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Investigation of factors that influence phosphorylation of pp60c-src on tyrosine 527.

作者信息

Schuh S M, Brugge J S

机构信息

Department of Microbiology, State University of New York, Stony Brook 11794.

出版信息

Mol Cell Biol. 1988 Jun;8(6):2465-71. doi: 10.1128/mcb.8.6.2465-2471.1988.

DOI:10.1128/mcb.8.6.2465-2471.1988
PMID:2457151
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC363446/
Abstract

Phosphorylation at tyrosine 527 of the proto-oncogene product, pp60c-src, has been proposed to decrease the tyrosine kinase activity of the enzyme. We have investigated potential factors that might influence phosphorylation at this site by making mutant variants of the pp60c-src protein. By effectively eliminating the site of N-terminal myristylation, we demonstrated that stable membrane association is not necessary for tyrosine 527 phosphorylation. Furthermore, mutational elimination of the enzymatic activity of this mutant pp60c-src protein did not alter the efficiency of phosphorylation at tyrosine 527. These data are consistent with the proposal that pp60c-src may be phosphorylated at tyrosine 527 by a cellular tyrosine kinase distinct from pp60c-src. In addition, using detergent-permeabilized cells, we established conditions that allow efficient phosphorylation of tyrosine 527 in vitro.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/ee1743a23acb/molcellb00066-0213-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/5ae5335d8505/molcellb00066-0211-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/e31b3464991b/molcellb00066-0211-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/1cc8c3544898/molcellb00066-0212-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/2c906ce6349a/molcellb00066-0213-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/ee1743a23acb/molcellb00066-0213-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/5ae5335d8505/molcellb00066-0211-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/e31b3464991b/molcellb00066-0211-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/1cc8c3544898/molcellb00066-0212-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/2c906ce6349a/molcellb00066-0213-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/44fb/363446/ee1743a23acb/molcellb00066-0213-b.jpg

相似文献

1
Investigation of factors that influence phosphorylation of pp60c-src on tyrosine 527.
Mol Cell Biol. 1988 Jun;8(6):2465-71. doi: 10.1128/mcb.8.6.2465-2471.1988.
2
Myristylation and amino-terminal phosphorylation are required for activation of pp60c-src during mitosis.在有丝分裂过程中,pp60c-src的激活需要肉豆蔻酰化和氨基末端磷酸化。
Oncogene. 1993 Mar;8(3):575-81.
3
The sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-src.蛋白激酶C的磷酸化位点和完整的SH2结构域对于过表达c-src的细胞中对β-肾上腺素能激动剂增强的反应是必需的。
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Biochemistry. 1996 Sep 10;35(36):11874-87. doi: 10.1021/bi9603940.
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Tyr527 is phosphorylated in pp60c-src: implications for regulation.酪氨酸527在pp60c-src中被磷酸化:对调节的影响。
Science. 1986 Mar 21;231(4744):1431-4. doi: 10.1126/science.2420005.

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J Proteome Res. 2008 Sep;7(9):3900-10. doi: 10.1021/pr800198w. Epub 2008 Aug 13.
2
Complex formation with focal adhesion kinase: A mechanism to regulate activity and subcellular localization of Src kinases.与粘着斑激酶形成复合物:一种调节Src激酶活性和亚细胞定位的机制。
Mol Biol Cell. 1999 Oct;10(10):3489-505. doi: 10.1091/mbc.10.10.3489.
3
Inhibition of src family kinases by a combinatorial action of 5'-AMP and small heat shock proteins, identified from the adult heart.

本文引用的文献

1
Identification and characterization of cellular targets for tyrosine protein kinases.酪氨酸蛋白激酶细胞靶点的鉴定与表征
J Biol Chem. 1983 Jan 25;258(2):1108-15.
2
Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein.肉豆蔻酸在合成过程中或合成后立即与劳氏肉瘤病毒的转化蛋白相连,并以可溶性和膜结合形式存在于该蛋白中。
Mol Cell Biol. 1984 Dec;4(12):2697-704. doi: 10.1128/mcb.4.12.2697-2704.1984.
3
Expression of v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src.
5'-AMP与从小鼠成年心脏中鉴定出的小分子热休克蛋白的联合作用对src家族激酶的抑制作用
Mol Cell Biol. 1999 Oct;19(10):6858-71. doi: 10.1128/MCB.19.10.6858.
4
Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets.Csk同源激酶(Chk/Hyl)的易位控制凝血酶刺激的血小板中CD36锚定的Lyn酪氨酸激酶的活性。
EMBO J. 1997 May 1;16(9):2342-51. doi: 10.1093/emboj/16.9.2342.
5
Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae.C末端Src激酶对c-Src活性的抑制涉及c-Src的SH2和SH3结构域:酿酒酵母分析
Mol Cell Biol. 1993 Sep;13(9):5290-300. doi: 10.1128/mcb.13.9.5290-5300.1993.
6
Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src.Csk对c-Src活性的抑制需要Src的SH2和SH3结构域。
EMBO J. 1993 Jul;12(7):2625-34. doi: 10.1002/j.1460-2075.1993.tb05923.x.
7
Redistribution of activated pp60c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets.在凝血酶刺激的血小板中,活化的pp60c-src重新分布至整合素依赖性细胞骨架复合物。
Mol Cell Biol. 1993 Mar;13(3):1863-71. doi: 10.1128/mcb.13.3.1863-1871.1993.
8
Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis.在有丝分裂过程中,肉豆蔻酰化对于Tyr-527去磷酸化和pp60c-src的激活是必需的。
Mol Cell Biol. 1993 Mar;13(3):1464-70. doi: 10.1128/mcb.13.3.1464-1470.1993.
9
Differential effects of phosphotyrosine phosphatase expression on hormone-dependent and independent pp60c-src activity.磷酸酪氨酸磷酸酶表达对激素依赖性和非依赖性pp60c-src活性的不同影响。
Mol Cell Biochem. 1994 Oct 26;139(2):167-75. doi: 10.1007/BF01081740.
10
Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.在c-Src的抑制和有丝分裂激活过程中,Csk的Src同源2结构域与酪氨酸磷酸化蛋白结合的分析。
Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3984-8. doi: 10.1073/pnas.91.9.3984.
v-src和鸡c-src在大鼠细胞中的表达证明了pp60v-src和pp60c-src之间的质的差异。
Cell. 1984 May;37(1):131-9. doi: 10.1016/0092-8674(84)90308-8.
4
Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses.识别禽肉瘤病毒转化蛋白的单克隆抗体的分离
J Virol. 1983 Nov;48(2):352-60. doi: 10.1128/JVI.48.2.352-360.1983.
5
Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus.与劳氏肉瘤病毒src基因同源的细胞基因的结构与序列以及产生转化病毒的机制。
Cell. 1983 Mar;32(3):881-90. doi: 10.1016/0092-8674(83)90073-9.
6
Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex.劳氏肉瘤病毒转化蛋白与两种细胞磷蛋白之间的相互作用:该复合物的周转和分布分析。
Mol Cell Biol. 1983 Jan;3(1):9-19. doi: 10.1128/mcb.3.1.9-19.1983.
7
Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.酪氨酸磷酸化位点周围氨基酸序列的分析
Proc Natl Acad Sci U S A. 1982 Feb;79(4):973-7. doi: 10.1073/pnas.79.4.973.
8
Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src).劳氏肉瘤病毒转化蛋白(pp60v-src)及其正常细胞同源物(pp60c-src)中酪氨酸磷酸化位点的鉴定
Proc Natl Acad Sci U S A. 1981 Oct;78(10):6013-7. doi: 10.1073/pnas.78.10.6013.
9
The protein encoded by the transforming gene of avian sarcoma virus (pp60src) and a homologous protein in normal cells (pp60proto-src) are associated with the plasma membrane.禽肉瘤病毒转化基因编码的蛋白质(pp60src)和正常细胞中的同源蛋白质(pp60原癌基因src)与质膜相关。
Proc Natl Acad Sci U S A. 1980 Jul;77(7):3783-7. doi: 10.1073/pnas.77.7.3783.
10
A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation.p60src的N端的一段短序列对于p60src的豆蔻酰化、膜结合以及细胞转化是必需的。
Mol Cell Biol. 1984 Sep;4(9):1834-42. doi: 10.1128/mcb.4.9.1834-1842.1984.