Proline-rich sequences mediate the interaction of the Arg protein tyrosine kinase with Crk.

摘要: Arg is a ubiquitously expressed member of the Abelson family nonreceptor protein-tyrosine kinases. Defining sequences that mediate its interaction with other proteins essential to elucidating role in cellular signaling. In this report we demonstrate associates c-Crk, an adaptor protein composed SH2 domain and two SH3 domains, examine molecular mechanism interaction. vitro experiments revealed three proline-rich distinct specificities for domains are located C-terminal domain, just kinase these bind Crk N-terminal domain. These conform PxLPxK/R motif has been observed The c-Crk living cells was confirmed by detection coimmunoprecipitation coinfected Sf9 cells. addition, increased phosphorylation cotransfected COS cells, indicating substrate. site identified as tyrosine 221, residue whose modification shown result intramolecular folded conformation. extend known interacting motifs include binding sites suggest may function effector well regulator activity.