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Articoli di riviste sul tema "Tyrosine"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 25 luglio 2025

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1

Hunter, Tony. "THE CROONIAN LECTURE 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 353, no. 1368 (1998): 583–605. http://dx.doi.org/10.1098/rstb.1998.0228.

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The reversible phosphorylation of tyrosines in proteins plays a key role in regulating many different processes in eukaryotic organisms, such as growth control, cell cycle control, differentiation, cell shape and movement, gene transcription, synaptic transmission, and insulin action. Phosphorylation of proteins is brought about by enzymes called protein–tyrosine kinases that add phosphate to specific tyrosines in target proteins; phosphate is removed from phosphorylated tyrosines by enzymes called protein–tyrosine phosphatases. Phosphorylated tyrosines are recognized by specialized binding do

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2

Longmore, Gregory D., Yun You, Jaime Molden, et al. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo." Blood 91, no. 3 (1998): 870–78. http://dx.doi.org/10.1182/blood.v91.3.870.

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Abstract Cytokine receptors have been shown in cell culture systems to use phosphotyrosine residues as docking sites for certain signal transduction intermediates. Studies using various cellular backgrounds have yielded conflicting information about the importance of such residues. The present studies were undertaken to determine whether or not tyrosine residues within the erythropoietin receptor (EPOR) are essential for biologic activity during hematopoiesis in vivo. A variant of the EPOR was constructed that contains both a substitution (R129C) causing constitutive receptor activation as wel

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3

Longmore, Gregory D., Yun You, Jaime Molden, et al. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo." Blood 91, no. 3 (1998): 870–78. http://dx.doi.org/10.1182/blood.v91.3.870.870_870_878.

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Cytokine receptors have been shown in cell culture systems to use phosphotyrosine residues as docking sites for certain signal transduction intermediates. Studies using various cellular backgrounds have yielded conflicting information about the importance of such residues. The present studies were undertaken to determine whether or not tyrosine residues within the erythropoietin receptor (EPOR) are essential for biologic activity during hematopoiesis in vivo. A variant of the EPOR was constructed that contains both a substitution (R129C) causing constitutive receptor activation as well as repl

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4

Hansen, J. A., L. H. Hansen, X. Wang, et al. "The role of GH receptor tyrosine phosphorylation in Stat5 activation." Journal of Molecular Endocrinology 18, no. 3 (1997): 213–21. http://dx.doi.org/10.1677/jme.0.0180213.

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ABSTRACT Stimulation of GH receptors leads to rapid activation of Jak2 kinase and subsequent tyrosine phosphorylation of the GH receptor. Three specific tyrosines located in the C-terminal domain of the GH receptor have been identified as being involved in GH-stimulated transcription of the Spi 2·1 promoter. Mutated GH receptors lacking all but one of these three tyrosines are able to mediate a transcriptional response when transiently transfected into CHO cells together with a Spi 2·1 promoter/luciferase construct. Similarly, these GH receptors were found to be able to mediate activation of S

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5

King, M. J., and G. J. Sale. "Dephosphorylation of insulin-receptor autophosphorylation sites by particulate and soluble phosphotyrosyl-protein phosphatases." Biochemical Journal 266, no. 1 (1990): 251–59. http://dx.doi.org/10.1042/bj2660251.

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Insulin stimulates autophosphorylation of the insulin receptor on multiple tyrosines in three domains: tyrosines 1316 and 1322 in the C-terminal tail, 1146, 1150 and 1151 in the tyrosine-1150 domain, and possibly 953, 960 or 972 in the juxtamembrane domain. In the present work the sequence of dephosphorylation of the various autophosphorylation sites by particulate and cytosolic preparations of phosphotyrosyl-protein phosphatase from rat liver was studied with autophosphorylated human placental insulin receptor as substrate. Both phosphatase preparations elicited a broadly similar pattern of d

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6

Pao, Lily I., Sara J. Famiglietti, and John C. Cambier. "Asymmetrical Phosphorylation and Function of Immunoreceptor Tyrosine-Based Activation Motif Tyrosines in B Cell Antigen Receptor Signal Transduction." Journal of Immunology 160, no. 7 (1998): 3305–14. http://dx.doi.org/10.4049/jimmunol.160.7.3305.

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Abstract CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). ITAMs contain two conserved tyrosines that may become phosphorylated upon receptor aggregation and bind distinct effectors by virtue of the distinct preference of phosphotyrosyl-containing sequences for SH2 domains. To explore the function of CD79a and CD79b ITAM tyrosines, we created membrane molecules composed of MHC class II I-Ak extracellular and transmembrane domains, and CD79a or CD79b cytoplasmic domains in whic

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7

Argetsinger, Lawrence S., Jean-Louis K. Kouadio, Hanno Steen, Allan Stensballe, Ole N. Jensen, and Christin Carter-Su. "Autophosphorylation of JAK2 on Tyrosines 221 and 570 Regulates Its Activity." Molecular and Cellular Biology 24, no. 11 (2004): 4955–67. http://dx.doi.org/10.1128/mcb.24.11.4955-4967.2004.

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ABSTRACT The tyrosine kinase JAK2 is a key signaling protein for at least 20 receptors in the cytokine/hematopoietin receptor superfamily and is a component of signaling by insulin receptor and several G-protein-coupled receptors. However, there is only limited knowledge of the physical structure of JAK2 or which of the 49 tyrosines in JAK2 are autophosphorylated. In this study, mass spectrometry and two-dimensional peptide mapping were used to determine that tyrosines 221, 570, and 1007 in JAK2 are autophosphorylated. Phosphorylation of tyrosine 570 is particularly robust. In response to grow

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8

GIBSON, Spencer, Ken TRUITT, Yiling LU, et al. "Efficient CD28 signalling leads to increases in the kinase activities of the TEC family tyrosine kinase EMT/ITK/TSK and the SRC family tyrosine kinase LCK." Biochemical Journal 330, no. 3 (1998): 1123–28. http://dx.doi.org/10.1042/bj3301123.

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Optimal T cell activation requires crosslinking of the T cell receptor (TCR) concurrently with an accessory receptor, most efficiently CD28. Crosslinking of CD28 leads to increased interleukin 2 (IL2) production, inhibition of anergy and prevention of programmed cell death. Crosslinking of CD28 leads to rapid increases in tyrosine phosphorylation of specific intracellular substrates including CD28 itself. Since CD28 does not encode an intrinsic tyrosine kinase domain, CD28 must activate an intracellular tyrosine kinase(s). Indeed, crosslinking of CD28 increases the activity of the intracellula

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9

Zhang, Juan, Teruaki Kimura, and Reuben P. Siraganian. "Mutations in the Activation Loop Tyrosines of Protein Tyrosine Kinase Syk Abrogate Intracellular Signaling But Not Kinase Activity." Journal of Immunology 161, no. 8 (1998): 4366–74. http://dx.doi.org/10.4049/jimmunol.161.8.4366.

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Abstract The protein tyrosine kinase Syk plays a pivotal role in mediating the high-affinity IgE receptor (FcεRI)-induced degranulation of mast cells. To examine the mechanism of Syk regulation, the two tyrosine residues at 519 and 520 in the putative activation loop of rat Syk were mutated to phenylalanine either singly or in combination. The various mutants were expressed in a Syk-negative variant of the RBL-2H3 (rat basophilic leukemia 2H3) mast cell line. In these transfected cell lines, mutant Syk did show increased tyrosine phosphorylation in vivo and increased enzymatic activity in vitr

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10

King, P. D., A. Sadra, J. M. Teng, et al. "Analysis of CD28 cytoplasmic tail tyrosine residues as regulators and substrates for the protein tyrosine kinases, EMT and LCK." Journal of Immunology 158, no. 2 (1997): 580–90. http://dx.doi.org/10.4049/jimmunol.158.2.580.

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Abstract The CD28 cell surface receptor provides an important costimulatory signal for T cells necessary for their response to Ag. Early events in CD28 signaling include recruitment and activation of phosphatidylinositol 3-kinase (PI3-kinase) and activation of the protein tyrosine kinases (PTKs), LCK and EMT. Recruitment and activation of PI3-kinase is known to be dependent upon phosphorylation of tyrosine 173 of the CD28 cytoplasmic tail contained within a YMNM motif. By contrast, little is known of which residues of the CD28 tail, including tyrosines, are required for the activation of PTKs.

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11

de Castro, Rodrigo Orlandini. "Regulation and Function of Syk Tyrosine Kinase in Mast Cell Signaling and Beyond." Journal of Signal Transduction 2011 (May 12, 2011): 1–9. http://dx.doi.org/10.1155/2011/507291.

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The protein tyrosine kinase Syk plays a critical role in FcεRI signaling in mast cells. Binding of Syk to phosphorylated immunoreceptor tyrosine-based activation motifs (p-ITAM) of the receptor subunits results in conformational changes and tyrosine phosphorylation at multiple sites that leads to activation of Syk. The phosphorylated tyrosines throughout the molecule play an important role in the regulation of Syk-mediated signaling. Reconstitution of receptor-mediated signaling in Syk-/- cells by wild-type Syk or mutants which have substitution of these tyrosines with phenylalanine together w

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12

Marumo, K., and J. H. Waite. "Optimization of hydroxylation of tyrosine and tyrosine-containing peptides by mushroom tyrosinase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 872, no. 1-2 (1986): 98–103. http://dx.doi.org/10.1016/0167-4838(86)90152-4.

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13

Xia, Kai, Robert S. Lee, Radha P. Narsimhan, Nishit K. Mukhopadhyay, Benjamin G. Neel, and Thomas M. Roberts. "Tyrosine Phosphorylation of the Proto-Oncoprotein Raf-1 Is Regulated by Raf-1 Itself and the Phosphatase Cdc25A." Molecular and Cellular Biology 19, no. 7 (1999): 4819–24. http://dx.doi.org/10.1128/mcb.19.7.4819.

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ABSTRACT There is a growing body of evidence demonstrating that Raf-1 is phosphorylated on tyrosines upon stimulation of a variety of receptors. Although detection of Raf-1 tyrosine phosphorylation has remained elusive, genetic analyses have demonstrated it to be important for Raf-1 activation. Here we report new findings which indicate that Raf-1 tyrosine phosphorylation is regulated in vivo. In both a mammalian and baculovirus expression system, a kinase-inactive allele of Raf-1 was found to be tyrosine phosphorylated at levels much greater than that of wild-type Raf-1. The level of tyrosine

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14

Head, Julie A., Dongyan Jiang, Min Li, et al. "Cortactin Tyrosine Phosphorylation Requires Rac1 Activity and Association with the Cortical Actin Cytoskeleton." Molecular Biology of the Cell 14, no. 8 (2003): 3216–29. http://dx.doi.org/10.1091/mbc.e02-11-0753.

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Cortactin is an F-actin binding protein that activates actin-related protein 2/3 complex and is localized within lamellipodia. Cortactin is a substrate for Src and other protein tyrosine kinases involved in cell motility, where its phosphorylation on tyrosines 421, 466, and 482 in the carboxy terminus is required for cell movement and metastasis. In spite of the importance of cortactin tyrosine phosphorylation in cell motility, little is known regarding the structural, spatial, or signaling requirements regulating cortactin tyrosine phosphorylation. Herein, we report that phosphorylation of co

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15

Deng, Kaiping, Jason R. Mock, Steven Greenberg, Nicolai S. C. van Oers, and Eric J. Hansen. "Haemophilus ducreyi LspA Proteins Are Tyrosine Phosphorylated by Macrophage-Encoded Protein Tyrosine Kinases." Infection and Immunity 76, no. 10 (2008): 4692–702. http://dx.doi.org/10.1128/iai.00513-08.

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ABSTRACTThe LspA proteins (LspA1 and LspA2) ofHaemophilus ducreyiare necessary for this pathogen to inhibit the phagocytic activity of macrophage cell lines, an event that can be correlated with a reduction in the level of active Src family protein tyrosine kinases (PTKs) in these eukaryotic cells. During studies investigating this inhibitory mechanism, it was discovered that the LspA proteins themselves were tyrosine phosphorylated after wild-typeH. ducreyicells were incubated with macrophages. LspA proteins in cell-free concentratedH. ducreyiculture supernatant fluid could also be tyrosine p

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16

Tripathi, R. K., C. Chaya Devi, and A. Ramaiah. "pH-dependent interconversion of two forms of tyrosinase in human skin." Biochemical Journal 252, no. 2 (1988): 481–87. http://dx.doi.org/10.1042/bj2520481.

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1. We have shown that the characteristic lag in cresolase activity of human skin tyrosinase at inhibitory concentration of tyrosine was absent at all pH values studied, i.e. pH 5.2, 5.7, 6.2 and 6.8, if the enzyme solubilized at low pH was used as the source of enzyme, but the same enzyme when dialysed against buffers of various pH values showed linear activity only at pH 5.2 and was not inhibited by excess tyrosine, whereas at higher pH values it exhibited a lag and inhibition by excess tyrosine. 2. However, the enzyme solubilized in buffer/detergent, pH 6.8, when dialysed against buffer of t

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17

Mitchell, MA, MM Huang, P. Chien, ZK Indik, XQ Pan, and AD Schreiber. "Substitutions and deletions in the cytoplasmic domain of the phagocytic receptor Fc gamma RIIA: effect on receptor tyrosine phosphorylation and phagocytosis [published erratum appears in Blood 1994 Nov 1;84(9):3252]." Blood 84, no. 6 (1994): 1753–59. http://dx.doi.org/10.1182/blood.v84.6.1753.1753.

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Abstract Fc gamma RIIA in the absence of other Fc receptors or receptor subunits induces the ingestion of IgG-coated cells. The cytoplasmic domain of Fc gamma RIIA contains two Y-x-x-L sequences similar to those in other Ig gene family receptors plus an additional tyrosine residue not in a Y-x- x-L motif. Upon cross-linking, Fc gamma RIIA is phosphorylated on tyrosine and the cytoplasmic tyrosines, Y275 (Y1), Y282 (Y2), and Y298 (Y3), may be important for its phagocytic activity. Because COS-1 cells can serve as a model for examining molecular structures involved in phagocytosis, substitutions

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18

Mitchell, MA, MM Huang, P. Chien, ZK Indik, XQ Pan, and AD Schreiber. "Substitutions and deletions in the cytoplasmic domain of the phagocytic receptor Fc gamma RIIA: effect on receptor tyrosine phosphorylation and phagocytosis [published erratum appears in Blood 1994 Nov 1;84(9):3252]." Blood 84, no. 6 (1994): 1753–59. http://dx.doi.org/10.1182/blood.v84.6.1753.bloodjournal8461753.

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Fc gamma RIIA in the absence of other Fc receptors or receptor subunits induces the ingestion of IgG-coated cells. The cytoplasmic domain of Fc gamma RIIA contains two Y-x-x-L sequences similar to those in other Ig gene family receptors plus an additional tyrosine residue not in a Y-x- x-L motif. Upon cross-linking, Fc gamma RIIA is phosphorylated on tyrosine and the cytoplasmic tyrosines, Y275 (Y1), Y282 (Y2), and Y298 (Y3), may be important for its phagocytic activity. Because COS-1 cells can serve as a model for examining molecular structures involved in phagocytosis, substitutions and dele

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19

Slominski, Andrzej, and John Pawelek. "MSH binding in bomirski amelanotic hamster melanoma cells is stimulated by L-tyrosine." Bioscience Reports 7, no. 12 (1987): 949–54. http://dx.doi.org/10.1007/bf01122128.

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Bomirski Ab amelanotic melanoma cells have recently been shown to undergo striking phenotypic changes when precursors of the melanogenic pathway, L-tyrosine and L-dopa, are added to the culture medium. The changes include increased tyrosinase activity and de novo synthesis of melanosomes and melanin. L-tyrosine and L-dopa appeared to elicit these responses through separate but overlapping regulatory pathways. Here we show an additional effect of L-tyrosine: stimulation of MSH binding capacity. Cells cultured for 24–48 hours in the presence of 200 μM L-tyrosine display a 3–4 fold increase in th

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20

Ragab, Ashraf, Sonia Séverin, Marie-Pierre Gratacap та ін. "Roles of the C-terminal tyrosine residues of LAT in GPVI-induced platelet activation: insights into the mechanism of PLCγ2 activation". Blood 110, № 7 (2007): 2466–74. http://dx.doi.org/10.1182/blood-2007-02-075432.

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Linker for activation of T cells (LAT) is an adaptor protein required for organization of the signaling machinery downstream of the platelet collagen receptor, the glycoprotein VI (GPVI). Here, we investigated the effect of LAT mutations on specific signaling pathways and on platelet functions in response to GPVI triggering by convulxin (Cvx). Using mice containing tyrosine to phenylalanine mutations of the adaptor, we show the crucial role played by the tyrosine residues at positions 175, 195, and 235 in the phosphorylation of LAT and in the whole pattern of protein tyrosine phosphorylation i

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21

Slominski, A., G. Moellmann, and E. Kuklinska. "MSH inhibits growth in a line of amelanotic hamster melanoma cells and induces increases in cyclic AMP levels and tyrosinase activity without inducing melanogenesis." Journal of Cell Science 92, no. 4 (1989): 551–59. http://dx.doi.org/10.1242/jcs.92.4.551.

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In Bomirski Ab amelanotic hamster melanoma cells, L-tyrosine and/or L-dopa induce increases in tyrosinase activity as well as synthesis of melanosomes and melanin. L-tyrosine also modifies melanocyte-stimulating hormone (MSH) binding. In this paper we show that in the Bomirski amelanotic melanoma system MSH and agents that raise intracellular cyclic AMP induce dendrite formation, inhibit cell growth, and cause substantial increases in tyrosinase activity without inducing melanin synthesis. Tyrosinase activity is detected only in broken cell preparations, or cytochemically in fixed cells. In th

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22

Zhang, Juan, Elsa Berenstein та Reuben P. Siraganian. "Phosphorylation of Tyr342 in the Linker Region of Syk Is Critical for FcεRI Signaling in Mast Cells". Molecular and Cellular Biology 22, № 23 (2002): 8144–54. http://dx.doi.org/10.1128/mcb.22.23.8144-8154.2002.

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ABSTRACT The linker region of Syk and ZAP70 tyrosine kinases plays an important role in regulating their function. There are three conserved tyrosines in this linker region; Tyr317 of Syk and its equivalent residue in ZAP70 were previously shown to negatively regulate the function of Syk and ZAP70. Here we studied the roles of the other two tyrosines, Tyr342 and Tyr346 of Syk, in FcεRI-mediated signaling. Antigen stimulation resulted in Tyr342 phosphorylation in mast cells. Syk with Y342F mutation failed to reconstitute FcεRI-initiated histamine release. In the Syk Y342F-expressing cells there

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23

Naish-Byfield, S., and P. A. Riley. "Oxidation of monohydric phenol substrates by tyrosinase. An oximetric study." Biochemical Journal 288, no. 1 (1992): 63–67. http://dx.doi.org/10.1042/bj2880063.

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The purity of commercially available mushroom tyrosinase was investigated by non-denaturing PAGE. Most of the protein in the preparation migrated as a single band under these conditions. This band contained both tyrosinase and dopa oxidase activity. No other activity of either classification was found in the preparation. Oxygen consumption by tyrosinase during oxidation of the monohydric phenol substrates tyrosine and 4-hydroxyanisole (4HA) was monitored by oximetry in order to determine the stoichiometry of the reactions. For complete oxidation, the molar ratio of oxygen: 4HA was 1:1. Under i

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24

Johnson, Jared L., Tomer M. Yaron, Lewis C. Cantley, et al. "Abstract 3487: An atlas of substrate specificities for the human tyrosine kinome." Cancer Research 83, no. 7_Supplement (2023): 3487. http://dx.doi.org/10.1158/1538-7445.am2023-3487.

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Abstract Numerous physiological processes are governed by tyrosine phosphorylation. The protein tyrosine kinases that carry this out are dysregulated in a variety of cancers and are the targets of efficacious drugs. For most tyrosine kinases, we have a very limited understanding of their downstream signaling pathways and phosphorylation targets. Conversely, thousands of tyrosine phosphorylation events have so far been experimentally identified, and the overwhelming majority of these do not have an associated kinase. In this work, we have utilized peptide arrays to determine the substrate seque

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25

Barber, Dwayne L., Bryan K. Beattie, Jacqueline M. Mason, et al. "A common epitope is shared by activated signal transducer and activator of transcription-5 (STAT5) and the phosphorylated erythropoietin receptor: implications for the docking model of STAT activation." Blood 97, no. 8 (2001): 2230–37. http://dx.doi.org/10.1182/blood.v97.8.2230.

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Abstract Erythropoietin (EPO) specifically activates the Janus kinase JAK2 and the transcription factor signal transducer and activator of transcription-5 (STAT5). All members of the STAT family are tyrosine phosphorylated in response to cytokine stimulation at a conserved carboxy-terminal tyrosine, Y694, in the case of STAT5. To determine structural features important for STAT signaling, we generated an activation-specific STAT5 antibody using a phosphopeptide containing amino acids 687 to 698 of STAT5 as antigen. This antibody specifically recognizes tyrosine- phosphorylated STAT5 but not no

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26

Slominski, A., G. Moellmann, E. Kuklinska, A. Bomirski, and J. Pawelek. "Positive regulation of melanin pigmentation by two key substrates of the melanogenic pathway, L-tyrosine and L-dopa." Journal of Cell Science 89, no. 3 (1988): 287–96. http://dx.doi.org/10.1242/jcs.89.3.287.

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We describe results demonstrating the positive regulation of melanogenesis by two substrates of the melanogenic pathway. We have found that L-tyrosine and L-dihydroxyphenylalanine (L-dopa), whose metabolic fates are affected by the activity of that pathway, can also act as its regulators. In living pigment cells, tyrosinase (EC 1.14.18.1), a crucial and rate-limiting enzyme of melanogenesis, acts in subcellular organelles known as melanosomes. Melanin is laid down only in these organelles. We demonstrate that supplementing Ham's F-10 medium with additional L-tyrosine or L-dopa during the cultu

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Gobert, S., F. Porteu, S. Pallu, et al. "Tyrosine phosphorylation of the erythropoietin receptor: role for differentiation and mitogenic signal transduction." Blood 86, no. 2 (1995): 598–606. http://dx.doi.org/10.1182/blood.v86.2.598.bloodjournal862598.

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The erythropoietin (Epo) receptor belongs to the cytokine receptor superfamily. Although the cytokine receptors do not possess a tyrosine kinase consensus sequence in the intracellular domain, rapid stimulation of a tyrosine kinase activity occurs after activation by the ligand. We and others have shown that Epo induces the tyrosine phosphorylation of its cognate receptor as well as phosphorylation of other proteins. In this report, we examined the role of the receptor tyrosine residues in signal transduction. Eight tyrosine residues are located within the intracellular domain of the murine Ep

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Heffetz, D., W. J. Rutter, and Y. Zick. "The insulinomimetic agents H2O2 and vanadate stimulate tyrosine phosphorylation of potential target proteins for the insulin receptor kinase in intact cells." Biochemical Journal 288, no. 2 (1992): 631–35. http://dx.doi.org/10.1042/bj2880631.

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H2O2 and vanadate are known insulinomimetic agents. Together they induce insulin's bioeffects with a potency which exceeds that seen with insulin, vanadate or H2O2 alone. We have previously shown that a combination of H2O2 and vanadate, when added to intact cells, rapidly stimulates protein tyrosine phosphorylation, owing to the inhibitory effects of these agents on intracellular protein tyrosine phosphatases (PTPases). Employing Western blotting with anti-phosphotyrosine antibodies, we have now identified in Chinese-hamster ovary (CHO) cells transfected with a wild-type insulin-receptor gene

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Suwunwong, T., T. Kobkeatthawin, K. Chanawanno, N. Saewan, P. Wisitsak, and Suchada Chantrapromma. "Tyrosinase Inhibitory Activity of Pyrazole Derivatives." Advanced Materials Research 506 (April 2012): 194–97. http://dx.doi.org/10.4028/www.scientific.net/amr.506.194.

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A series of 3,5-substituted-4,5-dihydro-1H-pyrazole-1-carbothioamide derivatives were synthesized. Their structures were determined on the basis of spectroscopic data interpretation and their tyrosinase inhibitory activity was determined. The results showed that compound 2 (at 1.00 mg/mL) exhibits significant tyrosinase inhibitory activity with % inhibition of 91.866 ± 2.086 with L-tyrosine as substrate whereas compound 3 (at 1.00 mg/mL) exhibits significant tyrosinase inhibitory activity with % inhibition of 79.266 ± 0.552 and 89.593 ± 1.015 with L-tyrosine and L-DOPA as substrates. The IC50v

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Kimura, T., H. Sakamoto, E. Appella, and R. P. Siraganian. "Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides." Molecular and Cellular Biology 16, no. 4 (1996): 1471–78. http://dx.doi.org/10.1128/mcb.16.4.1471.

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A critical event in signaling in immune cells is the interaction of Syk or ZAP-70 protein tyrosine kinases with multisubunit receptors that contain an approximately 18-amino-acid domain called the immunoreceptor tyrosine-based activation motif (ITAM). Tyrosine-phosphorylated Syk from activated cells was in a conformation different from that in nonstimulated cells as demonstrated by changes in immunoreactivity. The addition of tyrosine-diphosphorylated ITAM peptides resulted in a similar conformational change in Syk from nonactivated cells. The peptides based on FcepsilonRIgamma were more activ

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Binns, Kathleen L., Paul P. Taylor, Frank Sicheri, Tony Pawson, and Sacha J. Holland. "Phosphorylation of Tyrosine Residues in the Kinase Domain and Juxtamembrane Region Regulates the Biological and Catalytic Activities of Eph Receptors." Molecular and Cellular Biology 20, no. 13 (2000): 4791–805. http://dx.doi.org/10.1128/mcb.20.13.4791-4805.2000.

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ABSTRACT Members of the Eph family of receptor tyrosine kinases exhibit a striking degree of amino acid homology, particularly notable in the kinase and membrane-proximal regions. A mutagenesis approach was taken to address the functions of specific conserved tyrosine residues within these catalytic and juxtamembrane domains. Ligand stimulation of wild-type EphB2 in neuronal NG108-15 cells resulted in an upregulation of catalytic activity and an increase in cellular tyrosine phosphorylation, accompanied by a retraction of neuritic processes. Tyrosine-to-phenylalanine substitutions within the c

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Sadra, Ali, Tomas Cinek, Jerry L. Arellano, Jia Shi, Kenneth E. Truitt, and John B. Imboden. "Identification of Tyrosine Phosphorylation Sites in the CD28 Cytoplasmic Domain and Their Role in the Costimulation of Jurkat T Cells." Journal of Immunology 162, no. 4 (1999): 1966–73. http://dx.doi.org/10.4049/jimmunol.162.4.1966.

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Abstract The cytoplasmic domain of CD28 contains four tyrosine residues. Because signal transduction by CD28 appears to involve its tyrosine phosphorylation, we determined sites of CD28 tyrosine phosphorylation using mutants of mouse CD28 that retained tyrosine at one position, with the remaining three positions mutated to phenylalanine. When expressed in Jurkat cells and stimulated by mAb, only the mutants with tyrosine at position 170 or 188 were tyrosine phosphorylated. Phosphorylation of Tyr170 recruits phosphatidylinositol 3-kinase to CD28. Tyr188 has not been associated with any specific

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33

Rybalchenko I.V., Krylov V. I. "Synthesis of O-tyrosine Phosphorylated Adducts of Methylphosphonic and Phosphoric Acid Derivatives as Reference Compounds for the Analysis of Biomedical Samples." Journal of NBC Protection Corps 3, no. 2 (2019): 103–10. http://dx.doi.org/10.35825/2587-5728-2019-3-2-103-110.

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Organophosphorus chemical agents are included in the 1st List of the Annex on Chemicals of the Convention on the Prohibition of the Development, Production, Stockpiling and Use of Chemical Weapons and on Their Destruction (Chemical Weapons Convention, CWC). For the purposes of verification of compliance with the provisions of the CWC, special methods, which are considered the most informative at determining the retrospective effects of organophosphorus toxicants on the body, are necessary. Typical long-lived biomarkers of organophosphate toxic agents are tyrosine phosphorylation products, the

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34

Matos, Maria João, Lourdes Santana, Eugenio Uriarte, et al. "Tyrosine-like condensed derivatives as tyrosinase inhibitors." Journal of Pharmacy and Pharmacology 64, no. 5 (2012): 742–46. http://dx.doi.org/10.1111/j.2042-7158.2012.01467.x.

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35

Musch, M. W., F. M. McConnell, L. Goldstein, and M. Field. "Tyrosine transport in winter flounder intestine: interaction with Na+-K+-2Cl- cotransport." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 253, no. 2 (1987): R264—R269. http://dx.doi.org/10.1152/ajpregu.1987.253.2.r264.

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Tyrosine absorption across the brush border of the intestinal epithelium of the winter flounder Pseudopleuronectes americanus was studied in Ussing chambers modified to determine early rates of uptake. At 0.1 mM tyrosine, the 4-min rate of uptake (influx) of tyrosine across the brush border averaged 37.5 nmol X cm-2 X h-1. Omission of Na decreased influx by 60%, indicating that tyrosine influx occurs, at least in part, by a Na-coupled process. Ouabain inhibited influx by 80%. Inhibition of brush border Na+-K+-2Cl- cotransport by bumetanide, 8-bromo-cyclic GMP, or Cl replacement stimulated tyro

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36

Castro, Rodrigo, Juan Zhang, Maria Jamur, Constance Oliver, and Reuben Siraganian. "Tyrosines in the carboxy-terminal region regulate Syk function (86.18)." Journal of Immunology 184, no. 1_Supplement (2010): 86.18. http://dx.doi.org/10.4049/jimmunol.184.supp.86.18.

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Abstract The Syk tyrosine kinase family has an essential role in immunoreceptor tyrosine-based activation motif (ITAM) signaling. The binding of Syk to tyrosine phosphorylated ITAMs in the subunits of FcϵRI results in a conformational change, with an increase in the enzymatic activity of Syk. This conformational change exposes the COOH terminal region of Syk which has three conserved Tyr residues (Y623, Y624, Y625 of rat Syk). To understand the role of these residues in signaling, wild-type and mutant Syk with these three Tyr mutated to Phe were expressed in Syk-deficient mast cells. There was

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37

Gauen, L. K., Y. Zhu, F. Letourneur, et al. "Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif." Molecular and Cellular Biology 14, no. 6 (1994): 3729–41. http://dx.doi.org/10.1128/mcb.14.6.3729-3741.1994.

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Abstract (sommario):

The tyrosine-based activation motif is a 20- to 25-amino-acid sequence contained in the cytoplasmic domains of many hematopoietic receptors which is sufficient by itself to reconstitute signalling. This motif is characterized by two YXXL/I sequences separated by approximately 10 residues. The molecular basis of signalling by this motif is unknown. Here we demonstrate that the tyrosine-based activation motif is required and sufficient for association with the tyrosine kinases p59fyn and ZAP-70, suggesting that association with these kinases is a general feature of this motif. Focusing on the si

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38

Gauen, L. K., Y. Zhu, F. Letourneur, et al. "Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif." Molecular and Cellular Biology 14, no. 6 (1994): 3729–41. http://dx.doi.org/10.1128/mcb.14.6.3729.

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Abstract (sommario):

The tyrosine-based activation motif is a 20- to 25-amino-acid sequence contained in the cytoplasmic domains of many hematopoietic receptors which is sufficient by itself to reconstitute signalling. This motif is characterized by two YXXL/I sequences separated by approximately 10 residues. The molecular basis of signalling by this motif is unknown. Here we demonstrate that the tyrosine-based activation motif is required and sufficient for association with the tyrosine kinases p59fyn and ZAP-70, suggesting that association with these kinases is a general feature of this motif. Focusing on the si

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39

Keshvara, Lakhu M., Christina C. Isaacson, Thomas M. Yankee, Radmila Sarac, Marietta L. Harrison, and Robert L. Geahlen. "Syk- and Lyn-Dependent Phosphorylation of Syk on Multiple Tyrosines Following B Cell Activation Includes a Site That Negatively Regulates Signaling." Journal of Immunology 161, no. 10 (1998): 5276–83. http://dx.doi.org/10.4049/jimmunol.161.10.5276.

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Abstract (sommario):

Abstract The Syk protein tyrosine kinase is an essential component of the B cell Ag receptor signaling pathway. Syk is phosphorylated on tyrosine following B cell activation. However, the sites that are modified and the kinases responsible for these modifications have yet to be determined. To approach this problem, we used a mapping strategy based on the electrophoretic separation of peptides on alkaline polyacrylamide gels to identify the tryptic phosphopeptides derived from metabolically labeled Syk. In this work, we report that Syk from activated B cells is phosphorylated principally on six

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40

Slominski, Andrzej, Pawel Jastreboff, and John Pawelek. "L-Tyrosine stimulates induction of tyrosinase activity by MSH and reduces cooperative interactions between MSH receptors in hamster melanoma cells." Bioscience Reports 9, no. 5 (1989): 579–86. http://dx.doi.org/10.1007/bf01119801.

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Abstract (sommario):

L-tyrosine, a precurosr to melanin, has recently been shown to be a regulator of the melanogenic pathway in some cultured melanoma cell lines. In this paper we demonstrated that L-tyrosine, besides increasing binding capacity for MSH, decreased cooperativity between MSH receptors and increased the level of tyrosinase induction by MSH. Apparently, regulation of MSH receptor activity by L-tyrosine involves specific changes in the interactions between the receptors and modification of the cellular responsiveness to MSH.

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41

Müller, Günter, Susanne Wied, and Wendelin Frick. "Cross Talk of pp125FAK and pp59Lyn Non-Receptor Tyrosine Kinases to Insulin-Mimetic Signaling in Adipocytes." Molecular and Cellular Biology 20, no. 13 (2000): 4708–23. http://dx.doi.org/10.1128/mcb.20.13.4708-4723.2000.

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Abstract (sommario):

ABSTRACT Signaling molecules downstream from the insulin receptor, such as the insulin receptor substrate protein 1 (IRS-1), are also activated by other receptor tyrosine kinases. Here we demonstrate that the non-receptor tyrosine kinases, focal adhesion kinase pp125FAK and Src-class kinase pp59Lyn, after insulin-independent activation by phosphoinositolglycans (PIG), can cross talk to metabolic insulin signaling in rat and 3T3-L1 adipocytes. Introduction by electroporation of neutralizing antibodies against pp59Lyn and pp125FAK into isolated rat adipocytes blocked IRS-1 tyrosine phosphorylati

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42

Kurzer, Jason H., Lawrence S. Argetsinger, Yong-Jie Zhou, Jean-Louis K. Kouadio, John J. O'Shea та Christin Carter-Su. "Tyrosine 813 Is a Site of JAK2 Autophosphorylation Critical for Activation of JAK2 by SH2-Bβ". Molecular and Cellular Biology 24, № 10 (2004): 4557–70. http://dx.doi.org/10.1128/mcb.24.10.4557-4570.2004.

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Abstract (sommario):

ABSTRACT The tyrosine kinase Janus kinase 2 (JAK2) binds to the majority of the known members of the cytokine family of receptors. Ligand-receptor binding leads to activation of the associated JAK2 molecules, resulting in rapid autophosphorylation of multiple tyrosines within JAK2. Phosphotyrosines can then serve as docking sites for downstream JAK2 signaling molecules. Despite the importance of these phosphotyrosines in JAK2 function, only a few sites and binding partners have been identified. Using two-dimensional phosphopeptide mapping and a phosphospecific antibody, we identified tyrosine

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43

Saitoh, Shin-ichiroh, Sandra Odom, Gregorio Gomez та ін. "The Four Distal Tyrosines Are Required for LAT-dependent Signaling in FcεRI-mediated Mast Cell Activation". Journal of Experimental Medicine 198, № 5 (2003): 831–43. http://dx.doi.org/10.1084/jem.20030574.

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Abstract (sommario):

The linker for activation of T cells (LAT) is an adaptor protein critical for FcεRI-mediated mast cell activation. LAT is a substrate of the tyrosine kinases activated after TCR and FcεRI engagement. After phosphorylation of the cytosolic domain of LAT, multiple signaling molecules such as phospholipase C–γ1, Grb2, and Gads associate with phosphorylated LAT via their SH2 domains. The essential role of the four distal tyrosines in TCR-mediated signaling and T cell development has been demonstrated by experiments using LAT-deficient cell lines and genetically modified mice. To investigate the ro

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44

Kulathu, Yogesh, Christa Zuern, Jianying Yang, and Michael Reth. "Synthetic biology of B cell activation: understanding signal amplification at the B cell antigen receptor using a rebuilding approach." Biological Chemistry 400, no. 4 (2019): 555–63. http://dx.doi.org/10.1515/hsz-2018-0308.

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Abstract (sommario):

Abstract Upon activation of the B cell antigen receptor (BCR), the spleen tyrosine kinase (Syk) and the Src family kinase Lyn phosphorylate tyrosines of the immunoreceptor tyrosine-based activation motif (ITAM) of Igα and Igβ which further serve as binding sites for the SH2 domains of these kinases. Using a synthetic biology approach, we dissect the roles of different ITAM residues of Igα in Syk activation. We found that a leucine to glycine mutation at the Y+3 position after the first ITAM tyrosine prevents Syk binding and activation. However, a pre-activated Syk can still phosphorylate this

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45

REILAND, Jane, Vanessa L. OTT, Connie S. LEBAKKEN, Charles YEAMAN, James McCARTHY, and Alan C. RAPRAEGER. "Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1." Biochemical Journal 319, no. 1 (1996): 39–47. http://dx.doi.org/10.1042/bj3190039.

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Abstract (sommario):

Syndecan-1 is a transmembrane haparan sulphate proteoglycan that binds extracellular matrices and growth factors, making it a candidate to act between these regulatory molecules and intracellular signalling pathways. It has a highly conserved transmembrane/cytoplasmic domain that contains four conserved tyrosines. One of these is in a consensus sequence for tyrosine kinase phosphorylation. As an initial step to investigating whether or not phosphorylation of these tyrosines is part of a signal-transduction pathway, we have monitored the tyrosine phosphorylation of syndecan-1 by cytoplasmic tyr

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46

Tauchi, T., JE Damen, K. Toyama, GS Feng, HE Broxmeyer, and G. Krystal. "Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis." Blood 87, no. 11 (1996): 4495–501. http://dx.doi.org/10.1182/blood.v87.11.4495.bloodjournal87114495.

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Abstract (sommario):

Erythropoietin (Epo), the primary in vivo stimulator of erythroid proliferation and differentiation, acts, in part, by altering the tyrosine phosphorylation levels of various intracellular signaling molecules. These phosphorylation levels are tightly regulated by both tyrosine kinases and tyrosine phosphatases. We have recently shown that the SH2 containing tyrosine phosphatase, Syp, binds directly to both the tyrosine phosphorylated form of the Epo receptor (EpoR) and to Grb2 after Epo stimulation of M07e cells engineered to express high levels of human EpoRs (T. Tauchi, et al: J Biol Chem 27

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47

Rocchi, Stéphane, Sophie Tartare-Deckert, Joseph Murdaca, Marina Holgado-Madruga, Albert J. Wong, and Emmanuel Van Obberghen. "Determination of Gab1 (Grb2-Associated Binder-1) Interaction with Insulin Receptor-Signaling Molecules." Molecular Endocrinology 12, no. 7 (1998): 914–23. http://dx.doi.org/10.1210/mend.12.7.0141.

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Abstract (sommario):

Abstract The newly identified insulin receptor (IR) substrate, Gab1 [growth factor receptor bound 2 (Grb2)-associated binder-1] is rapidly phosphorylated on several tyrosine residues by the activated IR. Phosphorylated Gab1 acts as a docking protein for Src homology-2 (SH2) domain-containing proteins. These include the regulatory subunit p85 of phosphatidylinositol 3-kinase and phosphotyrosine phosphatase, SHP-2. In this report, using a modified version of the yeast two-hybrid system, we localized which Gab1 phospho-tyrosine residues are required for its interaction with phosphatidylinositol 3

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48

Backer, J. M., S. E. Shoelson, M. A. Weiss, et al. "The insulin receptor juxtamembrane region contains two independent tyrosine/beta-turn internalization signals." Journal of Cell Biology 118, no. 4 (1992): 831–39. http://dx.doi.org/10.1083/jcb.118.4.831.

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Abstract (sommario):

We have investigated the role of tyrosine residues in the insulin receptor cytoplasmic juxtamembrane region (Tyr953 and Tyr960) during endocytosis. Analysis of the secondary structure of the juxtamembrane region by the Chou-Fasman algorithms predicts that both the sequences GPLY953 and NPEY960 form tyrosine-containing beta-turns. Similarly, analysis of model peptides by 1-D and 2-D NMR show that these sequences form beta-turns in solution, whereas replacement of the tyrosine residues with alanine destabilizes the beta-turn. CHO cell lines were prepared expressing mutant receptors in which each

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49

den Hartog, Marcel T., Carin C. Sijmons, Onno Bakker, Carrie Ris-Stalpers, and Jan JM de Vijlder. "Importance of the content and localization of tyrosine residues for thyroxine formation within the N-terminal part of human thyroglobulin." European Journal of Endocrinology 132, no. 5 (1995): 611–17. http://dx.doi.org/10.1530/eje.0.1320611.

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Abstract (sommario):

Den Hartog MT, Sijmons CC, Bakker 0, Ris-Stalpers C, de Vijlder JJM. Importance of the content and localization of tyrosine residues for thyroxine formation within the N-terminal part of human thyroglobulin. Eur J Endocrinol 1995;132:611–17. ISSN 0804–4643 Thyroxine (T4) is formed by coupling of iodinated tyrosine residues within thyroglobulin (TG). In mature TG, some iodinated tyrosine residues are involved preferentially in T4 formation. In order to investigate the specific role of various tyrosine residues in T4 formation, N-terminal TG fragments with mutated tyrosine residues were construc

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50

Chin, Hiroshi, Ayako Arai, Hiroshi Wakao, Ryuichi Kamiyama, Nobuyuki Miyasaka, and Osamu Miura. "Lyn Physically Associates With the Erythropoietin Receptor and May Play a Role in Activation of the Stat5 Pathway." Blood 91, no. 10 (1998): 3734–45. http://dx.doi.org/10.1182/blood.v91.10.3734.

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Abstract (sommario):

Abstract Protein tyrosine phosphorylation plays a crucial role in signaling from the receptor for erythropoietin (Epo), although the Epo receptor (EpoR) lacks the tyrosine kinase domain. We have previously shown that the Jak2 tyrosine kinase couples with the EpoR to transduce a growth signal. In the present study, we demonstrate that Lyn, a Src family tyrosine kinase, physically associates with the EpoR in Epo-dependent hematopoietic cell lines, 32D/EpoR-Wt and F36E. Coexpression experiments in COS7 cells further showed that Lyn induces tyrosine phosphorylation of the EpoR and that both LynA a

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