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Volumn 15, Issue 4, 2006, Pages 569-579

Multi-level regulation of myotubularin-related protein-2 phosphatase activity by myotubularin-related protein-13/set-binding factor-2

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROPHOSPHOLIPID; MYOTUBULARIN RELATED PROTEIN 2; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PHOSPHATIDYLINOSITOL 3,5 BISPHOSPHATE; SET BINDING FACTOR 2; UNCLASSIFIED DRUG;

EID: 32144452023     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/ddi473     Document Type: Article
Times cited : (85)

References (37)
  • 1
    • 0141833983 scopus 로고    scopus 로고
    • Disease mechanisms in inherited neuropathies
    • Suter, U. and Scherer, S.S. (2003) Disease mechanisms in inherited neuropathies. Nat. Rev. Neurosci., 4, 714-726.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 714-726
    • Suter, U.1    Scherer, S.S.2
  • 6
    • 0038744272 scopus 로고    scopus 로고
    • Mutations in MTMR13, a new pseudophosphatase homologue of MTMR2 and Sbf1, in two families with an autosomal recessive demyelinating form of Charcot-Marie-Tooth disease associated with early-onset glaucoma
    • Azzedine, H., Bolino, A., Taieb, T., Birouk, N., Di Duca, M., Bouhouche, A., Benamou, S., Mrabet, A., Hammadouche, T., Chkili, T. et al. (2003) Mutations in MTMR13, a new pseudophosphatase homologue of MTMR2 and Sbf1, in two families with an autosomal recessive demyelinating form of Charcot-Marie-Tooth disease associated with early-onset glaucoma. Am. J. Hum. Genet., 72, 1141-1153.
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 1141-1153
    • Azzedine, H.1    Bolino, A.2    Taieb, T.3    Birouk, N.4    Di Duca, M.5    Bouhouche, A.6    Benamou, S.7    Mrabet, A.8    Hammadouche, T.9    Chkili, T.10
  • 7
    • 9044222886 scopus 로고    scopus 로고
    • A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast
    • Laporte, J., Hu, L.J., Kretz, C., Mandel, J.L., Kioschis, P., Coy, J.F., Klauck, S.M., Poustka, A. and Dahl, N. (1996) A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast. Nat. Genet., 13, 175-182.
    • (1996) Nat. Genet. , vol.13 , pp. 175-182
    • Laporte, J.1    Hu, L.J.2    Kretz, C.3    Mandel, J.L.4    Kioschis, P.5    Coy, J.F.6    Klauck, S.M.7    Poustka, A.8    Dahl, N.9
  • 8
    • 0036899518 scopus 로고    scopus 로고
    • PTEN and myotubularin phosphatases: From 3-phosphoinositide dephosphorylation to disease. Phosphatase and tensin homolog deleted on chromosome ten
    • Wishart, M.J. and Dixon, J.E. (2002) PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease. Phosphatase and tensin homolog deleted on chromosome ten. Trends Cell Biol., 12, 579-585.
    • (2002) Trends Cell Biol. , vol.12 , pp. 579-585
    • Wishart, M.J.1    Dixon, J.E.2
  • 9
    • 0141891208 scopus 로고    scopus 로고
    • Myotubularins, a large disease-associated family of cooperating catalytically active and inactive phosphoinositides phosphatases
    • Laporte, J., Bedez, F., Bolino, A. and Mandel, J.L. (2003) Myotubularins, a large disease-associated family of cooperating catalytically active and inactive phosphoinositides phosphatases. Hum. Mol. Genet., 12, R285-R292.
    • (2003) Hum. Mol. Genet. , vol.12
    • Laporte, J.1    Bedez, F.2    Bolino, A.3    Mandel, J.L.4
  • 10
    • 0035899863 scopus 로고    scopus 로고
    • Characterization of MTMR3. An inositol lipid 3-phosphatase with novel substrate specificity
    • Walker, D.M., Urbe, S., Dove, S.K., Tenza, D., Raposo, G. and Clague, M.J. (2001) Characterization of MTMR3. An inositol lipid 3-phosphatase with novel substrate specificity. Curr. Biol., 11, 1600-1605.
    • (2001) Curr. Biol. , vol.11 , pp. 1600-1605
    • Walker, D.M.1    Urbe, S.2    Dove, S.K.3    Tenza, D.4    Raposo, G.5    Clague, M.J.6
  • 11
    • 0037096759 scopus 로고    scopus 로고
    • Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1
    • Berger, P., Bonneick, S., Willi, S., Wymann, M. and Suter, U. (2002) Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1. Hum. Mol. Genet., 11, 1569-1579.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1569-1579
    • Berger, P.1    Bonneick, S.2    Willi, S.3    Wymann, M.4    Suter, U.5
  • 12
    • 0037452874 scopus 로고    scopus 로고
    • Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases
    • Schaletzky, J., Dove, S.K., Short, B., Lorenzo, O., Clague, M.J. and Barr, F.A. (2003) Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases. Curr. Biol., 13, 504-509.
    • (2003) Curr. Biol. , vol.13 , pp. 504-509
    • Schaletzky, J.1    Dove, S.K.2    Short, B.3    Lorenzo, O.4    Clague, M.J.5    Barr, F.A.6
  • 13
    • 0031945475 scopus 로고    scopus 로고
    • Association of SET domain and myotubularin-related proteins modulates growth control
    • Cui, X., De Vivo, I., Slany, R., Miyamoto, A., Firestein, R. and Cleary, M.L. (1998) Association of SET domain and myotubularin-related proteins modulates growth control. Nat. Genet., 18, 331-337.
    • (1998) Nat. Genet. , vol.18 , pp. 331-337
    • Cui, X.1    De Vivo, I.2    Slany, R.3    Miyamoto, A.4    Firestein, R.5    Cleary, M.L.6
  • 14
    • 0035859811 scopus 로고    scopus 로고
    • Characterization of an adapter subunit to a phosphatidylinositol (3)P 3-phosphatase: Identification of a myotubularin-related protein lacking catalytic activity
    • Nandurkar, H.H., Caldwell, K.K., Whisstock, J.C., Layton, M.J., Gaudet, E.A., Norris, F.A., Majerus, P.W. and Mitchell, C.A. (2001) Characterization of an adapter subunit to a phosphatidylinositol (3)P 3-phosphatase: Identification of a myotubularin-related protein lacking catalytic activity. Proc. Natl Acad. Sci. USA, 98, 9499-9504.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 9499-9504
    • Nandurkar, H.H.1    Caldwell, K.K.2    Whisstock, J.C.3    Layton, M.J.4    Gaudet, E.A.5    Norris, F.A.6    Majerus, P.W.7    Mitchell, C.A.8
  • 15
    • 0142027784 scopus 로고    scopus 로고
    • Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module
    • Berger, P., Schaffitzel, C., Berger, I., Ban, N. and Suter, U. (2003) Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module. Proc. Natl Acad. Sci. USA, 100, 12177-12182.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12177-12182
    • Berger, P.1    Schaffitzel, C.2    Berger, I.3    Ban, N.4    Suter, U.5
  • 16
    • 1842690628 scopus 로고    scopus 로고
    • Myotubularin regulates the function of the late endosome through the GRAM domain- phosphatidylinositol 3,5-bisphosphate interaction
    • Tsujita, K., Itoh, T., Ijuin, T., Yamamoto, A., Shisheva, A., Laporte, J. and Takenawa, T. (2004) Myotubularin regulates the function of the late endosome through the GRAM domain- phosphatidylinositol 3,5-bisphosphate interaction. J. Biol. Chem., 279, 13817-13824.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13817-13824
    • Tsujita, K.1    Itoh, T.2    Ijuin, T.3    Yamamoto, A.4    Shisheva, A.5    Laporte, J.6    Takenawa, T.7
  • 17
    • 0032530384 scopus 로고    scopus 로고
    • Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast
    • Isakoff, S.J., Cardozo, T., Andreev, J., Li, Z., Ferguson, K.M., Abagyan, R., Lemmon, M.A., Aronheim, A. and Skolnik, E.Y. (1998) Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J., 17, 5374-5387.
    • (1998) EMBO J. , vol.17 , pp. 5374-5387
    • Isakoff, S.J.1    Cardozo, T.2    Andreev, J.3    Li, Z.4    Ferguson, K.M.5    Abagyan, R.6    Lemmon, M.A.7    Aronheim, A.8    Skolnik, E.Y.9
  • 21
    • 0346099346 scopus 로고    scopus 로고
    • Disease-related myotubularins function in endocytic traffic in Caenorhabditis elegans
    • Dang, H., Li, Z., Skolnik, E.Y. and Fares, H. (2004) Disease-related myotubularins function in endocytic traffic in Caenorhabditis elegans. Mol. Biol. Cell, 15, 189-196.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 189-196
    • Dang, H.1    Li, Z.2    Skolnik, E.Y.3    Fares, H.4
  • 22
    • 0037155216 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve. Endomenbrane localization
    • Sbrissa, D., Ikonomov, O.C. and Shisheva, A. (2002) Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve. Endomenbrane localization. J. Biol. Chem., 277, 6073-6079.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6073-6079
    • Sbrissa, D.1    Ikonomov, O.C.2    Shisheva, A.3
  • 24
    • 0141532093 scopus 로고    scopus 로고
    • Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization
    • Whitley, P., Reaves, B.J., Hashimoto, M., Riley, A.M., Potter, B.V. and Holman, G.D. (2003) Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization. J. Biol. Chem., 278, 38786-38795.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38786-38795
    • Whitley, P.1    Reaves, B.J.2    Hashimoto, M.3    Riley, A.M.4    Potter, B.V.5    Holman, G.D.6
  • 25
    • 3042723253 scopus 로고    scopus 로고
    • Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body
    • Eugster, A., Pecheur, E.I., Michel, F., Winsor, B., Letourneur, F. and Friant, S. (2004) Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol. Biol. Cell, 15, 3031-3041.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3031-3041
    • Eugster, A.1    Pecheur, E.I.2    Michel, F.3    Winsor, B.4    Letourneur, F.5    Friant, S.6
  • 28
    • 0042693009 scopus 로고    scopus 로고
    • Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9
    • Mochizuki, Y. and Majerus, P.W. (2003) Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9. Proc. Natl Acad. Sci. USA, 100, 9768-9773.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9768-9773
    • Mochizuki, Y.1    Majerus, P.W.2
  • 29
    • 0037447066 scopus 로고    scopus 로고
    • Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase
    • Kim, S.A., Vacratsis, P.O., Firestein, R., Cleary, M.L. and Dixon, J.E. (2003) Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase. Proc. Natl Acad. Sci. USA, 100, 4492-4497.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 4492-4497
    • Kim, S.A.1    Vacratsis, P.O.2    Firestein, R.3    Cleary, M.L.4    Dixon, J.E.5
  • 30
    • 24744446022 scopus 로고    scopus 로고
    • The phosphoinositide 3-phosphatase MTMR2 associates with MTMR13, a novel membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-Tooth disease
    • Robinson, F.L. and Dixon, J.E. (2005) The phosphoinositide 3-phosphatase MTMR2 associates with MTMR13, a novel membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-Tooth disease. J. Biol. Chem., 280, 31699-31707.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31699-31707
    • Robinson, F.L.1    Dixon, J.E.2
  • 31
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger, I., Fitzgerald, D.J. and Richmond, T.J. (2004) Baculovirus expression system for heterologous multiprotein complexes. Nat. Biotechnol., 22, 1583-1587.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 32
    • 0346156077 scopus 로고    scopus 로고
    • Crystal structure of a phosphoinositide phosphatase, MTMR2: Insights into myotubular myopathy and Charcot-Marie-Tooth syndrome
    • Begley, M.J., Taylor, G.S., Kim, S.A., Veine, D.M., Dixon, J.E. and Stuckey, J.A. (2003) Crystal structure of a phosphoinositide phosphatase, MTMR2: Insights into myotubular myopathy and Charcot-Marie-Tooth syndrome. Mol. Cell, 12, 1391-1402.
    • (2003) Mol. Cell , vol.12 , pp. 1391-1402
    • Begley, M.J.1    Taylor, G.S.2    Kim, S.A.3    Veine, D.M.4    Dixon, J.E.5    Stuckey, J.A.6
  • 33
    • 0034306454 scopus 로고    scopus 로고
    • GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins
    • Doerks, T., Strauss, M., Brendel, M. and Bork, P. (2000) GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Trends Biochem. Sci., 25, 483-485.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 483-485
    • Doerks, T.1    Strauss, M.2    Brendel, M.3    Bork, P.4
  • 34
  • 35
    • 0030669546 scopus 로고    scopus 로고
    • Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis
    • Dove, S.K., Cooke, F.T., Douglas, M.R., Sayers, L.G., Parker, P.J. and Michell, R.H. (1997) Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis. Nature, 390, 187-192.
    • (1997) Nature , vol.390 , pp. 187-192
    • Dove, S.K.1    Cooke, F.T.2    Douglas, M.R.3    Sayers, L.G.4    Parker, P.J.5    Michell, R.H.6
  • 36
    • 0038959159 scopus 로고    scopus 로고
    • The identification of phosphatidylinositol 3,5-bisphosphate in T-lymphocytes and its regulation by interleukin-2
    • Jones, D.R., Gonzalez-Garcia, A., Diez, E., Martinez, A.C., Carrera, A.C. and Merida, I. (1999) The identification of phosphatidylinositol 3,5-bisphosphate in T-lymphocytes and its regulation by interleukin-2. J. Biol. Chem., 274, 18407-18413.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18407-18413
    • Jones, D.R.1    Gonzalez-Garcia, A.2    Diez, E.3    Martinez, A.C.4    Carrera, A.C.5    Merida, I.6
  • 37
    • 0041808715 scopus 로고    scopus 로고
    • Myotubularin-related 2 protein phosphatase and neurofilament light chain protein, both mutated in CMT neuropathies, interact in peripheral nerve
    • Previtali, S.C., Zerega, B., Sherman, D.L., Brophy, P.J., Dina, G., King, R.H., Salih, M.M., Feltri, L., Quattrini, A., Ravazzolo, R. et al. (2003) Myotubularin-related 2 protein phosphatase and neurofilament light chain protein, both mutated in CMT neuropathies, interact in peripheral nerve. Hum. Mol. Genet., 12, 1713-1723.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1713-1723
    • Previtali, S.C.1    Zerega, B.2    Sherman, D.L.3    Brophy, P.J.4    Dina, G.5    King, R.H.6    Salih, M.M.7    Feltri, L.8    Quattrini, A.9    Ravazzolo, R.10


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