EC Number   |
General Information |
Reference |
|---|
   3.1.3.95 | malfunction |
both depletion and overexpression of either myotubularin-related protein 3 or myotubularin-related protein 4 results in abnormal midbody morphology and cytokinesis failure |
751566 |
| 3.1.3.95 | malfunction |
enzyme knockdown markedly suppresses the motility, fusion, and fission of phosphatidylinositol 3-phosphate-enriched structures, resulting in decreases in late endosomes, autophagosomes, and lysosomes, and enlargement of phosphatidylinositol 3-phosphate-enriched early and late endosomes. Enzyme knockdown impairs starvation-induced transcription factor-EB nuclear translocation and lysosome biogenesis |
750697 |
| 3.1.3.95 | malfunction |
isoform MTMR14 deletion induces overweight and adult obesity accompanied by chronic inflammation in an age-dependent manner |
750259 |
| 3.1.3.95 | metabolism |
enzyme levels control Piezo2 ion channels-mediated rapidly adapting mechanically activated currents |
750410 |
| 3.1.3.95 | physiological function |
complex formation between the active isoform MTMR6 and catalytically inactive MTMR9 increases its catalytic activity and alters its substrate specificity. The MTMR6/MTMR9 complex prefers 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate as substrate. Presence of MTMR9 increases the enzymatic activity of MTMR6 toward 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate by over 30fold, and enhances the activity toward 1-phosphatidyl-1D-myo-inositol 3-phosphate by only 2fold. In cells, the MTMR6/R9 complex significantly increases the cellular levels of 1-phosphatidyl-1D-myo-inositol 3-phosphate, the product of 1-phosphatidyl-1D-myo-inositol 3-phosphate dephosphorylation |
728687 |
| 3.1.3.95 | physiological function |
complex formation between the active isoform MTMR6 and catalytically inactive MTMR9 increases its catalytic activity and alters its substrate specificity. The MTMR6/MTMR9 complex prefers 1-phosphatidyl-1D-myo-inositol 3-phosphate as substrate. Presence of MTMR9 increases the enzymatic activity of MTMR8 toward 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate by 1.4fold, and enhances the activity toward 1-phosphatidyl-1D-myo-inositol 3-phosphate by 4fold. In cells, the MTMR8/R9 complex reduces the cellular levels of 1-phosphatidyl-1D-myo-inositol 3-phosphate |
728687 |
| 3.1.3.95 | physiological function |
endogenous isoform MTMR2 and myotubularin-related protein MTMR13 proteins are associated in human embryonic kidney 293 cells. MTMR2-MTMR13 association is mediated by coiled-coil sequences present in each protein. Loss of MTMR13 function in Charcot-Marie-Tooth disease type 4B patients may lead to alterations in MTMR2 function and subsequent alterations in 3-phosphoinositide signaling |
665651 |
| 3.1.3.95 | physiological function |
in L6 myotubes overexpressing isoform MTM1, hyperosmotic shock induces an increase in the mass level of 1-phosphatidyl-1D-myo-inositol 5-phosphate that is reduced by 50% upon overexpression of the MTM1 inactive mutant D278A |
665599 |
| 3.1.3.95 | physiological function |
mutations in the gene encoding myotubularin-related protein MTMR2 are responsible for autosomal recessive Charcot-Marie-Tooth disease type 4B1. The known disease-associated MTMR2 mutations lead to dramatically reduced phosphatase activity |
727605 |
| 3.1.3.95 | physiological function |
myotubularin-related proteins 3 and 4 interact with polo-like kinase 1 and centrosomal protein of 55000 Da to ensure proper abscission |
751566 |
