Difference between revisions of "Phosphatase Family Myotubularin"
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===== [[Phosphatase_Subfamily_MTMR1|MTMR1]] ===== | ===== [[Phosphatase_Subfamily_MTMR1|MTMR1]] ===== | ||
+ | MTMR1 is a lipid phosphatase that dephosphorylates the second messenger phosphatidylinositol 3-monophosphate [PI(3)P]. It is found across holozoan. | ||
===== [[Phosphatase_Subfamily_MTMR3|MTMR3]]===== | ===== [[Phosphatase_Subfamily_MTMR3|MTMR3]]===== |
Revision as of 01:26, 31 December 2014
Phosphatase Classification: FoldCC1: Superfamily CC1: Family Myotubularin
Myotubularins are 3-phosphatases specific for PtdIns3P and PtdIns(3,5)P2, two PIs that function within the endosomal-lysomal pathway . In yeast, there is a single myotubularin Ymr1p, and its functions appear to be redundant with those of other 3-phosphatases. In C. elegans, which has six myotubularins, several of the myotublarins have non-redundant roles in regulating PtdIns3P during endocytosis. In human, there are 14 myotublarins, and mutations in several of them lead to myotubular myopathy and Charcot-Marie-Tooth peripheral neuropathy. Interestingly, around half of myotubularins are catalytically inactive. One of their possible function is regulating active myotubularins by protein interaction. For details, see the review [1].
Contents
Subfamilies
MTMR1
MTMR1 is a lipid phosphatase that dephosphorylates the second messenger phosphatidylinositol 3-monophosphate [PI(3)P]. It is found across holozoan.
MTMR3
MTMR3 is an inositol lipid 3-phosphatase. It is probably a protein phosphatase of receptor-regulated SMAD. It is found throughout metazoan, with a signature FYVE domain.
MTMR5 (SBF)
Inactive myotubularin subfamily.
MTMR7
MTMR9
MTMR10
MTMR14
YMR1
Yeast has a single myotubularin YMR1, encoding PI(3)P phosphatase [2].
Reference
- Robinson FL and Dixon JE. Myotubularin phosphatases: policing 3-phosphoinositides. Trends Cell Biol. 2006 Aug;16(8):403-12. DOI:10.1016/j.tcb.2006.06.001 |
- Taylor GS, Maehama T, and Dixon JE. Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate. Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8910-5. DOI:10.1073/pnas.160255697 |