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Originally published In Press as doi:10.1074/jbc.M105128200 on July 30, 2001

J. Biol. Chem., Vol. 276, Issue 40, 37700-37707, October 5, 2001
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Cellular Stress Regulates the Nucleocytoplasmic Distribution of the Protein-tyrosine Phosphatase TCPTP*

Mark H. C. LamDagger §, Belinda J. Michell, Michelle T. Fodero-TavolettiDagger , Bruce E. Kemp, Nicholas K. Tonks||, and Tony TiganisDagger **

From the Dagger  Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia,  St. Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia, and || Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724

Specific cellular stresses, including hyperosmotic stress, caused a dramatic but reversible cytoplasmic accumulation of the otherwise nuclear 45-kDa variant of the protein-tyrosine phosphatase TCPTP (TC45). In the cytoplasm, TC45 dephosphorylated the epidermal growth factor receptor and down-regulated the hyperosmotic stress-induced activation of the c-Jun N-terminal kinase. The hyperosmotic stress-induced nuclear exit of TC45 was not inhibited by leptomycin B, indicating that TC45 nuclear exit was independent of the exportin CRM-1. Moreover, hyperosmotic stress did not induce the cytoplasmic accumulation of a green fluorescent protein-TC45 fusion protein that was too large to diffuse across the nuclear pore. Our results indicate that TC45 nuclear exit may occur by passive diffusion and that cellular stress may induce the cytoplasmic accumulation of TC45 by inhibiting nuclear import. Neither p42Erk2 nor the stress-activated c-Jun N-terminal kinase or p38 mediated the stress-induced redistribution of TC45. We found that only those stresses that stimulated the metabolic stress-sensing enzyme AMP-activated protein kinase (AMPK) induced the redistribution of TC45. In addition, specific pharmacological activation of the AMPK was sufficient to cause the accumulation of TC45 in the cytoplasm. Our studies indicate that specific stress-activated signaling pathways that involve the AMPK can alter the nucleocytoplasmic distribution of TC45 and thus regulate TC45 function in vivo.

* This work was supported by funds from the National Health and Medical Research Council of Australia (to T. T. and B. E. K.) and from the Anti-Cancer Council of Victoria and the National Breast Cancer Foundation of Australia (to T. T.) and by National Institutes of Health Grant CA53840 (to N. K. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of National Health and Medical Research Council of Australia Peter Doherty Fellowship 007051.

** Recipient of National Health and Medical Research Council of Australia R. D. Wright Fellowship 007757 and a Monash University Logan Fellowship. To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, P.O. Box 13D, Monash University, Vic. 3800, Australia. Tel.: 61-3-9905-3772; Fax: 61-3-9905-4699; E-mail: Tony.Tiganis@med.monash.edu.au.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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