Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin - Wikidata - wikimedia - TriplyDB

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

http://www.wikidata.org/entity/Q28264272

about

RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1 Protein tyrosine phosphatases expression during development of mouse superior colliculus Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts.Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion 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 Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain Phosphatidylinositol 3,4,5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin Alpha4 integrins and the immune response PTEN regulates tumor cell adhesion of colon carcinoma cells under dynamic conditions of fluid flow The paxillin LD motifs A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration A new member of the LIM protein family binds to filamin B and localizes at stress fibers Regulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST Regulation of cell adhesion by protein-tyrosine phosphatases. I. Cell-matrix adhesion PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates NMR structure of integrin α4 cytosolic tail and its interactions with paxillin The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling Regulation of the Src kinase-associated phosphoprotein 55 homologue by the protein tyrosine phosphatase PTP-PEST in the control of cell motility Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness.Paxillin: a focal adhesion-associated adaptor protein.Activation of the focal adhesion kinase signaling pathway by structural alterations in the carboxyl-terminal region of c-Crk II.Interactions between E6, FAK, and GIT1 at paxillin LD4 are necessary for transformation by bovine papillomavirus 1 E6 Paxillin enables attachment-independent tyrosine phosphorylation of focal adhesion kinase and transformation by RAS.Transformation by bovine papillomavirus type 1 E6 requires paxillin.FERM domain interaction promotes FAK signaling.Paxillin binding is not the sole determinant of focal adhesion localization or dominant-negative activity of focal adhesion kinase/focal adhesion kinase-related nonkinase Caspase-3 regulates catalytic activity and scaffolding functions of the protein tyrosine phosphatase PEST, a novel modulator of the apoptotic response.PTP1B regulates neurite extension mediated by cell-cell and cell-matrix adhesion molecules.Identification of a filamin docking site on PTP-PEST.Echistatin inhibits pp125FAK autophosphorylation, paxillin phosphorylation and pp125FAK-paxillin interaction in fibronectin-adherent melanoma cells.PTEN gene and integrin signaling in cancer.Roles of protein tyrosine phosphatases in cell migration and adhesion.c-Src-mediated phosphorylation of TRIP6 regulates its function in lysophosphatidic acid-induced cell migration.Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells.Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK Serine phosphorylation regulates paxillin turnover during cell migration.The interplay between Src and integrins in normal and tumor biology.Impaired integrin-mediated adhesion and signaling in fibroblasts expressing a dominant-negative mutant PTP1B.

P2860

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P2860

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

http://www.wikidata.org/entity/Q28264272

description

1998 nî lūn-bûn

@nan

1998 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի մարտին հրատարակված գիտական հոդված

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1998年の論文

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1998年学术文章

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1998年学术文章

@zh-cn

1998年学术文章

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1998年学术文章

@zh-my

1998年学术文章

@zh-sg

1998年學術文章

@yue

name

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@ast

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@en

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@nl

type

label

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@ast

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@en

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@nl

prefLabel

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@ast

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@en

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@nl

P1433

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P2860

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P356

JBC.273.11.6474

P1433

Journal of Biological Chemistry

P1476

Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin

@en

P2093

A Veillette

http://www.w3.org/2001/XMLSchema#string

G Schneider

http://www.w3.org/2001/XMLSchema#string

J F Cloutier

http://www.w3.org/2001/XMLSchema#string

M D Schaller

http://www.w3.org/2001/XMLSchema#string

Y Shen

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P2860

Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition

Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases

Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)

Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases.

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

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

Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly

Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins

Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST.

Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions.

P304

6474-81

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scholarly article

P356

10.1074/JBC.273.11.6474

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P407

P433

11

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P478

273

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P577

1998-03-13T00:00:00Z

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P698

9497381

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