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PNAS 97 (16): 8910-8915

Copyright © 2000 by the National Academy of Sciences.

Inaugural Article


Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate

Gregory S. Taylor, Tomohiko Maehama*, and Jack E. Dixon{dagger}

Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606

Contributed by Jack E. Dixon

Accepted for publication June 2, 2000.

Abstract: The lipid second messenger phosphatidylinositol 3-phosphate [PI(3)P] plays a crucial role in intracellular membrane trafficking. We report here that myotubularin, a protein tyrosine phosphatase required for muscle cell differentiation, is a potent PI(3)P phosphatase. Recombinant human myotubularin specifically dephosphorylates PI(3)P in vitro. Overexpression of a catalytically inactive substrate-trapping myotubularin mutant (C375S) in human 293 cells increases PI(3)P levels relative to that of cells overexpressing the wild-type enzyme, demonstrating that PI(3)P is a substrate for myotubularin in vivo. In addition, a Saccharomyces cerevisiae strain in which the myotubularin-like gene (YJR110w) is disrupted also exhibits increased PI(3)P levels. Both the recombinant yeast enzyme and a human myotubularin-related protein (KIAA0371) are able to dephosphorylate PI(3)P in vitro, suggesting that this activity is intrinsic to all myotubularin family members. Mutations in the MTM1 gene that cause human myotubular myopathy dramatically reduce the ability of the phosphatase to dephosphorylate PI(3)P. Our findings provide evidence that myotubularin exerts its effects during myogenesis by regulating cellular levels of the inositol lipid PI(3)P.

* Present address: Department of Pharmacology, Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo, Tokyo 113-8163, Japan.

{dagger} To whom reprint requests should be addressed. E-mail: jedixon{at}

This contribution is part of the special series of Inaugural Articles by members of the National Academy of Sciences elected on May 2, 2000.

Article published online before print: Proc. Natl. Acad. Sci. USA, 10.1073/pnas.160255697.

Article and publication date are at

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Characterization of an adapter subunit to a phosphatidylinositol (3)P 3-phosphatase: Identification of a myotubularin-related protein lacking catalytic activity.
H. H. Nandurkar, K. K. Caldwell, J. C. Whisstock, M. J. Layton, E. A. Gaudet, F. A. Norris, P. W. Majerus, and C. A. Mitchell (2001)
PNAS 98, 9499-9504
   Abstract »    Full Text »    PDF »
A Unique Carbohydrate Binding Domain Targets the Lafora Disease Phosphatase to Glycogen.
J. Wang, J. A. Stuckey, M. J. Wishart, and J. E. Dixon (2002)
J. Biol. Chem. 277, 2377-2380
   Abstract »    Full Text »    PDF »
Activation of the Akt-related cytokine-independent survival kinase requires interaction of its phox domain with endosomal phosphatidylinositol 3-phosphate.
J. V. Virbasius, X. Song, D. P. Pomerleau, Y. Zhan, G. W. Zhou, and M. P. Czech (2001)
PNAS 98, 12908-12913
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Regulation of Fab1 Phosphatidylinositol 3-Phosphate 5-Kinase Pathway by Vac7 Protein and Fig4, a Polyphosphoinositide Phosphatase Family Member.
J. D. Gary, T. K. Sato, C. J. Stefan, C. J. Bonangelino, L. S. Weisman, and S. D. Emr (2002)
Mol. Biol. Cell 13, 1238-1251
   Abstract »    Full Text »    PDF »

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