Cellular stress regulates the nucleocytoplasmic distribution of the protein-tyrosine phosphatase TCPTP.
作者： Mark H. C. Lam , Belinda J. Michell , Michelle T. Fodero-Tavoletti , Bruce E. Kemp , Nicholas K. Tonks
关键词:
摘要: Specific cellular stresses, including hyperosmotic stress, caused a dramatic but reversible cytoplasmic accumulation of the otherwise nuclear 45-kDa variant protein-tyrosine phosphatase TCPTP (TC45). In cytoplasm, TC45 dephosphorylated epidermal growth factor receptor and down-regulated stress-induced activation c-Jun N-terminal kinase. The exit was not inhibited by leptomycin B, indicating that independent exportin CRM-1. Moreover, stress did induce green fluorescent protein-TC45 fusion protein too large to diffuse across pore. Our results indicate may occur passive diffusion inhibiting import. Neither p42(Erk2) nor stress-activated kinase or p38 mediated redistribution TC45. We found only those stresses stimulated metabolic stress-sensing enzyme AMP-activated (AMPK) induced addition, specific pharmacological AMPK sufficient cause in cytoplasm. studies signaling pathways involve can alter nucleocytoplasmic distribution thus regulate function vivo.
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