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多瘤病毒中T抗原-酪氨酸激酶复合物中细胞和病毒成分的化学计量学。

Stoichiometry of cellular and viral components in the polyomavirus middle-T antigen-tyrosine kinase complex.

作者信息

Cheng S H, Espino P C, Marshall J, Harvey R, Smith A E

机构信息

Laboratory of Cellular Regulation, Genzyme Corporation, Framingham, Massachusetts 01701.

出版信息

Mol Cell Biol. 1990 Oct;10(10):5569-74. doi: 10.1128/mcb.10.10.5569-5574.1990.

DOI:10.1128/mcb.10.10.5569-5574.1990
PMID:1697932
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC361277/
Abstract

Our results indicate that only one type of tyrosine kinase is present within each middle-T antigen-tyrosine kinase complex, suggesting that middle-T antigen forms separate complexes with different tyrosine kinases. Furthermore, we determined that there is only one molecule of middle-T antigen within any one of these complexes. We interpret this to mean that in any given cell, polyomavirus transformation involves, at least in part, the simultaneous deregulation of a number of separate pathways controlling cellular proliferation. Finally, we also demonstrate that the separate middle-T:pp60c-src and middle-T:pp59c-fyn complexes are each able to interact with the same cellular p81/85-kDa phosphoprotein, a possible component of the phosphatidylinositol kinase.

摘要

我们的结果表明,每个中T抗原 - 酪氨酸激酶复合物中仅存在一种类型的酪氨酸激酶,这表明中T抗原与不同的酪氨酸激酶形成单独的复合物。此外,我们确定在这些复合物中的任何一个中仅存在一个中T抗原分子。我们将此解释为,在任何给定细胞中,多瘤病毒转化至少部分涉及同时解除对许多控制细胞增殖的独立途径的调节。最后,我们还证明,单独的中T:pp60c-src和中T:pp59c-fyn复合物各自能够与相同的细胞p81/85-kDa磷蛋白相互作用,该磷蛋白可能是磷脂酰肌醇激酶的一个组分。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f563/361277/7fca5583e9cd/molcellb00046-0556-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f563/361277/72fd605cb8e5/molcellb00046-0554-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f563/361277/1fd9c1c7c187/molcellb00046-0555-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f563/361277/7fca5583e9cd/molcellb00046-0556-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f563/361277/72fd605cb8e5/molcellb00046-0554-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f563/361277/1fd9c1c7c187/molcellb00046-0555-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f563/361277/7fca5583e9cd/molcellb00046-0556-a.jpg

相似文献

1
Stoichiometry of cellular and viral components in the polyomavirus middle-T antigen-tyrosine kinase complex.多瘤病毒中T抗原-酪氨酸激酶复合物中细胞和病毒成分的化学计量学。
Mol Cell Biol. 1990 Oct;10(10):5569-74. doi: 10.1128/mcb.10.10.5569-5574.1990.
2
An 81 kd protein complexed with middle T antigen and pp60c-src: a possible phosphatidylinositol kinase.一种与中T抗原和pp60c-src复合的81kd蛋白质:一种可能的磷脂酰肌醇激酶。
Cell. 1987 Sep 25;50(7):1031-7. doi: 10.1016/0092-8674(87)90169-3.
3
Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus.针对人类c-fyn基因产物的肽抗体表明,pp59c-fyn能够与多瘤病毒的中间T抗原形成复合物。
EMBO J. 1988 Dec 1;7(12):3845-55. doi: 10.1002/j.1460-2075.1988.tb03270.x.
4
Induction of tumor formation and cell transformation by polyoma middle T antigen in the absence of Src.在缺乏Src的情况下,多瘤病毒中T抗原诱导肿瘤形成和细胞转化。
Oncogene. 1993 Sep;8(9):2521-9.
5
Further characterisation of the complex containing middle T antigen and pp60.
Curr Top Microbiol Immunol. 1989;144:121-8. doi: 10.1007/978-3-642-74578-2_15.
6
Transformation by polyoma virus middle T antigen.多瘤病毒中T抗原介导的转化
Cancer Surv. 1986;5(2):173-82.
7
Structural elements that regulate pp59c-fyn catalytic activity, transforming potential, and ability to associate with polyomavirus middle-T antigen.调节pp59c-fyn催化活性、转化潜能以及与多瘤病毒中T抗原结合能力的结构元件。
J Virol. 1991 Jan;65(1):170-9. doi: 10.1128/JVI.65.1.170-179.1991.
8
The amino-terminal half of pp59c-fyn contains sequences necessary for formation of a 75 kDa form and also repressive elements absent in pp60c-src.pp59c-fyn的氨基末端一半包含形成75 kDa形式所必需的序列,并且还包含pp60c-src中不存在的抑制元件。
Oncogene. 1992 Feb;7(2):317-22.
9
Mutation of a cysteine residue in polyomavirus middle T antigen abolishes interactions with protein phosphatase 2A, pp60c-src, and phosphatidylinositol-3 kinase, activation of c-fos expression, and cellular transformation.多瘤病毒中T抗原的一个半胱氨酸残基发生突变,会消除与蛋白磷酸酶2A、pp60c-src和磷脂酰肌醇-3激酶的相互作用,c-fos表达的激活以及细胞转化。
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10
12-O-tetradecanoylphorbol-13-acetate stimulates phosphorylation of the 58,000-Mr form of polyomavirus middle T antigen in vivo: implications for a possible role of protein kinase C in middle T function.12 - O - 十四烷酰佛波醇 - 13 - 乙酸酯在体内刺激多瘤病毒中T抗原58,000 - Mr形式的磷酸化:对蛋白激酶C在中T功能中可能作用的启示。
J Virol. 1986 May;58(2):239-46. doi: 10.1128/JVI.58.2.239-246.1986.

引用本文的文献

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Lessons in signaling and tumorigenesis from polyomavirus middle T antigen.多瘤病毒中T抗原在信号传导与肿瘤发生方面的启示
Microbiol Mol Biol Rev. 2009 Sep;73(3):542-63, Table of Contents. doi: 10.1128/MMBR.00009-09.
2
Natural biology of polyomavirus middle T antigen.多瘤病毒中T抗原的自然生物学特性
Microbiol Mol Biol Rev. 2001 Jun;65(2):288-318 ; second and third pages, table of contents. doi: 10.1128/MMBR.65.2.288-318.2001.
3
Multimerization of polyomavirus middle-T antigen.多瘤病毒中T抗原的多聚化

本文引用的文献

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Polyomavirus middle-T antigen associates with the kinase domain of Src-related tyrosine kinases.多瘤病毒中T抗原与Src相关酪氨酸激酶的激酶结构域相关联。
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Interleukin 2- and polyomavirus middle T antigen-induced modification of phosphatidylinositol 3-kinase activity in activated T lymphocytes.白细胞介素2和多瘤病毒中T抗原诱导活化T淋巴细胞中磷脂酰肌醇3激酶活性的改变。
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Transformation-defective mutants of polyomavirus middle T antigen associate with phosphatidylinositol 3-kinase (PI 3-kinase) but are unable to maintain wild-type levels of PI 3-kinase products in intact cells.多瘤病毒中T抗原的转化缺陷型突变体与磷脂酰肌醇3激酶(PI 3激酶)相关联,但无法在完整细胞中维持PI 3激酶产物的野生型水平。
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针对劳氏肉瘤病毒pp60src的单克隆抗体可与源自禽类和哺乳动物的具有酶活性的细胞pp60src发生反应。
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An antibody to a synthetic peptide recognizes polyomavirus middle-T antigen and reveals multiple in vitro tyrosine phosphorylation sites.一种针对合成肽的抗体可识别多瘤病毒中T抗原,并揭示多个体外酪氨酸磷酸化位点。
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Enhancement of cellular src gene product associated tyrosyl kinase activity following polyoma virus infection and transformation.多瘤病毒感染和转化后细胞src基因产物相关酪氨酸激酶活性的增强。
Cell. 1984 Oct;38(3):767-77. doi: 10.1016/0092-8674(84)90272-1.
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Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain.由在羧基末端调节结构域发生突变的pp60c-src引起的细胞转化。
Cell. 1987 Apr 10;49(1):83-91. doi: 10.1016/0092-8674(87)90758-6.
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Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src.酪氨酸磷酸化调节pp60c-src的生化和生物学特性。
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Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation.通过其酪氨酸磷酸化主要位点的突变激活和抑制pp60c-src转化能力。
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Identification and characterization of p59fyn (a src-like protein tyrosine kinase) in normal and polyoma virus transformed cells.正常细胞和多瘤病毒转化细胞中p59fyn(一种src样蛋白酪氨酸激酶)的鉴定与特性分析
EMBO J. 1988 Dec 1;7(12):3837-44. doi: 10.1002/j.1460-2075.1988.tb03269.x.
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Association of the polyomavirus middle-T antigen with c-yes protein.
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