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Commentary: The carboxyl‐terminal Crk SH3 domain: Regulatory strategies and new perspectives
Author(s) -
Sriram Ganapathy,
Birge Raymond B.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.04.040
Subject(s) - adapter molecule crk , signal transducing adaptor protein , sh3 domain , sh2 domain , receptor tyrosine kinase , microbiology and biotechnology , signal transduction , biology , phosphorylation , kinase , tyrosine kinase , hamp domain , grb2 , computational biology , biochemistry , protein domain , gene
Since their discovery as cellular counterparts of viral oncogenes more than two decades ago, enormous progress has been made in unraveling the complex regulatory pathways of signal transduction initiated by the Crk family of proteins. New structural and biochemical studies have uncovered novel insights into both negative and positive regulation of Crk mediated by its atypical carboxyl‐terminal SH3 domain (SH3C). Moreover, SH3C is tyrosine phosphorylated by receptor tyrosine kinases and non‐receptor tyrosine kinases, thereby permitting assemblages of other SH2/PTB domain containing proteins. Such non‐canonical signaling by the Crk SH3C reveals new regulatory strategies for adaptor proteins.