Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases (Q30168876)

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English	Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

9 June 2017

Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases (English)

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

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author name string

Lock LS

1

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Royal I

2

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Europe PubMed Central

PubMed publication ID

9 June 2017

Naujokas MA

3

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Europe PubMed Central

PubMed publication ID

9 June 2017

Park M

4

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Europe PubMed Central

PubMed publication ID

9 June 2017

language of work or name

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publication date

1 October 2000

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Europe PubMed Central

PubMed publication ID

9 June 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

9 June 2017

275

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Europe PubMed Central

PubMed publication ID

9 June 2017

40

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

31536-31545

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Europe PubMed Central

PubMed publication ID

9 June 2017

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Association of the Multisubstrate Docking Protein Gab1 with the Hepatocyte Growth Factor Receptor Requires a Functional Grb2 Binding Site Involving Tyrosine 1356

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Met-induced JNK activation is mediated by the adapter protein Crk and correlates with the Gab1 - Crk signaling complex formation

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Interaction between Gab1 and the c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis

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Efficient Cellular Transformation by the Met Oncoprotein Requires a Functional Grb2 Binding Site and Correlates with Phosphorylation of the Grb2-associated Proteins, Cbl and Gab1

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Gab1 coupling to the HGF/Met receptor multifunctional docking site requires binding of Grb2 and correlates with the transforming potential.

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Grb2-associated binder-1 mediates phosphatidylinositol 3-kinase activation and the promotion of cell survival by nerve growth factor

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The Gab1 protein is a docking site for multiple proteins involved in signaling by the B cell antigen receptor.

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Alternative splicing generates isoforms of the met receptor tyrosine kinase which undergo differential processing

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DNA-mediated transfer of the adenine phosphoribosyltransferase locus into mammalian cells

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Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains

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Structural basis for the binding of proline-rich peptides to SH3 domains

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Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition

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Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands

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Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation

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Identifiers

10.1074/JBC.M003597200

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

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