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First published online July 5, 2006

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Myotubularins pick more partners

Myotubularins (MTMs) specifically hydrolyse phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol (3,5)-bisphosphate [PtdIns(3,5)P₂], two lipid regulators of endosomal trafficking. Heteromeric interactions between MTMs are thought to be important but are poorly characterized. Michael Clague and colleagues have therefore performed a systematic analysis of possible MTM interactions (see p. 2953). They confirm previously identified interactions and identify two new ones: MTMR8 interacts with MTMR9; and MTMR3 interacts with MTMR4. The second of these provides the first example of a heteromeric interaction between enzymatically active MTMs – there are 14 MTMs but only eight are catalytically active. Although much attention has focused on possible endosomal functions for MTMs, the authors show that only MTMR4 localizes to endosomal structures. Furthermore, although all the catalytically active MTMs that they test hydrolyse the endosomal pool of PtdIns3P when overexpressed, most MTM constructs have little effect on EGF receptor trafficking. A catalytically inactive form of MTMR4, however, severely impedes EGF receptor downregulation. These results suggest that MTMR4 is involved in endosomal function and provide a general framework for further investigation of this family of lipid phosphatases.

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Related articles in JCS:

Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosomerelated functions

Óscar Lorenzo, Sylvie Urbé, and Michael J. Clague
JCS 2006 119: 2953-2959. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?