Close linkage of p130 and Ft1 is conserved among mammals.

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作者信息

Lesche R, Rüther U

机构信息

Institut für Molekularbiologie, Medizinische Hochschule Hannover, Germany.

出版信息

Mamm Genome. 1998 Mar;9(3):253-5. doi: 10.1007/s003359900737.

DOI:10.1007/s003359900737

PMID:9501314

Abstract

摘要

相似文献

Close linkage of p130 and Ft1 is conserved among mammals.

Mamm Genome. 1998 Mar;9(3):253-5. doi: 10.1007/s003359900737.

Ft1, a novel gene related to ubiquitin-conjugating enzymes, is deleted in the Fused toes mouse mutation.Ft1是一种与泛素结合酶相关的新基因，在融合趾小鼠突变中缺失。

Mamm Genome. 1997 Dec;8(12):879-83. doi: 10.1007/s003359900604.

A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner.一种新型信号分子p130在体内以酪氨酸磷酸化依赖的方式与v-Crk和v-Src形成稳定复合物。

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Cloning and characterization of the rat p130, a member of the retinoblastoma gene family.

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p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene.在由BCR/ABL致癌基因转化的造血细胞中，p130CAS与衔接蛋白CRKL形成信号复合物。

J Biol Chem. 1996 Oct 11;271(41):25198-203. doi: 10.1074/jbc.271.41.25198.

Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells.Crk相关底物p130（Cas）与肾囊肿蛋白相互作用，且这两种蛋白均定位于极化上皮细胞的细胞间连接部位。

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Insulin stimulates the tyrosine dephosphorylation of docking protein p130cas (Crk-associated substrate), promoting the switch of the adaptor protein crk from p130cas to newly phosphorylated insulin receptor substrate-1.胰岛素刺激对接蛋白p130cas（Crk相关底物）的酪氨酸去磷酸化，促使衔接蛋白crk从p130cas转换至新磷酸化的胰岛素受体底物-1。

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Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain.对接/衔接蛋白HEF1通过羧基末端螺旋-环-螺旋结构域发生二聚化。

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Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST.桩蛋白完整的LIM 3和LIM 4结构域是其与蛋白酪氨酸磷酸酶-PEST的一个新的多聚脯氨酸区域（Pro 2）结合所必需的。

J Biol Chem. 1999 Jul 16;274(29):20550-60. doi: 10.1074/jbc.274.29.20550.

Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas.粘着斑激酶与Crk相关酪氨酸激酶底物p130Cas之间的相互作用。

Proc Natl Acad Sci U S A. 1995 Nov 7;92(23):10678-82. doi: 10.1073/pnas.92.23.10678.

本文引用的文献

Ft1, a novel gene related to ubiquitin-conjugating enzymes, is deleted in the Fused toes mouse mutation.Ft1是一种与泛素结合酶相关的新基因，在融合趾小鼠突变中缺失。

Mamm Genome. 1997 Dec;8(12):879-83. doi: 10.1007/s003359900604.

Cloning and characterization of the rat p130, a member of the retinoblastoma gene family.

Biochim Biophys Acta. 1997 Jul 10;1361(1):20-7. doi: 10.1016/s0925-4439(97)00037-9.

Molecular cloning, expression, and developmental characterization of the murine retinoblastoma-related gene Rb2/p130.小鼠视网膜母细胞瘤相关基因Rb2/p130的分子克隆、表达及发育特征分析

Cell Growth Differ. 1995 Dec;6(12):1659-64.

Retinoblastoma protein family in cell cycle and cancer: a review.细胞周期与癌症中的视网膜母细胞瘤蛋白家族：综述

J Cell Biochem. 1996 Sep 1;62(3):418-30. doi: 10.1002/(SICI)1097-4644(199609)62:3%3C418::AID-JCB12%3E3.0.CO;2-E.

Activity of the retinoblastoma family proteins, pRB, p107, and p130, during cellular proliferation and differentiation.视网膜母细胞瘤家族蛋白pRB、p107和p130在细胞增殖和分化过程中的活性。

Crit Rev Biochem Mol Biol. 1996 Jun;31(3):237-71. doi: 10.3109/10409239609106585.

G1 cyclin/CDK-independent phosphorylation and accumulation of p130 during the transition from G1 to G0 lead to its association with E2F-4.在从G1期向G0期转变过程中，p130的G1期细胞周期蛋白/细胞周期蛋白依赖性激酶非依赖性磷酸化和积累导致其与E2F-4结合。

Oncogene. 1996 Jul 18;13(2):237-46.

Cloning and expression of the Rb-related mouse p130 mRNA.

Oncogene. 1996 Apr 4;12(7):1433-40.

Molecular cloning and developmental expression of mouse p130, a member of the retinoblastoma gene family.

J Biol Chem. 1996 Apr 19;271(16):9567-72.

Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain.一种与E1A转化结构域结合的视网膜母细胞瘤基因家族新成员（pRb2）的克隆。

Oncogene. 1993 Sep;8(9):2561-6.

Cell cycle-specific association of E2F with the p130 E1A-binding protein.E2F与p130 E1A结合蛋白的细胞周期特异性关联。

Genes Dev. 1993 Dec;7(12A):2392-404. doi: 10.1101/gad.7.12a.2392.

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