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Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.

ABSTRACT: Intracellular signaling is mediated by reversible posttranslational modifications (PTMs) that include phosphorylation, ubiquitination, and acetylation, among others. In response to extracellular stimuli such as growth factors, receptor tyrosine kinases (RTKs) typically dimerize and initiate signaling through phosphorylation of their cytoplasmic tails and downstream scaffolds. Signaling effectors are recruited to these phosphotyrosine (pTyr) sites primarily through Src homology 2 (SH2) domains and pTyr-binding (PTB) domains. This review describes how these conserved domains specifically recognize pTyr residues and play a major role in mediating precise downstream signaling events.

SUBMITTER: Wagner MJ

PROVIDER: S-EPMC3839611 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.

Wagner Melany J MJ Stacey Melissa M MM Liu Bernard A BA Pawson Tony T

Cold Spring Harbor perspectives in biology 20131201 12

Intracellular signaling is mediated by reversible posttranslational modifications (PTMs) that include phosphorylation, ubiquitination, and acetylation, among others. In response to extracellular stimuli such as growth factors, receptor tyrosine kinases (RTKs) typically dimerize and initiate signaling through phosphorylation of their cytoplasmic tails and downstream scaffolds. Signaling effectors are recruited to these phosphotyrosine (pTyr) sites primarily through Src homology 2 (SH2) domains an ...[more]

PMID: 24296166

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