SH2 domain of Src binds to the active receptor

Stable Identifier
Homo sapiens
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The Src family of tyrosine kinases are characterized by a SH3 and a SH2 domain in addition to the kinase domain.Src is activated when the SH2 domain binds to autophosphorylation sites on PDGF receptors (Tyr579 and 581 in the beta-receptor, Tyr572 and 574 in the alpha receptor), in conjuction with dephosporylation of the COOH-terminal phosphorylated tyrosine 527.

Literature References
PubMed ID Title Journal Year
10508235 Mechanism of action and in vivo role of platelet-derived growth factor

Westermark, B, Heldin, CH

Physiol Rev 1999
9488729 A role for Src in signal relay by the platelet-derived growth factor alpha receptor

Bazenet, C, Kazlauskas, A, Gelderloos, JA, Rosenkranz, S

J Biol Chem 1998
9739761 Signal transduction via platelet-derived growth factor receptors

Ostman, A, Heldin, CH, Rönnstrand, L

Biochim Biophys Acta 1998
7685273 Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases

Engström, A, Mori, S, Courtneidge, SA, Yokote, K, Heldin, CH, Claesson-Welsh, L, Rönnstrand, L

EMBO J 1993
Orthologous Events
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