Syk and the downstream propagation of signals required FcεRI aggregation. This chimeric Syk was less active than wild-type Syk in FcεRI-mediated signal transduction. In contrast, a truncated membrane-associated form of Syk that lacked the SH2 domains was not tyrosine phosphorylated by receptor aggregation and failed to transduce intracellular signals. These findings suggest that SH2 domain–mediated membrane translocation of Syk is essential for the FcεRI-mediated activation of Syk for downstream signaling events leading to histamine release. Furthermore, the localization of Syk in glycolipid-enriched microdomains by itself is not enough to generate or enhance signaling events.
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41

Abraham, N., and A. Veillette. "Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation." Molecular and Cellular Biology 10, no. 10 (1990): 5197–206. http://dx.doi.org/10.1128/mcb.10.10.5197-5206.1990.

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Abstract:
Mutation of the major site of in vivo tyrosine phosphorylation of p56lck (tyrosine 505) to a phenylalanine constitutively enhances the p56lck-associated tyrosine-specific protein kinase activity. The mutant polypeptide is extensively phosphorylated in vivo at the site of in vitro Lck autophosphorylation (tyrosine 394) and is capable of oncogenic transformation of rodent fibroblasts. These observations have suggested that phosphorylation at Tyr-505 down regulates the tyrosine protein kinase activity of p56lck. Herein we have attempted to examine whether other posttranslational modifications may be involved in regulation of the enzymatic function of p56lck. The results indicated that activation of p56lck by mutation of Tyr-505 was prevented by a tyrosine-to-phenylalanine substitution at position 394. Furthermore, activation of p56lck by mutation of the carboxy-terminal tyrosine residue was rendered less efficient by substituting an alanine residue for the amino-terminal glycine. This second mutation prevented p56lck myristylation and stable membrane association and was associated with decreased in vivo phosphorylation at Tyr-394. Taken together, these findings imply that lack of phosphorylation at Tyr-505 may be insufficient for enhancement of the p56lck-associated tyrosine protein kinase activity. Our data suggest that activation of p56lck may be dependent on phosphorylation at Tyr-394 and that this process may be facilitated by myristylation, membrane association, or both.
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42

Baird, Nicholas L., Jason L. Starkey, David J. Hughes, and John W. Wills. "Myristylation and palmitylation of HSV-1 UL11 are not essential for its function." Virology 397, no. 1 (2010): 80–88. http://dx.doi.org/10.1016/j.virol.2009.10.046.

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43

Ansardi, D. C., D. C. Porter, and C. D. Morrow. "Myristylation of poliovirus capsid precursor P1 is required for assembly of subviral particles." Journal of Virology 66, no. 7 (1992): 4556–63. http://dx.doi.org/10.1128/jvi.66.7.4556-4563.1992.

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44

BRUSS, VOLKER, JENS HAGELSTEIN, ELLEN GERHARDT, and PETER R. GALLE. "Myristylation of the Large Surface Protein Is Required for Hepatitis B Virusin VitroInfectivity." Virology 218, no. 2 (1996): 396–99. http://dx.doi.org/10.1006/viro.1996.0209.

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45

Que, Quideng, Yu Li, Ing-Nang Wang, Leslie C. Lane, William G. Chaney, and James L. Van Etten. "Protein Glycosylation and Myristylation in Chlorella Virus PBCV-1 and Its Antigenic Variants." Virology 203, no. 2 (1994): 320–27. http://dx.doi.org/10.1006/viro.1994.1490.

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46

Johnson, Marc C., Heather M. Scobie, and Volker M. Vogt. "PR Domain of Rous Sarcoma Virus Gag Causes an Assembly/Budding Defect in Insect Cells." Journal of Virology 75, no. 9 (2001): 4407–12. http://dx.doi.org/10.1128/jvi.75.9.4407-4412.2001.

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ABSTRACT While baculovirus expression of Gag proteins from numerous retroviruses has led reliably to production of virus-like particles (VLPs), we observed that expression of Rous sarcoma virus Gag failed to produce VLPs. Transmission and scanning electron microscopy analysis revealed that the Gag protein reached the plasma membrane but was unable to correctly form particles. Addition of a myristylation signal had no effect on the budding defect, but deletion of the PR domain of Gag restored normal budding. The resulting VLPs were morphologically distinct from human immunodeficiency virus type 1 VLPs expressed in parallel.
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47

Rudner, Lynnie, Sascha Nydegger, Lori V. Coren, Kunio Nagashima, Markus Thali, and David E. Ott. "Dynamic Fluorescent Imaging of Human Immunodeficiency Virus Type 1 Gag in Live Cells by Biarsenical Labeling." Journal of Virology 79, no. 7 (2005): 4055–65. http://dx.doi.org/10.1128/jvi.79.7.4055-4065.2005.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) Gag is the primary structural protein of the virus and is sufficient for particle formation. We utilized the recently developed biarsenical-labeling method to dynamically observe HIV-1 Gag within live cells by adding a tetracysteine tag (C-C-P-G-C-C) to the C terminus of Gag in both Pr55Gag expression and full-length proviral constructs. Membrane-permeable biarsenical compounds FlAsH and ReAsH covalently bond to this tetracysteine sequence and specifically fluoresce, effectively labeling Gag in the cell. Biarsenical labeling readily and specifically detected a tetracysteine-tagged HIV-1 Gag protein (Gag-TC) in HeLa, Mel JuSo, and Jurkat T cells by deconvolution fluorescence microscopy. Gag-TC was localized primarily at or near the plasma membrane in all cell types examined. Fluorescent two-color analysis of Gag-TC in HeLa cells revealed that nascent Gag was present mostly at the plasma membrane in distinct regions. Intracellular imaging of a Gag-TC myristylation mutant observed a diffuse signal throughout the cell, consistent with the role of myristylation in Gag localization to the plasma membrane. In contrast, mutation of the L-domain core sequence did not appreciably alter the localization of Gag, suggesting that the PTAP L domain functions at the site of budding rather than as a targeting signal. Taken together, our results show that Gag concentrates in specific plasma membrane areas rapidly after translation and demonstrate the utility of biarsenical labeling for visualizing the dynamic localization of Gag.
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48

Rohrschneider, L., and S. Reynolds. "Regulation of cellular morphology by the Rous sarcoma virus src gene: analysis of fusiform mutants." Molecular and Cellular Biology 5, no. 11 (1985): 3097–107. http://dx.doi.org/10.1128/mcb.5.11.3097.

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We have been interested in how Rous sarcoma virus (RSV) influences transformed cell morphology and compared the molecular properties of chicken embryo cells (CEC) infected with mutants of RSV that induce the fusiform transformed cell morphology with those of CEC infected by wild-type RSV, which induces the more normal round transformed cell morphology. We looked for properties shared by all fusiform mutant-infected cells, because these may be responsible for maintaining the fusiform morphology. Five different fusiform mutants, two wild-type RSVs, and one wild-type back revertant of a fusiform mutant were studied. In the fusiform mutant-infected cells, the localization and myristylation of pp60src were determined and the extent of expression of the extracellular matrix protein fibronectin was examined at both the mRNA and protein levels. The phosphorylation of vinculin on tyrosine also was examined in the same CEC. Within all fusiform mutant-transformed CEC, pp60src was dramatically absent from the adhesion plaque sites normally seen in cells transformed with wild-type RSV, and these transformed CEC all expressed more fibronectin mRNA and protein in the extracellular matrix than did the wild-type RSV-transformed CEC. The absence of pp60src from the adhesion plaques was not due to lack of myristylation of the src protein, and tyrosine phosphorylation of vinculin was not related to fibronectin expression. These results suggest that the inverse relationship between pp60src in the adhesion plaques and fibronectin expression in the extracellular matrix may be interconnected phenomena and could be related to the maintenance of the fusiform transformed morphology.
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49

Rohrschneider, L., and S. Reynolds. "Regulation of cellular morphology by the Rous sarcoma virus src gene: analysis of fusiform mutants." Molecular and Cellular Biology 5, no. 11 (1985): 3097–107. http://dx.doi.org/10.1128/mcb.5.11.3097-3107.1985.

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We have been interested in how Rous sarcoma virus (RSV) influences transformed cell morphology and compared the molecular properties of chicken embryo cells (CEC) infected with mutants of RSV that induce the fusiform transformed cell morphology with those of CEC infected by wild-type RSV, which induces the more normal round transformed cell morphology. We looked for properties shared by all fusiform mutant-infected cells, because these may be responsible for maintaining the fusiform morphology. Five different fusiform mutants, two wild-type RSVs, and one wild-type back revertant of a fusiform mutant were studied. In the fusiform mutant-infected cells, the localization and myristylation of pp60src were determined and the extent of expression of the extracellular matrix protein fibronectin was examined at both the mRNA and protein levels. The phosphorylation of vinculin on tyrosine also was examined in the same CEC. Within all fusiform mutant-transformed CEC, pp60src was dramatically absent from the adhesion plaque sites normally seen in cells transformed with wild-type RSV, and these transformed CEC all expressed more fibronectin mRNA and protein in the extracellular matrix than did the wild-type RSV-transformed CEC. The absence of pp60src from the adhesion plaques was not due to lack of myristylation of the src protein, and tyrosine phosphorylation of vinculin was not related to fibronectin expression. These results suggest that the inverse relationship between pp60src in the adhesion plaques and fibronectin expression in the extracellular matrix may be interconnected phenomena and could be related to the maintenance of the fusiform transformed morphology.
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50

Gasparovic, M. L., G. V. Gee, and W. J. Atwood. "JC Virus Minor Capsid Proteins Vp2 and Vp3 Are Essential for Virus Propagation." Journal of Virology 80, no. 21 (2006): 10858–61. http://dx.doi.org/10.1128/jvi.01298-06.

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ABSTRACT Virus-encoded capsid proteins play a major role in the life cycles of all viruses. The JC virus capsid is composed of 72 pentamers of the major capsid protein Vp1, with one of the minor coat proteins Vp2 or Vp3 in the center of each pentamer. Vp3 is identical to two-thirds of Vp2, and these proteins share a DNA binding domain, a nuclear localization signal, and a Vp1-interacting domain. We demonstrate here that both the minor proteins and the myristylation site on Vp2 are essential for the viral life cycle, including the proper packaging of its genome.
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