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

No abstract is available for this paper.

• Publication year

  1994

• Venue

  Nature

• Publication date

  1994-12-22

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1038/372786A0PMID 7997267
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Integrin-mediated cell adhesion activates mitogen-activated protein kinases.

  1994cited by this paper
• Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK

  1994cited by this paper
• Csk suppression of Src involves movement of Csk to sites of Src activity

  1994cited by this paper
• Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase.

  1994cited by this paper
• Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

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• SH2 domains recognize specific phosphopeptide sequences.

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• The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

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• Mutation of Tyr697, a GRB2‐binding site, and Tyr721, a PI 3‐kinase binding site, abrogates signal transduction by the murine CSF‐1 receptor expressed in Rat‐2 fibroblasts.

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• The SH2/SH3 domain‐containing protein GRB2 interacts with tyrosine‐phosphorylated IRS1 and Shc: implications for insulin control of ras signalling.

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• The when and how of Src regulation.

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• The mitogen-activated protein kinase signal transduction pathway.

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• Stimulation of tyrosine phosphorylation and accumulation of GTP-bound p21ras upon antibody-mediated alpha 2 beta 1 integrin activation in T-lymphoblastic cells.

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• The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling.

  1992cited by this paper
• pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

  1992cited by this paper
• Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase.

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

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• Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation

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

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