TAILIEUCHUNG - Báo cáo khoa học: Myristoylation of the dual-specificity phosphatase c-JUN N-terminal kinase (JNK) stimulatory phosphatase 1 is necessary for its activation of JNK signaling and apoptosis

Activation of the c-JUN N-terminal kinase (JNK) pathway is implicated in a number of important physiological processes, from embryonic morpho-genesis to cell survival and apoptosis. JNK stimulatory phosphatase 1 (JSP1) is a member of the dual-specificity phosphatase subfamily of protein tyrosine phosphatases. | Myristoylation of the dual-specificity phosphatase c-JUN N-terminal kinase JNK stimulatory phosphatase 1 is necessary for its activation of JNK signaling and apoptosis Ulla Schwertassek1 Deirdre A. Buckley1 z Chong-Feng Xu2 Andrew J. Lindsay3 Mary W. McCaffrey3 Thomas A. Neubert2 and Nicholas K. Tonks1 1 Cold Spring Harbor Laboratory Cold Spring Harbor NY USA 2 KimmelCenter for Biology and Medicine at the SkirballInstitute and Department of Pharmacology New York University Schoolof Medicine NY USA 3 Molecular CellBiology Laboratory Department of Biochemistry Biosciences Institute University College Cork Ireland Keywords apoptosis JNK JSP1 myristoylation phosphatase Correspondence N. K. Tonks Cold Spring Harbor Laboratory 1 Bungtown Road Cold Spring Harbor NY 11724-2208 USA Fax 001 516 367 6812 Tel 001 516 367 8846 E-mail tonks@ Present address CellBiology Laboratory Department of Biochemistry Biosciences Institute University College Cork Ireland Received 16 February 2010 revised 19 March 2010 accepted 23 March 2010 doi Activation of the c-JUN N-terminal kinase JNK pathway is implicated in a number of important physiological processes from embryonic morphogenesis to cell survival and apoptosis. JNK stimulatory phosphatase 1 JSP1 is a member of the dual-specificity phosphatase subfamily of protein tyrosine phosphatases. In contrast to other dual-specificity phosphatases that catalyze the inactivation of mitogen-activated protein kinases expression of JSP1 activates JNK-mediated signaling. JSP1 and its relative DUSP15 are unique among members of the protein tyrosine phosphatase family in that they contain a potential myristoylation site at the N-terminus MGNGMXK . In this study we investigated whether JSP1 was myristoy-lated and examined the functional consequences of myristoylation. Using mass spectrometry we showed that wild-type JSP1 but not a JSP1 mutant in which Gly2 was mutated to Ala JSP1-G2A was myristoylated in cells.

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