Myotubularin-related protein 1 (MTMR1)

Myotubularin-related protein 1 (MTMR1) is a lipid phosphatase enzyme in the tyrosine/dual-specificity phosphatase superfamily[1][2][5]. It hydrolyzes the D-3 phosphate of phosphatidylinositol 3-monophosphate and phosphatidylinositol 3,5-bisphosphate to generate phosphatidylinositol and phosphatidylinositol 5-monophosphate, respectively, playing a central role in phosphoinositide metabolism and membrane dynamics[1][2][5]. MTMR1 contains a Pleckstrin homology (PH)-GRAM domain important for lipid binding and a protein tyrosine phosphatase (PTP) catalytic domain responsible for its enzymatic activity[1][2]. It is implicated in cellular processes like autophagy, signal transduction, and potentially muscle and cardiovascular function[1][3][5]. Mutations or altered function may be linked to diseases such as myotonic dystrophy and possibly contribute to certain cancers and cardiovascular disorders[1][3][5]. The protein is relatively understudied compared to some family members, and no clinically used drugs directly target MTMR1 as of current knowledge.

Other names

Phosphatidylinositol-3-phosphate phosphatase MTMR1Phosphatidylinositol-3,5-bisphosphate 3-phosphataseMyotubularin-related protein 1phosphatidylinositol-3-phosphate phosphatasephosphatidylinositol-3,5-bisphosphate 3-phosphatase

Dephosphorylation of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, producing phosphatidylinositol and phosphatidylinositol 5-phosphate, respectively