Recombinant Human MTMR7 protein

MTMR7 (Myotubularin-related protein 7) is a member of the myotubularin family of lipid phosphatases, which specifically dephosphorylate phosphatidylinositol (PI) signaling molecules, particularly PI3P and PI(3.5)P2. These lipids play critical roles in membrane trafficking, autophagy, and endocytic pathways. MTMR7 is characterized by a conserved catalytic active site within its protein tyrosine phosphatase (PTP) domain, along with a PH-GRAM domain for membrane association and a coiled-coil domain mediating protein interactions. Unlike some family members, MTMR7 lacks enzymatic activity unless it forms heterodimers with catalytically active partners like MTMR1 or MTMR2. suggesting a regulatory role in phosphoinositide metabolism.

Recombinant MTMR7 protein is engineered for in vitro studies to investigate its structural properties, substrate specificity, and interaction networks. Its production typically involves expression systems (e.g., E. coli or mammalian cells) followed by purification via affinity tags. Research highlights its involvement in neuronal development and maintenance, as mutations in related myotubularins are linked to Charcot-Marie-Tooth neuropathy. Dysregulation of MTMR7 has also been implicated in cancer progression, potentially through PI3K/AKT/mTOR pathway modulation. Additionally, studies using recombinant MTMR7 explore its role in autophagy-lysosomal dysfunction, a key feature in neurodegenerative diseases. This protein serves as a tool for drug screening aimed at targeting lipid phosphatase activity or restoring phosphoinositide homeostasis in pathological conditions.