Commentary: The carboxyl-terminal Crk SH3 domain: Regulatory strategies and new perspectives.
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.
Department of Biochemistry and Molecular Biology, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA.
Ganapathy
G
Sriram
Raymond B
RB
Birge
D000818:Animals; D002465:Cell Movement; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D050737:Proto-Oncogene Proteins c-crk / Q000737:chemistry*; D015398:Signal Transduction; D014443:Tyrosine / Q000737:chemistry; D018909:src Homology Domains
D010455:Peptides; D050737:Proto-Oncogene Proteins c-crk; D014443:Tyrosine