메뉴 건너뛰기




Volumn 11, Issue 6, 2009, Pages 769-776

Deficiency of MIP/MTMR14 phosphatase induces a muscle disorder by disrupting Ca2+ homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; MUSCLE SPECIFIC INOSITOL PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4 BISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,5 BISPHOSPHATE; RYANODINE RECEPTOR 1; UNCLASSIFIED DRUG;

EID: 67349251211     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1884     Document Type: Article
Times cited : (86)

References (32)
  • 1
    • 0033624484 scopus 로고    scopus 로고
    • MacLennan, D. H. Ca2+ signalling and muscle disease. Eur. J. Biochem. 267, 5291-5297 (2000).
    • MacLennan, D. H. Ca2+ signalling and muscle disease. Eur. J. Biochem. 267, 5291-5297 (2000).
  • 2
    • 0036899518 scopus 로고    scopus 로고
    • PTEN and myotubularin phosphatases: From 3-phosphoinositide dephosphorylation to disease
    • Wishart, M. J. & Dixon, J. E. PTEN and myotubularin phosphatases: From 3-phosphoinositide dephosphorylation to disease. Trends Cell Biol. 12, 579-585 (2002).
    • (2002) Trends Cell Biol , vol.12 , pp. 579-585
    • Wishart, M.J.1    Dixon, J.E.2
  • 3
    • 2942581416 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the human genome
    • Alonso, A. et al. Protein tyrosine phosphatases in the human genome. Cell 117, 699-711 (2004).
    • (2004) Cell , vol.117 , pp. 699-711
    • Alonso, A.1
  • 4
    • 33750219395 scopus 로고    scopus 로고
    • Tosch, V. et al. A novel PtdIns3P and PtdIns(3, 5)P2 phosphatase with an inactivating variant in centronuclear myopathy. Hum. Mol. Genet. 15, 3098-3106 (2006).
    • Tosch, V. et al. A novel PtdIns3P and PtdIns(3, 5)P2 phosphatase with an inactivating variant in centronuclear myopathy. Hum. Mol. Genet. 15, 3098-3106 (2006).
  • 5
    • 33645754718 scopus 로고    scopus 로고
    • Enhanced resistance to fatigue and altered calcium handling properties of sarcalumenin knockout mice
    • Zhao, X. et al. Enhanced resistance to fatigue and altered calcium handling properties of sarcalumenin knockout mice. Physiol. Genomics 23, 72-78 (2005).
    • (2005) Physiol. Genomics , vol.23 , pp. 72-78
    • Zhao, X.1
  • 6
    • 0034626683 scopus 로고    scopus 로고
    • Increased susceptibility to fatigue of slow- and fast-twitch muscles from mice lacking the MG29 gene
    • Nagaraj, R. Y. et al. Increased susceptibility to fatigue of slow- and fast-twitch muscles from mice lacking the MG29 gene. Physiol. Genomics 4, 43-49 (2000).
    • (2000) Physiol. Genomics , vol.4 , pp. 43-49
    • Nagaraj, R.Y.1
  • 7
    • 0034626669 scopus 로고    scopus 로고
    • Functional properties of skeletal muscle from transgenic animals with upregulated heat shock protein 70
    • Nosek, T. M. et al. Functional properties of skeletal muscle from transgenic animals with upregulated heat shock protein 70. Physiol. Genomics 4, 25-33 (2000).
    • (2000) Physiol. Genomics , vol.4 , pp. 25-33
    • Nosek, T.M.1
  • 8
    • 0028332473 scopus 로고
    • Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene
    • Takeshima, H. et al. Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene. Nature 369, 556-559 (1994).
    • (1994) Nature , vol.369 , pp. 556-559
    • Takeshima, H.1
  • 9
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai, F. A., Erickson, H. P., Rousseau, E., Liu, Q. Y. & Meissner, G. Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 331, 315-319 (1988).
    • (1988) Nature , vol.331 , pp. 315-319
    • Lai, F.A.1    Erickson, H.P.2    Rousseau, E.3    Liu, Q.Y.4    Meissner, G.5
  • 10
    • 0036098555 scopus 로고    scopus 로고
    • Dysfunction of store-operated calcium channel in muscle cells lacking mg29
    • Pan, Z. et al. Dysfunction of store-operated calcium channel in muscle cells lacking mg29. Nature Cell Biol. 4, 379-383 (2002).
    • (2002) Nature Cell Biol , vol.4 , pp. 379-383
    • Pan, Z.1
  • 11
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • Thastrup, O., Cullen, P. J., Drobak, B. K., Hanley, M. R. & Dawson, A. P. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase. Proc. Natl Acad. Sci. USA 87, 2466-2470 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 12
    • 33947243452 scopus 로고    scopus 로고
    • The molecular choreography of a store-operated calcium channel
    • Lewis, R. S. The molecular choreography of a store-operated calcium channel. Nature 446, 284-287 (2007).
    • (2007) Nature , vol.446 , pp. 284-287
    • Lewis, R.S.1
  • 13
    • 0025103909 scopus 로고
    • SKF 96365, a novel inhibitor of receptor-mediated calcium entry
    • Merritt, J. E. et al. SKF 96365, a novel inhibitor of receptor-mediated calcium entry. Biochem. J. 271, 515-522 (1990).
    • (1990) Biochem. J , vol.271 , pp. 515-522
    • Merritt, J.E.1
  • 14
    • 0031766729 scopus 로고    scopus 로고
    • Depletion of sarcoplasmic reticulum calcium prompts phosphorylation of phospholamban to stimulate store refilling
    • Bhogal, M. S. & Colyer, J. Depletion of sarcoplasmic reticulum calcium prompts phosphorylation of phospholamban to stimulate store refilling. Ann. NY Acad. Sci. 853, 260-263 (1998).
    • (1998) Ann. NY Acad. Sci , vol.853 , pp. 260-263
    • Bhogal, M.S.1    Colyer, J.2
  • 15
    • 0032210152 scopus 로고    scopus 로고
    • Quantitative assessment of [Ca2+]i levels in rat skeletal muscle in vivo
    • Toth, A. et al. Quantitative assessment of [Ca2+]i levels in rat skeletal muscle in vivo. Am. J. Physiol. 275, H1652-1662 (1998).
    • (1998) Am. J. Physiol , vol.275
    • Toth, A.1
  • 16
    • 30944461203 scopus 로고    scopus 로고
    • Phosphatidylinositol 3, 5-bisphosphate: Metabolism and cellular functions
    • Michell, R. H., Heath, V. L., Lemmon, M. A. & Dove, S. K. Phosphatidylinositol 3, 5-bisphosphate: Metabolism and cellular functions. Trends Biochem. Sci. 31, 52-63 (2006).
    • (2006) Trends Biochem. Sci , vol.31 , pp. 52-63
    • Michell, R.H.1    Heath, V.L.2    Lemmon, M.A.3    Dove, S.K.4
  • 17
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo, G. & De Camilli, P. Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651-657 (2006).
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 18
    • 33845789522 scopus 로고    scopus 로고
    • Min., J. et al. Forward chemical genetic approach identifies new role for GAPDH in insulin signaling. Nature Chem. Biol. 3, 55-59 (2007).
    • Min., J. et al. Forward chemical genetic approach identifies new role for GAPDH in insulin signaling. Nature Chem. Biol. 3, 55-59 (2007).
  • 19
    • 0037371512 scopus 로고    scopus 로고
    • Immunocytochemical detection of phosphatidylinositol 3-kinase activation by insulin and leptin
    • Niswender, K. D. et al. Immunocytochemical detection of phosphatidylinositol 3-kinase activation by insulin and leptin. J. Histochem. Cytochem. 51, 275-283 (2003).
    • (2003) J. Histochem. Cytochem , vol.51 , pp. 275-283
    • Niswender, K.D.1
  • 20
    • 0028304865 scopus 로고
    • Na(+)-, ouabain-, Ca(2+)-, and thapsigargin-sensitive ATPase activity expressed in chimeras between the calcium and the sodium pump alpha subunits
    • Ishii, T., Lemas, M. V. & Takeyasu, K. Na(+)-, ouabain-, Ca(2+)-, and thapsigargin-sensitive ATPase activity expressed in chimeras between the calcium and the sodium pump alpha subunits. Proc. Natl Acad. Sci. USA 91, 6103-6107 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6103-6107
    • Ishii, T.1    Lemas, M.V.2    Takeyasu, K.3
  • 21
    • 33646905484 scopus 로고    scopus 로고
    • Clotrimazole inhibits the Ca2+-ATPase (SERCA) by interfering with Ca2+ binding and favoring the E2 conformation
    • Bartolommei, G. et al. Clotrimazole inhibits the Ca2+-ATPase (SERCA) by interfering with Ca2+ binding and favoring the E2 conformation. J. Biol. Chem. 281, 9547-9551 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 9547-9551
    • Bartolommei, G.1
  • 22
    • 0346789109 scopus 로고    scopus 로고
    • Pharmacology of KB-R7943: A Na+-Ca2+ exchange inhibitor
    • Amran, M. S., Homma, N. & Hashimoto, K. Pharmacology of KB-R7943: A Na+-Ca2+ exchange inhibitor. Cardiovasc. Drug Rev. 21, 255-276 (2003).
    • (2003) Cardiovasc. Drug Rev , vol.21 , pp. 255-276
    • Amran, M.S.1    Homma, N.2    Hashimoto, K.3
  • 23
    • 44649184084 scopus 로고    scopus 로고
    • Congenital muscle disorders with cores: The ryanodine receptor calcium channel paradigm
    • Treves, S., Jungbluth, H., Muntoni, F. & Zorzato, F. Congenital muscle disorders with cores: The ryanodine receptor calcium channel paradigm. Curr. Opin. Pharmacol. 8, 319-326 (2008).
    • (2008) Curr. Opin. Pharmacol , vol.8 , pp. 319-326
    • Treves, S.1    Jungbluth, H.2    Muntoni, F.3    Zorzato, F.4
  • 25
    • 2942739035 scopus 로고    scopus 로고
    • Activation of skeletal ryanodine receptors by two novel scorpion toxins from Buthotus judaicus
    • Zhu, X., Zamudio, F. Z., Olbinski, B. A., Possani, L. D. & Valdivia, H. H. Activation of skeletal ryanodine receptors by two novel scorpion toxins from Buthotus judaicus. J. Biol. Chem. 279, 26588-26596 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 26588-26596
    • Zhu, X.1    Zamudio, F.Z.2    Olbinski, B.A.3    Possani, L.D.4    Valdivia, H.H.5
  • 26
    • 0942287935 scopus 로고    scopus 로고
    • The calmodulin binding region of the skeletal ryanodine receptor acts as a self-modulatory domain
    • Zhu, X., Ghanta, J., Walker, J. W., Allen, P. D. & Valdivia, H. H. The calmodulin binding region of the skeletal ryanodine receptor acts as a self-modulatory domain. Cell Calcium 35, 165-177 (2004).
    • (2004) Cell Calcium , vol.35 , pp. 165-177
    • Zhu, X.1    Ghanta, J.2    Walker, J.W.3    Allen, P.D.4    Valdivia, H.H.5
  • 27
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with ion channels and transporters
    • Hilgemann, D. W., Feng, S. & Nasuhoglu, C. The complex and intriguing lives of PIP2 with ion channels and transporters. Sci. STKE 2001, RE19 (2001).
    • (2001) Sci. STKE , vol.2001
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 28
    • 0036148860 scopus 로고    scopus 로고
    • Influence of ageing on the fatigability of isolated mouse skeletal muscles from mature and aged mice
    • Brotto, M. A., Nosek, T. M. & Kolbeck, R. C. Influence of ageing on the fatigability of isolated mouse skeletal muscles from mature and aged mice. Exp. Physiol. 87, 77-82 (2002).
    • (2002) Exp. Physiol , vol.87 , pp. 77-82
    • Brotto, M.A.1    Nosek, T.M.2    Kolbeck, R.C.3
  • 29
    • 32644447630 scopus 로고    scopus 로고
    • Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiation
    • Frock, R. L. et al. Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiation. Genes Dev. 20, 486-500 (2006).
    • (2006) Genes Dev , vol.20 , pp. 486-500
    • Frock, R.L.1
  • 30
    • 0037474297 scopus 로고    scopus 로고
    • A retrograde signal from calsequestrin for the regulation of storeoperated Ca2+ entry in skeletal muscle
    • Shin, D. W. et al. A retrograde signal from calsequestrin for the regulation of storeoperated Ca2+ entry in skeletal muscle. J. Biol. Chem. 278, 3286-3292 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 3286-3292
    • Shin, D.W.1
  • 31
    • 0036143029 scopus 로고    scopus 로고
    • A small-molecule inhibitor of skeletal muscle myosin II
    • Cheung, A. et al. A small-molecule inhibitor of skeletal muscle myosin II. Nature Cell Biol. 4, 83-88 (2002).
    • (2002) Nature Cell Biol , vol.4 , pp. 83-88
    • Cheung, A.1
  • 32
    • 0030832574 scopus 로고    scopus 로고
    • Jacquemond, V. Indo-1 fluorescence signals elicited by membrane depolarization in enzymatically isolated mouse skeletal muscle fibers. Biophys. J. 73, 920-928 (1997).
    • Jacquemond, V. Indo-1 fluorescence signals elicited by membrane depolarization in enzymatically isolated mouse skeletal muscle fibers. Biophys. J. 73, 920-928 (1997).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.