Myotubularin-related protein 2 (MTMR2)

**Myotubularin-related protein 2** (MTMR2) is a lipid phosphatase belonging to the myotubularin family, which are unique among protein tyrosine phosphatases for their specificity toward phosphoinositide substrates instead of phosphoproteins[1][3][4]. MTMR2 specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], thereby generating phosphatidylinositol and phosphatidylinositol 5-phosphate[1][3][4]. It contains several domains, including a PH-GRAM domain for membrane interaction, a PTP-like catalytic domain, and a coiled-coil domain for dimerization and interaction with inactive family members such as MTMR13/SBF2 and MTMR5[1][2][5]. MTMR2 function is critical for membrane trafficking, autophagy, and Schwann cell function. Mutations in MTMR2 cause Charcot-Marie-Tooth disease type 4B1, an autosomal recessive demyelinating neuropathy characterized by folding of myelin within peripheral nerves[2][3][4][5]. There are no approved therapies selectively targeting MTMR2, and loss of function leads to severe neurological deficits, indicating that its enzymatic activity is essential for nervous system health.

Other names

Phosphatidylinositol-3,5-bisphosphate 3-phosphatasePhosphatidylinositol-3-phosphate phosphataseMTMR2

Drugs targeting similar phosphoinositide phosphatases would act via **inhibition or modulation of phosphatase activity**, affecting phosphoinositide signaling and downstream cellular effects. No selective drugs for MTMR2 are approved or in clinical use.