Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction (Q28272714)

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M Karas

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Y Zick

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D LeRoith

Journal of Biological Chemistry

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language of work or name

English

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publication date

12 June 1998

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published in

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volume

273

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issue

24

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page(s)

14780-7

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cites work

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Insulin receptor substrate 1 and 2 (IRS1 and IRS2): what a tangled web we weave

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Differential signaling by insulin receptor substrate 1 (IRS-1) and IRS-2 in IRS-1-deficient cells

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The function of GRB2 in linking the insulin receptor to Ras signaling pathways

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Localization of the Insulin-like Growth Factor I Receptor Binding Sites for the SH2 Domain Proteins p85, Syp, and GTPase Activating Protein

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Two species of human CRK cDNA encode proteins with distinct biological activities

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CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells

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The Proto-oncogene Product c-Crk Associates with Insulin Receptor Substrate-1 and 4PS

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A novel viral oncogene with structural similarity to phospholipase C

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Both the SH2 and SH3 domains of human CRK protein are required for neuronal differentiation of PC12 cells

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CrkII signals from epidermal growth factor receptor to Ras

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Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk

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Downstream of Crk adaptor signaling pathway: activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G.

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A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic kidney cells is a new member of the insulin receptor substrate family

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In vivo regulation of CrkII and CrkL proto-oncogenes in the uterus by insulin-like growth factor-I. Differential effects on tyrosine phosphorylation and association with paxillin

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Crk interacts with tyrosine-phosphorylated p116 upon T cell activation

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Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor

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The CRKL adaptor protein transforms fibroblasts and functions in transformation by the BCR-ABL oncogene

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Tyrosine 207 in CRKL is the BCR/ABL phosphorylation site

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Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins

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DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane

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Guanine-nucleotide exchange protein C3G activates JNK1 by a ras-independent mechanism. JNK1 activation inhibited by kinase negative forms of MLK3 and DLK mixed lineage kinases

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Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL)

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The type I interferon receptor mediates tyrosine phosphorylation of the CrkL adaptor protein

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Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells

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Emerging components of the Crk oncogene product: the first identified adaptor protein

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CRKL links p210BCR/ABL with paxillin in chronic myelogenous leukemia cells

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pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk

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Src kinase plays an essential role in integrin-mediated tyrosine phosphorylation of Crk-associated substrate p130Cas

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Nerve growth factor stimulates the tyrosine phosphorylation of endogenous Crk-II and augments its association with p130Cas in PC-12 cells

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Interaction of insulin receptor substrate-2 (IRS-2) with the insulin and insulin-like growth factor I receptors. Evidence for two distinct phosphotyrosine-dependent interaction domains within IRS-2

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Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786

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Interaction in vitro of the product of the c-Crk-II proto-oncogene with the insulin-like growth factor I receptor

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The BCR/ABL oncogene alters interaction of the adapter proteins CRKL and CRK with cellular proteins

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