Interactions of STATs with Src Family Kinases

摘要: C-Src tyrosine kinase is the cellular homologue of v-Src, oncogenic form protein encoded by chicken retrovirus, Rous sarcoma virus (reviewed in 1, 2). The Src family kinases includes Src, Yes, Yrk, and Fyn which are ubiquitously expressed, Hck, Fgr, Lyn, Lck Blk expressed predominantly hematopoetic cells (myeloid B T lymphocytes). These proteins approximately 60kDa molecular weight composed six domains (Figure 1). For these are: 1) N-terminal domain that contains a signal for myristolyation targets cytosolic to intracellular membranes; 2) unique likely involved protein-protein interactions; 3) an SH3 binds proline-rich sequences; 4) SH2 phosphotyrosine residues; 5) catalytic domain; 6) negative regulatory region at C-terminus Tyr530 (originally identified c-Src as Tyr527). phosphorylated C-terminal (Csk), resulting intramolecular interaction between this thus rendering catalytically inactive. Displacement binding another protein, dephosphorylation, or mutation/deletion (as v-Src) changes conformation c-Src, activation. plays integral role growth factor-induced proliferation well initiation progression many human cancers, differentiation (1, 3, 4). This chapter will review current knowledge regarding interactions (and members) STAT proteins, including association with phosphorylation STATs (SFKs), SFKs activation factors, finally, biological effects require