Difference between revisions of "Phosphatase Family Myotubularin"

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==[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Family_Myotubularin|Myotubularin]]==
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_I|Superfamily Cys-based I]]:  [[Phosphatase_Family_Myotubularin|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. However, 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 <cite>Robinson06</cite>.
 
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. However, 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 <cite>Robinson06</cite>.

Revision as of 00:20, 7 May 2014

Phosphatase Classification: Superfamily Cys-based I: 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. However, 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].

Subfamilies

MTMR1

C2-MTMR1

The feature of this subfamily is a C2 domain attached to the R1-like sequence.

MTMR3

MTMR5

Inactive myotubularin subfamily.

MTMR6

MTMR9

MTMR10

MTMR14

Ymr1

Reference

  1. 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 | PubMed ID:16828287 | HubMed [Robinson06]