The myotubularin family: from genetic disease to phosphoinositide metabolism.
The myotubularin-related genes define a large family of eukaryotic proteins, most of them initially characterized by the presence of a ten-amino acid consensus sequence related to the active sites of tyrosine phosphatases, dual-specificity protein phosphatases and the lipid phosphatase PTEN. Myotubularin (hMTM1), the founder member, is mutated in myotubular myopathy, and a close homolog (hMTMR2) was recently found mutated in a recessive form of Charcot-Marie-Tooth neuropathy. Although myotubularin was thought to be a dual-specificity protein phosphatase, recent results indicate that it is primarily a lipid phosphatase, acting on phosphatidylinositol 3-monophosphate, and might be involved in the regulation of phosphatidylinositol 3-kinase ( PI 3-kinase) pathway and membrane trafficking.[1]References
- The myotubularin family: from genetic disease to phosphoinositide metabolism. Laporte, J., Blondeau, F., Buj-Bello, A., Mandel, J.L. Trends Genet. (2001) [Pubmed]
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