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Volumn 15, Issue 2, 2006, Pages 189-199

Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CELL PROTEIN; MUTANT PROTEIN; PROTEASOME; PROTEIN P97; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN;

EID: 31144470450     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddi426     Document Type: Article
Times cited : (160)

References (40)
  • 1
    • 0036797633 scopus 로고    scopus 로고
    • Inclusion-body myositis and myopathies: Different etiologies, possibly similar pathogenic mechanisms
    • Askanas, V. and Engel, W.K. (2002) Inclusion-body myositis and myopathies: Different etiologies, possibly similar pathogenic mechanisms. Curr. Opin. Neurol., 15, 525-531.
    • (2002) Curr. Opin. Neurol. , vol.15 , pp. 525-531
    • Askanas, V.1    Engel, W.K.2
  • 2
    • 0034513218 scopus 로고    scopus 로고
    • 'Fatal attractions' of proteins. A comprehensive hypothetical mechanism underlying Alzheimer's disease and other neurodegenerative disorders
    • Trojanowski, J.Q. and Lee, V.M. (2000) 'Fatal attractions' of proteins. A comprehensive hypothetical mechanism underlying Alzheimer's disease and other neurodegenerative disorders. Ann. NY Acad. Sci., 924, 62-67.
    • (2000) Ann. NY Acad. Sci. , vol.924 , pp. 62-67
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 3
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts, G.D., Wymer, J., Kovach, M.J., Mehta, S.G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M.P. and Kimonis, V.E. (2004) Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat. Genet., 36, 377-381.
    • (2004) Nat. Genet. , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6    Pestronk, A.7    Whyte, M.P.8    Kimonis, V.E.9
  • 5
    • 23844549677 scopus 로고    scopus 로고
    • Golgi reassembly after mitosis: The AAA family meets the ubiquitin family
    • Meyer, H.H. (2005) Golgi reassembly after mitosis: The AAA family meets the ubiquitin family. Biochim. Biophys. Acta, 1744, 481-492.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 481-492
    • Meyer, H.H.1
  • 6
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure - Diverse function
    • Ogura, T. and Wilkinson, A.J. (2001) AAA+ superfamily ATPases: Common structure - diverse function. Genes Cells, 6, 575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 8
    • 0242635839 scopus 로고    scopus 로고
    • p97, a protein coping with multiple identities
    • Woodman, P.G. (2003) p97, a protein coping with multiple identities. J. Cell. Sci., 116, 4283-4290.
    • (2003) J. Cell. Sci. , vol.116 , pp. 4283-4290
    • Woodman, P.G.1
  • 10
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai, R.M. and Li, C.C. (2001) Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell. Biol., 3, 740-744.
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 11
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha
    • Dai, R.M., Chen, E., Longo, D.L., Gorbea, C.M. and Li, C.C. (1998) Involvement of valosin-containing protein an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. J. Biol. Chem., 273, 3562-3573.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.C.5
  • 13
    • 8544263881 scopus 로고    scopus 로고
    • AAA ATPase p97/VCP interacts with gp78: A ubiquitin ligase for ER-associated degradation
    • Zhong, X., Shen, Y., Ballar, P., Apostolou, A., Agami, R. and Fang, S. (2004) AAA ATPase p97/VCP interacts with gp78: A ubiquitin ligase for ER-associated degradation. J. Biol. Chem., 279, 45676-45684.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45676-45684
    • Zhong, X.1    Shen, Y.2    Ballar, P.3    Apostolou, A.4    Agami, R.5    Fang, S.6
  • 14
    • 1842509180 scopus 로고    scopus 로고
    • VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments
    • Wang, Y., Satoh, A., Warren, G. and Meyer, H.H. (2004) VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments. J. Cell. Biol., 164, 973-978.
    • (2004) J. Cell. Biol. , vol.164 , pp. 973-978
    • Wang, Y.1    Satoh, A.2    Warren, G.3    Meyer, H.H.4
  • 15
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • Doss-Pepe, E.W., Stenroos, E.S., Johnson, W.G. and Madura, K. (2003) Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis. Mol. Cell. Biol., 23, 6469-6483.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 16
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H.H. and Rapoport, T.A. (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature, 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 17
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Frohlich, K.U., Diamant, N. and Bar-Nun, S. (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol., 22, 626-634.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 18
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D. and Rapoport, T.A. (2004) A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature, 429, 841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 19
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley, B.N. and Ploegh, H.L. (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature, 429, 834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 20
    • 0037986563 scopus 로고    scopus 로고
    • Vacuole-creating protein in neurodegenerative diseases in humans
    • Mizuno, Y., Hori, S., Kakizuka, A. and Okamoto, K. (2003) Vacuole-creating protein in neurodegenerative diseases in humans. Neurosci. Lett., 343, 77-80.
    • (2003) Neurosci. Lett. , vol.343 , pp. 77-80
    • Mizuno, Y.1    Hori, S.2    Kakizuka, A.3    Okamoto, K.4
  • 23
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre, B. and Brunger, A.T. (2003) Complete structure of p97/ valosin-containing protein reveals communication between nucleotide domains. Nat. Struct. Biol., 10, 856-863.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 856-863
    • DeLaBarre, B.1    Brunger, A.T.2
  • 24
    • 14644415865 scopus 로고    scopus 로고
    • Nucleotide dependent motion and mechanism of action of p97/VCP
    • DeLaBarre, B. and Brunger, A.T. (2005) Nucleotide dependent motion and mechanism of action of p97/VCP. J. Mol. Biol., 347, 437-452.
    • (2005) J. Mol. Biol. , vol.347 , pp. 437-452
    • DeLaBarre, B.1    Brunger, A.T.2
  • 25
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • Dalal, S., Rosser, M.F., Cyr, D.M. and Hanson, P.I. (2004) Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Mol. Biol. Cell., 15, 637-648.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.2    Cyr, D.M.3    Hanson, P.I.4
  • 26
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • Fujimuro, M., Sawada, H. and Yokosawa, H. (1994) Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett., 349, 173-180.
    • (1994) FEBS Lett. , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 27
    • 0347298790 scopus 로고    scopus 로고
    • Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells
    • Kobayashi, T., Tanaka, K., Inoue, K. and Kakizuka, A. (2002) Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells. J. Biol. Chem., 277, 47359-47365.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47359-47365
    • Kobayashi, T.1    Tanaka, K.2    Inoue, K.3    Kakizuka, A.4
  • 28
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L. and Riordan, J.R. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing, Cell, 83, 129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 29
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S. and Kopito, R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell, 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 30
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston, J.A., Dalton, M.J., Gurney, M.E. and Kopito, R.R. (2000) Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl Acad. Sci. USA, 97, 12571-12576.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 31
    • 4444301749 scopus 로고    scopus 로고
    • Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms
    • Ilkovski, B., Nowak, K.J., Domazetovska, A., Maxwell, A.L., Clement, S., Davies, K.E., Laing, N.G., North, K.N. and Cooper, S.T. (2004) Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms. Hum. Mol. Genet., 13, 1727-1743.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1727-1743
    • Ilkovski, B.1    Nowak, K.J.2    Domazetovska, A.3    Maxwell, A.L.4    Clement, S.5    Davies, K.E.6    Laing, N.G.7    North, K.N.8    Cooper, S.T.9
  • 32
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J.A., Ward, C.L. and Kopito, R.R. (1998) Aggresomes: A cellular response to misfolded proteins. J. Cell. Biol., 143, 1883-1898.
    • (1998) J. Cell. Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 34
    • 0029564918 scopus 로고
    • Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment
    • Raposo, G., van Santen, H.M., Leijendekker, R., Geuze, H.J. and Ploegh, H.L. (1995) Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment. J. Cell. Biol., 131, 1403-1419.
    • (1995) J. Cell. Biol. , vol.131 , pp. 1403-1419
    • Raposo, G.1    van Santen, H.M.2    Leijendekker, R.3    Geuze, H.J.4    Ploegh, H.L.5
  • 35
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F., Sampat, R.M. and Kopito, R.R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science, 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 36
    • 26444494585 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress compromises the ubiquitin-proteasome system
    • Menendez-Benito, V., Verhoef, L.G., Masucci, M.G. and Dantuma, N.P. (2005) Endoplasmic reticulum stress compromises the ubiquitin-proteasome system. Hum. Mol. Genet., 14, 2787-2799.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2787-2799
    • Menendez-Benito, V.1    Verhoef, L.G.2    Masucci, M.G.3    Dantuma, N.P.4
  • 38
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi, G., Engel, W.K., McFerrin, J. and Askanas, V. (2004) Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am. J. Pathol., 164, 1-7.
    • (2004) Am. J. Pathol. , vol.164 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 39
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R. and Heuser, J.E. (1997) Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell, 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.