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Journal articles on the topic 'Phosphorylation motif'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

NEWTON, Alexandra C. "Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm." Biochemical Journal 370, no. 2 (2003): 361–71. http://dx.doi.org/10.1042/bj20021626.

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Phosphorylation plays a central role in regulating the activation and signalling lifetime of protein kinases A, B (also known as Akt) and C. These kinases share three conserved phosphorylation motifs: the activation loop segment, the turn motif and the hydrophobic motif. This review focuses on how phosphorylation at each of these sites regulates the maturation, signalling and down-regulation of PKC as a paradigm for how these sites control the function of the ABC kinases.

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2

Fu, Zheng, Melanie J. Schroeder, Jeffrey Shabanowitz, et al. "Activation of a Nuclear Cdc2-Related Kinase within a Mitogen-Activated Protein Kinase-Like TDY Motif by Autophosphorylation and Cyclin-Dependent Protein Kinase-Activating Kinase." Molecular and Cellular Biology 25, no. 14 (2005): 6047–64. http://dx.doi.org/10.1128/mcb.25.14.6047-6064.2005.

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ABSTRACT Male germ cell-associated kinase (MAK) and intestinal cell kinase (ICK) are nuclear Cdc2-related kinases with nearly identical N-terminal catalytic domains and more divergent C-terminal noncatalytic domains. The catalytic domain is also related to mitogen-activated protein kinases (MAPKs) and contains a corresponding TDY motif. Nuclear localization of ICK requires subdomain XI and interactions of the conserved Arg-272, but not kinase activity or, surprisingly, any of the noncatalytic domain. Further, nuclear localization of ICK is required for its activation. ICK is activated by dual

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3

Das, Rahul K., Yongqi Huang, Aaron H. Phillips, Richard W. Kriwacki, and Rohit V. Pappu. "Cryptic sequence features within the disordered protein p27Kip1 regulate cell cycle signaling." Proceedings of the National Academy of Sciences 113, no. 20 (2016): 5616–21. http://dx.doi.org/10.1073/pnas.1516277113.

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Peptide motifs embedded within intrinsically disordered regions (IDRs) of proteins are often the sites of posttranslational modifications that control cell-signaling pathways. How do IDR sequences modulate the functionalities of motifs? We answer this question using the polyampholytic C-terminal IDR of the cell cycle inhibitory protein p27Kip1 (p27). Phosphorylation of Thr-187 (T187) within the p27 IDR controls entry into S phase of the cell division cycle. Additionally, the conformational properties of polyampholytic sequences are predicted to be influenced by the linear patterning of opposit

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4

Adams, Peter D., Xiaotong Li, William R. Sellers, et al. "Retinoblastoma Protein Contains a C-terminal Motif That Targets It for Phosphorylation by Cyclin-cdk Complexes." Molecular and Cellular Biology 19, no. 2 (1999): 1068–80. http://dx.doi.org/10.1128/mcb.19.2.1068.

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ABSTRACT Stable association of certain proteins, such as E2F1 and p21, with cyclin-cdk2 complexes is dependent upon a conserved cyclin-cdk2 binding motif that contains the core sequence ZRXL, where Z and X are usually basic. In vitro phosphorylation of the retinoblastoma tumor suppressor protein, pRB, by cyclin A-cdk2 and cyclin E-cdk2 was inhibited by a short peptide spanning the cyclin-cdk2 binding motif present in E2F1. Examination of the pRB C terminus revealed that it contained sequence elements related to ZRXL. Site-directed mutagenesis of one of these sequences, beginning at residue 870

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5

Baffi, Timothy R., Gema Lordén, Jacob M. Wozniak, et al. "mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved TOR interaction motif." Science Signaling 14, no. 678 (2021): eabe4509. http://dx.doi.org/10.1126/scisignal.abe4509.

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The complex mTORC2 is accepted to be the kinase that controls the phosphorylation of the hydrophobic motif, a key regulatory switch for AGC kinases, although whether mTOR directly phosphorylates this motif remains controversial. Here, we identified an mTOR-mediated phosphorylation site that we termed the TOR interaction motif (TIM; F-x3-F-pT), which controls the phosphorylation of the hydrophobic motif of PKC and Akt and the activity of these kinases. The TIM is invariant in mTORC2-dependent AGC kinases, is evolutionarily conserved, and coevolved with mTORC2 components. Mutation of this motif

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6

Hiraoka, D., E. Okumura, and T. Kishimoto. "Turn motif phosphorylation negatively regulates activation loop phosphorylation in Akt." Oncogene 30, no. 44 (2011): 4487–97. http://dx.doi.org/10.1038/onc.2011.155.

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7

García-Martínez, Juan M., and Dario R. Alessi. "mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)." Biochemical Journal 416, no. 3 (2008): 375–85. http://dx.doi.org/10.1042/bj20081668.

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SGK1 (serum- and glucocorticoid-induced protein kinase 1) is a member of the AGC (protein kinase A/protein kinase G/protein kinase C) family of protein kinases and is activated by agonists including growth factors. SGK1 regulates diverse effects of extracellular agonists by phosphorylating regulatory proteins that control cellular processes such as ion transport and growth. Like other AGC family kinases, activation of SGK1 is triggered by phosphorylation of a threonine residue within the T-loop of the kinase domain and a serine residue lying within the C-terminal hydrophobic motif (Ser422 in S

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8

Hayashi, Fumio, Noriyo Itoh, Tatsuya Uzumaki, et al. "Roles of Two ATPase-Motif-containing Domains in Cyanobacterial Circadian Clock Protein KaiC." Journal of Biological Chemistry 279, no. 50 (2004): 52331–37. http://dx.doi.org/10.1074/jbc.m406604200.

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Cyanobacterial clock protein KaiC has a hexagonal, pot-shaped structure composed of six identical dumbbell-shaped subunits. Each subunit has duplicated domains, and each domain has a set of ATPase motifs. The two spherical regions of the dumbbell are likely to correspond to two domains. We examined the role of the two sets of ATPase motifs by analyzing thein vitroactivity of ATPγS binding, AMPPNP-induced hexamerization, thermostability, and phosphorylation of KaiC and byin vivorhythm assays both in wild type KaiC (KaiCWT) and KaiCs carrying mutations in either Walker motif A or deduced catalyt

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Pollitt, Alice Y., Beata Grygielska, Bertrand Leblond, Laurent Désiré, Johannes A. Eble, and Steve P. Watson. "Phosphorylation of CLEC-2 is dependent on lipid rafts, actin polymerization, secondary mediators, and Rac." Blood 115, no. 14 (2010): 2938–46. http://dx.doi.org/10.1182/blood-2009-12-257212.

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Abstract The C-type lectin-like receptor 2 (CLEC-2) activates platelets through Src and Syk tyrosine kinases via a single cytoplasmic YxxL motif known as a hem immunoreceptor tyrosine-based activation motif (hemITAM). Here, we demonstrate using sucrose gradient ultracentrifugation and methyl-β-cyclodextrin treatment that CLEC-2 translocates to lipid rafts upon ligand engagement and that translocation is essential for hemITAM phosphorylation and signal initiation. HemITAM phosphorylation, but not translocation, is also critically dependent on actin polymerization, Rac1 activation, and release o

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10

Ikeda, Masato, Akiko Ikeda, and Richard Longnecker. "PY Motifs of Epstein-Barr Virus LMP2A Regulate Protein Stability and Phosphorylation of LMP2A-Associated Proteins." Journal of Virology 75, no. 12 (2001): 5711–18. http://dx.doi.org/10.1128/jvi.75.12.5711-5718.2001.

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ABSTRACT Latent membrane protein 2A (LMP2A) is expressed in latent Epstein-Barr virus (EBV) infection. We have demonstrated that Nedd4 family ubiquitin-protein ligases (E3s), AIP4, WWP2/AIP2, and Nedd4, bind specifically to two PY motifs present within the LMP2A amino-terminal domain. In this study, LMP2A PY motif mutant viruses were constructed to investigate the role of the LMP2A PY motifs. AIP4 was found to specifically associate with the LMP2A PY motifs in EBV-transformed lymphoblastoid cell lines (LCLs), extending our original observation to EBV-infected cells. Mutation of both of the LMP

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11

Miller, M. L., L. J. Jensen, F. Diella, et al. "Linear Motif Atlas for Phosphorylation-Dependent Signaling." Science Signaling 1, no. 35 (2008): ra2. http://dx.doi.org/10.1126/scisignal.1159433.

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12

Manning, Viola A., Rachael M. Andrie, Aaron F. Trippe, and Lynda M. Ciuffetti. "Ptr ToxA Requires Multiple Motifs for Complete Activity." Molecular Plant-Microbe Interactions® 17, no. 5 (2004): 491–501. http://dx.doi.org/10.1094/mpmi.2004.17.5.491.

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Ptr ToxA was the first proteinaceous necrosis-inducing toxin identified and cloned from the wheat pathogen, Pyrenophora tritici-repentis. How this protein causes necrosis in sensitive wheat cultivars is not known. In an effort to understand the structural features of Ptr ToxA required for induction of necrosis, we employed a combination of site-directed mutagenesis and peptide inhibition studies. Mutagenesis was carried out on conserved motifs within the active domain of Ptr ToxA. Proteins with mutations of potential casein kinase 2 phosphorylation sites but not protein kinase C phosphorylatio

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13

Schmücker, Anna, Bingkun Lei, Zdravko J. Lorković, et al. "Crosstalk between H2A variant-specific modifications impacts vital cell functions." PLOS Genetics 17, no. 6 (2021): e1009601. http://dx.doi.org/10.1371/journal.pgen.1009601.

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Selection of C-terminal motifs participated in evolution of distinct histone H2A variants. Hybrid types of variants combining motifs from distinct H2A classes are extremely rare. This suggests that the proximity between the motif cases interferes with their function. We studied this question in flowering plants that evolved sporadically a hybrid H2A variant combining the SQ motif of H2A.X that participates in the DNA damage response with the KSPK motif of H2A.W that stabilizes heterochromatin. Our inventory of PTMs of H2A.W variants showed that in vivo the cell cycle-dependent kinase CDKA phos

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14

Faustova, Ilona, Kaidi Möll, Ervin Valk, Mart Loog, and Mihkel Örd. "Docking to a Basic Helix Promotes Specific Phosphorylation by G1-Cdk1." International Journal of Molecular Sciences 22, no. 17 (2021): 9514. http://dx.doi.org/10.3390/ijms22179514.

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Cyclins are the activators of cyclin-dependent kinase (CDK) complex, but they also act as docking scaffolds for different short linear motifs (SLiMs) in CDK substrates and inhibitors. According to the unified model of CDK function, the cell cycle is coordinated by CDK both via general CDK activity thresholds and cyclin-specific substrate docking. Recently, it was found that the G1-cyclins of S. cerevisiae have a specific function in promoting polarization and growth of the buds, making the G1 cyclins essential for cell survival. Thus, while a uniform CDK specificity of a single cyclin can be s

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15

Das, Falguni, Nandini Ghosh-Choudhury, Meenalakshmi M. Mariappan, Balakuntalam S. Kasinath та Goutam Ghosh Choudhury. "Hydrophobic motif site-phosphorylated protein kinase CβII between mTORC2 and Akt regulates high glucose-induced mesangial cell hypertrophy". American Journal of Physiology-Cell Physiology 310, № 7 (2016): C583—C596. http://dx.doi.org/10.1152/ajpcell.00266.2015.

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PKCβII controls the pathologic features of diabetic nephropathy, including glomerular mesangial cell hypertrophy. PKCβII contains the COOH-terminal hydrophobic motif site Ser-660. Whether this hydrophobic motif phosphorylation contributes to high glucose-induced mesangial cell hypertrophy has not been determined. Here we show that, in mesangial cells, high glucose increased phosphorylation of PKCβII at Ser-660 in a phosphatidylinositol 3-kinase (PI3-kinase)-dependent manner. Using siRNAs to downregulate PKCβII, dominant negative PKCβII, and PKCβII hydrophobic motif phosphorylation-deficient mu

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Wang, Jianchuan, Chen Zhong, Fang Wang, Fangfang Qu, and Jianping Ding. "Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif." Biochemical Journal 454, no. 1 (2013): 39–47. http://dx.doi.org/10.1042/bj20121863.

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The activity of S6K1 (p70 ribosomal protein subunit 6 kinase 1) is stimulated by phosphorylation of Thr389 in the hydrophobic motif by mTORC1 (mammalian target of rapamycin complex 1) and phosphorylation of Thr229 in the activation loop by PDK1 (phosphoinositide-dependent kinase 1); however, the order of the two events is still ambiguous. In the present paper we report six crystal structures of the S6K1 kinase domain alone or plus the hydrophobic motif in various forms, in complexes with a highly specific inhibitor. The structural data, together with the biochemical data, reveal in vivo phosph

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17

Dietrich, Jes, Jesper Kastrup, Bodil L. Nielsen, Niels Ødum та Carsten Geisler. "Regulation and Function of the CD3γ DxxxLL Motif: A Binding Site for Adaptor Protein-1 and Adaptor Protein-2 in Vitro". Journal of Cell Biology 138, № 2 (1997): 271–81. http://dx.doi.org/10.1083/jcb.138.2.271.

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Several receptors are downregulated by internalization after ligand binding. Regulation of T cell receptor (TCR) expression is an important step in T cell activation, desensitization, and tolerance induction. One way T cells regulate TCR expression is by phosphorylation/dephosphorylation of the TCR subunit clusters of differentiation (CD)3γ. Thus, phosphorylation of CD3γ serine 126 (S126) causes a downregulation of the TCR. In this study, we have analyzed the CD3γ internalization motif in three different systems in parallel: in the context of the complete multimeric TCR; in monomeric CD4/CD3γ

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18

Argent, Richard H., James L. Hale, Emad M. El-Omar, and John C. Atherton. "Differences in Helicobacter pylori CagA tyrosine phosphorylation motif patterns between western and East Asian strains, and influences on interleukin-8 secretion." Journal of Medical Microbiology 57, no. 9 (2008): 1062–67. http://dx.doi.org/10.1099/jmm.0.2008/001818-0.

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Helicobacter pylori strains from East Asia have an ‘East Asian’ type of CagA that is more active and predominantly comprises a single type. Strains from other countries have a ‘western’ type of CagA, which is less active and comprises many different types generated by intragenomic recombination. Co-culture of AGS gastric epithelial cells with isolates of western strains that displayed microevolution in CagA showed that isolates with additional copies of the C motif induced significantly more interleukin (IL)-8 secretion. Co-culture of AGS cells with western and East Asian strains, each express

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Ritz, Anna, Gregory Shakhnarovich, Arthur R. Salomon, and Benjamin J. Raphael. "Discovery of phosphorylation motif mixtures in phosphoproteomics data." Bioinformatics 25, no. 1 (2008): 14–21. http://dx.doi.org/10.1093/bioinformatics/btn569.

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20

Hietakangas, V., J. Anckar, H. A. Blomster, et al. "PDSM, a motif for phosphorylation-dependent SUMO modification." Proceedings of the National Academy of Sciences 103, no. 1 (2005): 45–50. http://dx.doi.org/10.1073/pnas.0503698102.

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21

Diechler, Sebastian, Bianca E. Chichirau, Gernot Posselt, Dionyssios N. Sgouras, and Silja Wessler. "Helicobacter pylori CagA EPIYA Motif Variations Affect Metabolic Activity in B Cells." Toxins 13, no. 9 (2021): 592. http://dx.doi.org/10.3390/toxins13090592.

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Background: Helicobacter pylori (Hp) colonizes the human stomach and can induce gastric cancer and mucosa-associated lymphoid tissue (MALT) lymphoma. Clinical observations suggest a role for the Hp virulence factor cytotoxin-associated gene A (CagA) in pathogenesis. The pathogenic activity of CagA is partly regulated by tyrosine phosphorylation of C-terminal Glu-Pro-Ile-Tyr-Ala (EPIYA) motifs in host cells. However, CagA differs considerably in EPIYA motifs, whose functions have been well characterized in epithelial cells. Since CagA is fragmented in immune cells, different CagA variants may e

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22

Shin, Yeun-Kyung, Yang Li, Qiang Liu, Deborah H. Anderson, Lorne A. Babiuk, and Yan Zhou. "SH3 Binding Motif 1 in Influenza A Virus NS1 Protein Is Essential for PI3K/Akt Signaling Pathway Activation." Journal of Virology 81, no. 23 (2007): 12730–39. http://dx.doi.org/10.1128/jvi.01427-07.

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ABSTRACT Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K. Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K. Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p

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García-Martínez, Juan M., Jennifer Moran, Rosemary G. Clarke, et al. "Ku-0063794 is a specific inhibitor of the mammalian target of rapamycin (mTOR)." Biochemical Journal 421, no. 1 (2009): 29–42. http://dx.doi.org/10.1042/bj20090489.

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mTOR (mammalian target of rapamycin) stimulates cell growth by phosphorylating and promoting activation of AGC (protein kinase A/protein kinase G/protein kinase C) family kinases such as Akt (protein kinase B), S6K (p70 ribosomal S6 kinase) and SGK (serum and glucocorticoid protein kinase). mTORC1 (mTOR complex-1) phosphorylates the hydrophobic motif of S6K, whereas mTORC2 phosphorylates the hydrophobic motif of Akt and SGK. In the present paper we describe the small molecule Ku-0063794, which inhibits both mTORC1 and mTORC2 with an IC50 of ∼10 nM, but does not suppress the activity of 76 othe

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Leng, Xiaohong, Martin Noble, Peter D. Adams, Jun Qin, and J. Wade Harper. "Reversal of Growth Suppression by p107 via Direct Phosphorylation by Cyclin D1/Cyclin-Dependent Kinase 4." Molecular and Cellular Biology 22, no. 7 (2002): 2242–54. http://dx.doi.org/10.1128/mcb.22.7.2242-2254.2002.

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ABSTRACT p107 functions to control cell division and development through interaction with members of the E2F family of transcription factors. p107 is phosphorylated in a cell cycle-regulated manner, and its phosphorylation leads to its release from E2F. Although it is known that p107 physically associates with E- and A-type cyclin/cyclin-dependent kinase 2 (Cdk2) complexes through a cyclin-binding RXL motif located in the spacer domain, the mechanisms underlying p107 inactivation via phosphorylation remain poorly defined. Recent genetic evidence indicates a requirement for cyclin D1/Cdk4 compl

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25

Negishi, Masahiko, Kaoru Kobayashi, Tsutomu Sakuma, and Tatsuya Sueyoshi. "Nuclear receptor phosphorylation in xenobiotic signal transduction." Journal of Biological Chemistry 295, no. 45 (2020): 15210–25. http://dx.doi.org/10.1074/jbc.rev120.007933.

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Nuclear pregnane X receptor (PXR, NR1I2) and constitutive active/androstane receptor (CAR, NR1I3) are nuclear receptors characterized in 1998 by their capability to respond to xenobiotics and activate cytochrome P450 (CYP) genes. An anti-epileptic drug, phenobarbital (PB), activates CAR and its target CYP2B genes, whereas PXR is activated by drugs such as rifampicin and statins for the CYP3A genes. Inevitably, both nuclear receptors have been investigated as ligand-activated nuclear receptors by identifying and characterizing xenobiotics and therapeutics that directly bind CAR and/or PXR to ac

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26

Barbosa, Sónia, Suzanne Carreira, and Peter O’Hare. "GSK-3–mediated phosphorylation couples ER–Golgi transport and nuclear stabilization of the CREB-H transcription factor to mediate apolipoprotein secretion." Molecular Biology of the Cell 28, no. 11 (2017): 1565–79. http://dx.doi.org/10.1091/mbc.e17-01-0075.

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CREB-H, an ER-anchored transcription factor, plays a key role in regulating secretion in metabolic pathways, particularly triglyceride homeostasis. It controls the production both of secretory pathway components and cargoes, including apolipoproteins ApoA-IV and ApoC-II, contributing to VLDL/HDL distribution and lipolysis. The key mechanism controlling CREB-H activity involves its ER retention and forward transport to the Golgi, where it is cleaved by Golgi-resident proteases, releasing the N-terminal product, which traffics to the nucleus to effect transcriptional responses. Here we show that

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27

Guo, Tianyao, Xiaowei Wang, Maoyu Li, et al. "Identification of Glioblastoma Phosphotyrosine-Containing Proteins with Two-Dimensional Western Blotting and Tandem Mass Spectrometry." BioMed Research International 2015 (2015): 1–21. http://dx.doi.org/10.1155/2015/134050.

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To investigate the presence of, and the potential biological roles of, protein tyrosine phosphorylation in the glioblastoma pathogenesis, two-dimensional gel electrophoresis- (2DGE-) based Western blotting coupled with liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) analysis was used to detect and identify the phosphotyrosine immunoreaction-positive proteins in a glioblastoma tissue. MS/MS and Mascot analyses were used to determine the phosphotyrosine sites of each phosphopeptide. Protein domain and motif analysis and systems pathway analysis were used to

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28

Stegert, Mario R., Alexander Hergovich, Rastislav Tamaskovic, Samuel J. Bichsel, and Brian A. Hemmings. "Regulation of NDR Protein Kinase by Hydrophobic Motif Phosphorylation Mediated by the Mammalian Ste20-Like Kinase MST3." Molecular and Cellular Biology 25, no. 24 (2005): 11019–29. http://dx.doi.org/10.1128/mcb.25.24.11019-11029.2005.

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ABSTRACT NDR protein kinases are involved in the regulation of cell cycle progression and morphology. NDR1/NDR2 protein kinase is activated by phosphorylation on the activation loop phosphorylation site Ser281/Ser282 and the hydrophobic motif phosphorylation site Thr444/Thr442. Autophosphorylation of NDR is responsible for phosphorylation on Ser281/Ser282, whereas Thr444/Thr442 is targeted by an upstream kinase. Here we show that MST3, a mammalian Ste20-like protein kinase, is able to phosphorylate NDR protein kinase at Thr444/Thr442. In vitro, MST3 selectively phosphorylated Thr442 of NDR2, r

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29

PARRA-PALAU, Josep L., Gert C. SCHEPER, Daniel E. HARPER, and Christopher G. PROUD. "The Drosophila protein kinase LK6 is regulated by ERK and phosphorylates the eukaryotic initiation factor eIF4E in vivo." Biochemical Journal 385, no. 3 (2005): 695–702. http://dx.doi.org/10.1042/bj20040769.

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In Drosophila cells, phosphorylation of eIF4E (eukaryotic initiation factor 4E) is required for growth and development. In Drosophila melanogaster, LK6 is the closest homologue of mammalian Mnk1 and Mnk2 [MAPK (mitogen-activated protein kinase) signal-integrating kinases 1 and 2 respectively] that phosphorylate mammalian eIF4E. Mnk1 is activated by both mitogen- and stress-activated signalling pathways [ERK (extracellular-signal-regulated kinase) and p38 MAPK], whereas Mnk2 contains a MAPK-binding motif that is selective for ERKs. LK6 possesses a binding motif similar to that in Mnk2. In the p

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Krantz, David E., Clarissa Waites, Viola Oorschot, et al. "A Phosphorylation Site Regulates Sorting of the Vesicular Acetylcholine Transporter to Dense Core Vesicles." Journal of Cell Biology 149, no. 2 (2000): 379–96. http://dx.doi.org/10.1083/jcb.149.2.379.

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Vesicular transport proteins package classical neurotransmitters for regulated exocytotic release, and localize to at least two distinct types of secretory vesicles. In PC12 cells, the vesicular acetylcholine transporter (VAChT) localizes preferentially to synaptic-like microvesicles (SLMVs), whereas the closely related vesicular monoamine transporters (VMATs) localize preferentially to large dense core vesicles (LDCVs). VAChT and the VMATs contain COOH-terminal, cytoplasmic dileucine motifs required for internalization from the plasma membrane. We now show that VAChT undergoes regulated phosp

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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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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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LIU, Yin, Caroline GRAHAM, Aiqun LI, Robert J. FISHER та Stephen SHAW. "Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-κB induction". Biochemical Journal 361, № 2 (2002): 255–65. http://dx.doi.org/10.1042/bj3610255.

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Protein kinase C (PKC)-theta, a member of the ‘novel’ subfamily of PKC isoforms, is of singular importance in transducing signals in T-lymphocytes. Since understanding of regulatory phosphorylation of novel PKCs is fragmentary and inconsistent with findings for ‘classical’ PKC isoforms, we investigated three potential phosphorylation sites on PKC-theta; in the activation loop (Thr538), turn motif (Ser676) and hydrophobic motif (Ser695). Combined evidence from phospho-specific antisera and MS demonstrates phosphorylation at all three sites. Unlike its closest paralogue, PKC-delta, lack of negat

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Barbosa, Sónia, Suzanne Carreira, Daniel Bailey, Fernando Abaitua, and Peter O'Hare. "Phosphorylation and SCF-mediated degradation regulate CREB-H transcription of metabolic targets." Molecular Biology of the Cell 26, no. 16 (2015): 2939–54. http://dx.doi.org/10.1091/mbc.e15-04-0247.

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CREB‑H, an endoplasmic reticulum–anchored transcription factor, plays a key role in regulating secretion and in metabolic and inflammatory pathways, but how its activity is modulated remains unclear. We examined processing of the nuclear active form and identified a motif around S87–S90 with homology to DSG-type phosphodegrons. We show that this region is subject to multiple phosphorylations, which regulate CREB-H stability by targeting it to the SCFFbw1aE3 ubiquitin ligase. Data from phosphatase treatment, use of phosophospecific antibody, and substitution of serine residues demonstrate phosp

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Mehta, Sohum, Huiming Li, Patrick G. Hogan, and Kyle W. Cunningham. "Domain Architecture of the Regulators of Calcineurin (RCANs) and Identification of a Divergent RCAN in Yeast." Molecular and Cellular Biology 29, no. 10 (2009): 2777–93. http://dx.doi.org/10.1128/mcb.01197-08.

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ABSTRACT Regulators of calcineurin (RCANs) in fungi and mammals have been shown to stimulate and inhibit calcineurin signaling in vivo through direct interactions with the catalytic subunit of the phosphatase. The dual effects of RCANs on calcineurin were examined by performing structure-function analyses on yeast Rcn1 and human RCAN1 (a.k.a. DSCR1, MCIP1, and calcipressin 1) proteins expressed at a variety of different levels in yeast. At high levels of expression, the inhibitory effects required a degenerate PxIxIT-like motif and a novel LxxP motif, which may be related to calcineurin-bindin

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Gógl, Gergő, Beáta Biri-Kovács, Fabien Durbesson, et al. "Rewiring of RSK–PDZ Interactome by Linear Motif Phosphorylation." Journal of Molecular Biology 431, no. 6 (2019): 1234–49. http://dx.doi.org/10.1016/j.jmb.2019.01.038.

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Jensen, Ann-Sofie Mølleskov, Alexander Hovard Sparre-Ulrich, Nicholas Davis-Poynter, and Mette Marie Rosenkilde. "Structural Diversity in Conserved Regions Like the DRY-Motif among Viral 7TM Receptors—A Consequence of Evolutionary Pressure?" Advances in Virology 2012 (2012): 1–15. http://dx.doi.org/10.1155/2012/231813.

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Several herpes- and poxviruses have captured chemokine receptors from their hosts and modified these to their own benefit. The human and viral chemokine receptors belong to class A 7 transmembrane (TM) receptors which are characterized by several structural motifs like the DRY-motif in TM3 and the C-terminal tail. In the DRY-motif, the arginine residue serves important purposes by being directly involved in G protein coupling. Interestingly, among the viral receptors there is a greater diversity in the DRY-motif compared to their endogenous receptor homologous. The C-terminal receptor tail con

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Nugent, J. H., C. E. Alfa, T. Young, and J. S. Hyams. "Conserved structural motifs in cyclins identified by sequence analysis." Journal of Cell Science 99, no. 3 (1991): 669–74. http://dx.doi.org/10.1242/jcs.99.3.669.

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Cyclins, as regulatory subunits of the ubiquitous p34cdc2 protein kinase, act as key controlling elements of the eukaryotic cell cycle. We have examined published sequences of A- and B-type cyclins for both amino acid and secondary structure homologies. In particular, we sought regions of homology outside the recognised area of sequence conservation known as the “cyclin box”, as well as conserved features predicted to lie at the protein surface. Our analysis demonstrates the existence of a number of islands of homology outside the cyclin box, and indicates candidate residues for phosphorylatio

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Sun, Xun, H. Jane Dyson, and Peter E. Wright. "A phosphorylation-dependent switch in the disordered p53 transactivation domain regulates DNA binding." Proceedings of the National Academy of Sciences 118, no. 1 (2020): e2021456118. http://dx.doi.org/10.1073/pnas.2021456118.

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The tumor-suppressor p53 is a critical regulator of the cellular response to DNA damage and is tightly regulated by posttranslational modifications. Thr55 in the AD2 interaction motif of the N-terminal transactivation domain functions as a phosphorylation-dependent regulatory switch that modulates p53 activity. Thr55 is constitutively phosphorylated, becomes dephosphorylated upon DNA damage, and is subsequently rephosphorylated to facilitate dissociation of p53 from promoters and inactivate p53-mediated transcription. Using NMR and fluorescence spectroscopy, we show that Thr55 phosphorylation

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Ren, Wen, Nur P. Damayanti, Xiaolei Wang, and Joseph M. K. Irudayaraj. "Kinase phosphorylation monitoring with i-motif DNA cross-linked SERS probes." Chemical Communications 52, no. 2 (2016): 410–13. http://dx.doi.org/10.1039/c5cc06566f.

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Wade, Ramon, and Scott Vande Pol. "Minimal features of paxillin that are required for the tyrosine phosphorylation of focal adhesion kinase." Biochemical Journal 393, no. 2 (2005): 565–73. http://dx.doi.org/10.1042/bj20051241.

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Tyrosine phosphorylation of FAK (focal adhesion kinase) regulates signalling that results from the interaction of integrins with extracellular matrix and growth factor receptors. A critical step in this process is the phosphorylation of Tyr397 of FAK, which creates a binding site for Src family kinases, PI3K (phosphoinositide 3-kinase) and Shc (Src homology and collagen homology). An intact Tyr397 site is required for FAK-mediated regulation of cell migration, survival signals and full responsiveness to soluble growth factors. We showed previously that the adaptor protein paxillin is required

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Kim, Hak Rim, Cynthia Gallant, and Kathleen G. Morgan. "Regulation of PKC Autophosphorylation by Calponin in Contractile Vascular Smooth Muscle Tissue." BioMed Research International 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/358643.

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Protein kinase C (PKC) is a key enzyme involved in agonist-induced smooth muscle contraction. In some cases, regulatory phosphorylation of PKC is required for full activation of the enzyme. However, this issue has largely been ignored with respect to PKC-dependent regulation of contractile vascular smooth muscle (VSM) contractility. The first event in PKC regulation is a transphosphorylation by PDK at a conserved threonine in the activation loop of PKC, followed by the subsequent autophosphorylation at the turn motif and hydrophobic motif sites. In the present study, we determined whether phos

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Tridandapani, S., T. Kelley, M. Pradhan, D. Cooney, L. B. Justement, and K. M. Coggeshall. "Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif." Molecular and Cellular Biology 17, no. 8 (1997): 4305–11. http://dx.doi.org/10.1128/mcb.17.8.4305.

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Recently, we and others have demonstrated that negative signaling in B cells selectively induces the tyrosine phosphorylation of a novel inositol polyphosphate phosphatase, p145SHIP. In this study, we present data indicating that p145SHIP binds directly a phosphorylated motif, immunoreceptor tyrosine-based inhibition motif (ITIM), present in the cytoplasmic domain of Fc gammaRIIB1. Using recombinant SH2 domains, we show that binding is mediated via the Src homology region 2 (SH2)-containing inositol phosphatase (SHIP) SH2 domain. SHIP also bound to a phosphopeptide derived from CD22, raising t

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Sun, X. J., D. L. Crimmins, M. G. Myers, M. Miralpeix, and M. F. White. "Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1." Molecular and Cellular Biology 13, no. 12 (1993): 7418–28. http://dx.doi.org/10.1128/mcb.13.12.7418.

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IRS-1 (insulin receptor substrate 1) is a principal insulin receptor substrate that undergoes tyrosine phosphorylation during insulin stimulation. It contains over 20 potential tyrosine phosphorylation sites, and we suspect that multiple insulin signals are enabled when the activated insulin receptor kinase phosphorylates several of them. Tyrosine-phosphorylated IRS-1 binds specifically to various cellular proteins containing Src homology 2 (SH2) domains (SH2 proteins). We identified some of the tyrosine residues of IRS-1 that undergo insulin-stimulated phosphorylation by the purified insulin

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Sun, X. J., D. L. Crimmins, M. G. Myers, M. Miralpeix, and M. F. White. "Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1." Molecular and Cellular Biology 13, no. 12 (1993): 7418–28. http://dx.doi.org/10.1128/mcb.13.12.7418-7428.1993.

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IRS-1 (insulin receptor substrate 1) is a principal insulin receptor substrate that undergoes tyrosine phosphorylation during insulin stimulation. It contains over 20 potential tyrosine phosphorylation sites, and we suspect that multiple insulin signals are enabled when the activated insulin receptor kinase phosphorylates several of them. Tyrosine-phosphorylated IRS-1 binds specifically to various cellular proteins containing Src homology 2 (SH2) domains (SH2 proteins). We identified some of the tyrosine residues of IRS-1 that undergo insulin-stimulated phosphorylation by the purified insulin

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Wohlschlegel, James A., Brian T. Dwyer, David Y. Takeda, and Anindya Dutta. "Mutational Analysis of the Cy Motif from p21 Reveals Sequence Degeneracy and Specificity for Different Cyclin-Dependent Kinases." Molecular and Cellular Biology 21, no. 15 (2001): 4868–74. http://dx.doi.org/10.1128/mcb.21.15.4868-4874.2001.

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ABSTRACT Inhibitors, activators, and substrates of cyclin-dependent kinases (cdks) utilize a cyclin-binding sequence, known as a Cy or RXL motif, to bind directly to the cyclin subunit. Alanine scanning mutagenesis of the Cy motif of the cdk inhibitor p21 revealed that the conserved arginine or leucine (constituting the conserved RXL sequence) was important for p21's ability to inhibit cyclin E-cdk2 activity. Further analysis of mutant Cy motifs showed, however, that RXL was neither necessary nor sufficient for a functional cyclin-binding motif. Replacement of either of these two residues with

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Van den Herik-Oudijk, IE, PJ Capel, T. van der Bruggen, and JG Van de Winkel. "Identification of signaling motifs within human Fc gamma RIIa and Fc gamma RIIb isoforms." Blood 85, no. 8 (1995): 2202–11. http://dx.doi.org/10.1182/blood.v85.8.2202.bloodjournal8582202.

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To assess the functional capacity of the heterogeneous Fc gamma RII (CD32) family and to identify critical regions for functioning, we generated a panel of B-cell transfectants. The Fc gamma R-negative B-cell line IIA1.6 was transfected with wild-type or mutant human Fc gamma RIIa and IIb molecules. Solely Fc gamma RIIa-expressing IIA1.6 cells were capable of phagocytosing opsonized Staphylococcus aureus bacteria, and cross-linking of Fc gamma RIIa triggered a rapid induction of tyrosine phosphorylation after 20 seconds. Analysis of Fc gamma RIIa mutants identified the immunoreceptor tyrosine-

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Boelaert, K., R. Yu, L. A. Tannahill, et al. "PTTG’s C-terminal PXXP motifs modulate critical cellular processes in vitro." Journal of Molecular Endocrinology 33, no. 3 (2004): 663–77. http://dx.doi.org/10.1677/jme.1.01606.

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Human pituitary tumor-transforming gene (PTTG), known also as securin, is a multifunctional protein implicated in the control of mitosis and the pathogenesis of thyroid, colon, oesophageal and other tumour types. Critical to PTTG function is a C-terminal double PXXP motif, forming a putative SH3-interacting domain and housing the gene’s sole reported phosphorylation site. The exact role of phosphorylation and PXXP structure in the modulation of PTTG action in vitro remains poorly understood. We therefore examined the mitotic, transformation, proliferation and transactivation function of the C-

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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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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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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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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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