Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397. (Q44172481)

30 November 2017

title

Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397. (English)

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30 November 2017

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Tzeng-Horng Leu

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30 November 2017

Ming-Chei Maa

series ordinal

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30 November 2017

language of work or name

English

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publication date

1 October 2002

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30 November 2017

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30 November 2017

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30 November 2017

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30 November 2017

page(s)

6992-7000

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Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase

30 November 2017

cites work

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Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases

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Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase

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Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK.

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Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin

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Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase

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Autoregulatory mechanisms in protein-tyrosine kinases

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Protein kinase C is regulated in vivo by three functionally distinct phosphorylations

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Activation of protein kinase C by tyrosine phosphorylation in response to H2O2.

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Signaling by integrin receptors

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions

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Vanadate-dependent FAK activation is accomplished by the sustained FAK Tyr-576/577 phosphorylation

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Enhancement of tyrosyl phosphorylation and protein expression of eps8 by v-Src

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Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2.

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pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions

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Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

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Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase

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7 January 2021

Identifiers

DOI

10.1038/SJ.ONC.1205904

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30 November 2017

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