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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
1-phosphatidyl-1D-myo-inositol + phosphate
1-phosphatidyl-1D-myo-inositol 5-phosphate + H2O
1-phosphatidyl-1D-myo-inositol + phosphate
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di-C8 phosphatidylinositol 3,5-bisphosphate + H2O
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di-C8 phosphatidylinositol 5-phosphate + H2O
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additional information
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
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isoform MTM1 can hydrolyze phosphatidylinositol 3,5-bisphosphate both in vitro and in mammalian cells
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
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product causes myotubularin MTM1 to form a heptameric ring that is 12.5 nm in diameter, and it is a specific allosteric activator of myotubularin MTM1, and myotubularin-related proteins MTMR3 and MTMR6
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
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product stimulates cell migration
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
the enzyme also has the activity of EC 3.1.3.64 (phosphatidylinositol-3-phosphatase)
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
presence of catalytically inactive MTMR9 increases the enzymatic activity of isoform MTMR6 toward 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate by over 30fold
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
presence of catalytically inactive MTMR9 increases the enzymatic activity of isoform MTMR8 toward 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate by 1.4fold
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1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate
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substrate binds most strongly to the GRAM domain of isoform MTMR2
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1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
1-phosphatidyl-1D-myo-inositol + phosphate
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1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
1-phosphatidyl-1D-myo-inositol + phosphate
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1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
1-phosphatidyl-1D-myo-inositol + phosphate
presence of catalytically inactive MTMR9 increases the enzymatic activity of isoform MTMR6 toward 1-phosphatidyl-1D-myo-inositol 3-phosphate by 2fold
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1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O
1-phosphatidyl-1D-myo-inositol + phosphate
presence of catalytically inactive MTMR9 increases the enzymatic activity of isoform MTMR8 toward 1-phosphatidyl-1D-myo-inositol 3-phosphate by 4fold
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additional information
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isoform MTM1 additionally hydrolyzes 1-phosphatidyl-1D-myo-inositol 3-phosphate, reaction of EC 3.1.3.64
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additional information
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isoform MTMR6 shows similar activity with substrates 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate and 1-phosphatidyl-1D-myo-inositol 3-phosphate
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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
metabolism
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enzyme levels control Piezo2 ion channels-mediated rapidly adapting mechanically activated currents
malfunction
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both depletion and overexpression of either myotubularin-related protein 3 or myotubularin-related protein 4 results in abnormal midbody morphology and cytokinesis failure
malfunction
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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
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
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
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
physiological function
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on depletion of isoform MTMR3 by RNAi, BJ cells are unable to migrate into the wound and show a significant decrease in velocity of about 60% and a decrease in persistence. While 80% of control cells present actin fibres perpendicular to the wound, only 52% of the cells show this on MTMR3 depletion
physiological function
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myotubularin-related proteins 3 and 4 interact with polo-like kinase 1 and centrosomal protein of 55000 Da to ensure proper abscission
physiological function
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overexpression of isoform MTMR3 inhibits the activity of the serine/threonine kinase complex mTORC1. Thus the enzyme regulates autophagy via its effect on mTORC1 activity
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Schaletzky, J.; Dove, S.K.; Short, B.; Lorenzo, O.; Clague, M.J.; Barr, F.A.
Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases
Curr. Biol.
13
504-509
2003
Homo sapiens (Q9Y217)
brenda
Tronchere, H.; Laporte, J.; Pendaries, C.; Chaussade, C.; Liaubet, L.; Pirola, L.; Mandel, J.L.; Payrastre, B.
Production of phosphatidylinositol 5-phosphate by the phosphoinositide 3-phosphatase myotubularin in mammalian cells
J. Biol. Chem.
279
7304-7312
2004
Homo sapiens (Q13496)
brenda
Robinson, F.L.; Dixon, J.E.
The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-tooth disease
J. Biol. Chem.
280
31699-31707
2005
Homo sapiens (Q13614)
brenda
Walker, D.M.; Urbe, S.; Dove, S.K.; Tenza, D.; Raposo, G.; Clague, M.J.
Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity
Curr. Biol.
11
1600-1605
2001
Homo sapiens (Q13615)
brenda
Oppelt, A.; Lobert, V.H.; Haglund, K.; Mackey, A.M.; Rameh, L.E.; Liest?l, K.; Schink, K.O.; Pedersen, N.M.; Wenzel, E.M.; Haugsten, E.M.; Brech, A.; Rusten, T.E.; Stenmark, H.; Wesche, J.
Production of phosphatidylinositol 5-phosphate via PIKfyve and MTMR3 regulates cell migration
EMBO Rep.
14
57-64
2013
Homo sapiens
brenda
Tsujita, K.; Itoh, T.; Ijuin, T.; Yamamoto, A.; Shisheva, A.; Laporte, J.; Takenawa, T.
Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction
J. Biol. Chem.
279
13817-13824
2004
Homo sapiens
brenda
Zou, J.; Zhang, C.; Marjanovic, J.; Kisseleva, M.V.; Majerus, P.W.; Wilson, M.P.
Myotubularin-related protein (MTMR) 9 determines the enzymatic activity, substrate specificity, and role in autophagy of MTMR8
Proc. Natl. Acad. Sci. USA
109
9539-9544
2012
Homo sapiens (Q96EF0), Homo sapiens (Q9Y217)
brenda
Yoo, K.Y.; Son, J.Y.; Lee, J.U.; Shin, W.; Im, D.W.; Kim, S.J.; Ryu, S.E.; Heo, Y.S.
Structure of the catalytic phosphatase domain of MTMR8 implications for dimerization, membrane association and reversible oxidation
Acta Crystallogr. Sect. D
71
1528-1539
2015
Homo sapiens
brenda
Bong, S.M.; Yang, S.W.; Choi, J.W.; Kim, S.J.; Lee, B.I.
Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1
Acta Crystallogr. Sect. F
71
261-265
2015
Homo sapiens
brenda
Narayanan, P.; Huette, M.; Kudryasheva, G.; Taberner, F.J.; Lechner, S.G.; Rehfeldt, F.; Gomez-Varela, D.; Schmidt, M.
Myotubularin related protein-2 and its phospholipid substrate PIP2 control Piezo2-mediated mechanotransduction in peripheral sensory neurons
eLife
7
e32346
2018
Homo sapiens
brenda
Hao, F.; Itoh, T.; Morita, E.; Shirahama-Noda, K.; Yoshimori, T.; Noda, T.
The PtdIns3-phosphatase MTMR3 interacts with mTORC1 and suppresses its activity
FEBS Lett.
590
161-173
2016
Homo sapiens
brenda
Pham, H.Q.; Yoshioka, K.; Mohri, H.; Nakata, H.; Aki, S.; Ishimaru, K.; Takuwa, N.; Takuwa, Y.
MTMR4, a phosphoinositide-specific 3-phosphatase, regulates TFEB activity and the endocytic and autophagic pathways
Genes Cells
23
670-687
2018
Homo sapiens
brenda
St-Denis, N.; Gupta, G.D.; Lin, Z.Y.; Gonzalez-Badillo, B.; Pelletier, L.; Gingras, A.C.
Myotubularin-related proteins 3 and 4 interact with polo-like kinase 1 and centrosomal protein of 55 kDa to ensure proper abscission
Mol. Cell. Proteomics
14
946-960
2015
Homo sapiens
brenda
Bong, S.M.; Son, K.B.; Yang, S.W.; Park, J.W.; Cho, J.W.; Kim, K.T.; Kim, H.; Kim, S.J.; Kim, Y.J.; Lee, B.I.
Crystal structure of human myotubularin-related protein 1 provides insight into the structural basis of substrate specificity
PLoS ONE
11
e0152611
2016
Homo sapiens (Q13613), Homo sapiens
brenda