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Volumn 127, Issue 18, 2014, Pages 3877-3883

The VCP/p97 system at a glance: Connecting cellular function to disease pathogenesis

Author keywords

ALS; Cdc48; IBMPFD; p97; Ubiquitin; VCP

Indexed keywords

PROTEIN P97; RNA; UBIQUITIN; VALOSIN CONTAINING PROTEIN; ADENOSINE TRIPHOSPHATASE; CDC48 PROTEIN; CELL CYCLE PROTEIN;

EID: 84907059487     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.093831     Document Type: Article
Times cited : (338)

References (102)
  • 2
    • 82955233157 scopus 로고    scopus 로고
    • The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
    • Acs, K., Luijsterburg, M. S., Ackermann, L., Salomons, F. A., Hoppe, T. and Dantuma, N. P. (2011). The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18, 1345-1350.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1345-1350
    • Acs, K.1    Luijsterburg, M.S.2    Ackermann, L.3    Salomons, F.A.4    Hoppe, T.5    Dantuma, N.P.6
  • 3
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover
    • Alexandru, G., Graumann, J., Smith, G. T., Kolawa, N. J., Fang, R. and Deshaies, R. J. (2008). UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134, 804-816.
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5    Deshaies, R.J.6
  • 4
    • 78049244477 scopus 로고    scopus 로고
    • VCP associated inclusion body myopathy and paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease
    • Badadani, M., Nalbandian, A., Watts, G. D., Vesa, J., Kitazawa, M., Su, H., Tanaja, J., Dec, E., Wallace, D. C., Mukherjee, J. et al. (2010). VCP associated inclusion body myopathy and paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease. PLoS ONE 5, e13183.
    • (2010) PLoS ONE , vol.5 , pp. e13183
    • Badadani, M.1    Nalbandian, A.2    Watts, G.D.3    Vesa, J.4    Kitazawa, M.5    Su, H.6    Tanaja, J.7    Dec, E.8    Wallace, D.C.9    Mukherjee, J.10
  • 6
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson, M. H. and Joazeiro, C. A. (2010). Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 467, 470-473.
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 8
    • 70449524302 scopus 로고    scopus 로고
    • A conserved unfoldase activity for the p97 AAA-ATPase in proteasomal degradation
    • Beskow, A., Grimberg, K. B., Bott, L. C., Salomons, F. A., Dantuma, N. P. and Young, P. (2009). A conserved unfoldase activity for the p97 AAA-ATPase in proteasomal degradation. J. Mol. Biol. 394, 732-746.
    • (2009) J. Mol. Biol. , vol.394 , pp. 732-746
    • Beskow, A.1    Grimberg, K.B.2    Bott, L.C.3    Salomons, F.A.4    Dantuma, N.P.5    Young, P.6
  • 10
    • 0242573090 scopus 로고    scopus 로고
    • NSF and p97/VCP: similar at first, different at last
    • Brunger, A. T. and DeLaBarre, B. (2003). NSF and p97/VCP: similar at first, different at last. FEBS Lett. 555, 126-133.
    • (2003) FEBS Lett. , vol.555 , pp. 126-133
    • Brunger, A.T.1    DeLaBarre, B.2
  • 11
    • 84879349589 scopus 로고    scopus 로고
    • Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function
    • Buchan, J. R., Kolaitis, R. M., Taylor, J. P. and Parker, R. (2013). Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell 153, 1461-1474.
    • (2013) Cell , vol.153 , pp. 1461-1474
    • Buchan, J.R.1    Kolaitis, R.M.2    Taylor, J.P.3    Parker, R.4
  • 12
    • 84864385646 scopus 로고    scopus 로고
    • Expanding into new markets-VCP/p97 in endocytosis and autophagy
    • Bug, M. and Meyer, H. (2012). Expanding into new markets-VCP/p97 in endocytosis and autophagy. J. Struct. Biol. 179, 78-82.
    • (2012) J. Struct. Biol. , vol.179 , pp. 78-82
    • Bug, M.1    Meyer, H.2
  • 13
    • 0344845397 scopus 로고    scopus 로고
    • The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis
    • Cao, K., Nakajima, R., Meyer, H. H. and Zheng, Y. (2003). The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell 115, 355- 367.
    • (2003) Cell , vol.115 , pp. 355- 367
    • Cao, K.1    Nakajima, R.2    Meyer, H.H.3    Zheng, Y.4
  • 18
    • 0029904102 scopus 로고    scopus 로고
    • Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene
    • DeHoratius, C. and Silver, P. A. (1996). Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene. Mol. Biol. Cell 7, 1835-1855.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1835-1855
    • DeHoratius, C.1    Silver, P.A.2
  • 19
    • 62849091775 scopus 로고    scopus 로고
    • A novel mutation in the VCP gene (G157R) in a German family with inclusion-body myopathy with Paget disease of bone and frontotemporal dementia
    • Djamshidian, A., Schaefer, J., Haubenberger, D., Stogmann, E., Zimprich, F., Auff, E. and Zimprich, A. (2009). A novel mutation in the VCP gene (G157R) in a German family with inclusion-body myopathy with Paget disease of bone and frontotemporal dementia. Muscle Nerve 39, 389-391.
    • (2009) Muscle Nerve , vol.39 , pp. 389-391
    • Djamshidian, A.1    Schaefer, J.2    Haubenberger, D.3    Stogmann, E.4    Zimprich, F.5    Auff, E.6    Zimprich, A.7
  • 20
    • 79955528965 scopus 로고    scopus 로고
    • Cdc48/p97-Ufd1-Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells
    • Dobrynin, G., Popp, O., Romer, T., Bremer, S., Schmitz, M. H., Gerlich, D. W. and Meyer, H. (2011). Cdc48/p97-Ufd1-Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells. J. Cell Sci. 124, 1571-1580.
    • (2011) J. Cell Sci. , vol.124 , pp. 1571-1580
    • Dobrynin, G.1    Popp, O.2    Romer, T.3    Bremer, S.4    Schmitz, M.H.5    Gerlich, D.W.6    Meyer, H.7
  • 22
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger, J. P. and Berger, J. M. (2006). Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35, 93-114.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 23
    • 84873699402 scopus 로고    scopus 로고
    • A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization
    • Erzurumlu, Y., Kose, F. A., Gozen, O., Gozuacik, D., Toth, E. A. and Ballar, P. (2013). A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization. Int. J. Biochem. Cell Biol. 45, 773-782.
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 773-782
    • Erzurumlu, Y.1    Kose, F.A.2    Gozen, O.3    Gozuacik, D.4    Toth, E.A.5    Ballar, P.6
  • 25
    • 77953121380 scopus 로고    scopus 로고
    • Imbalances in p97 co-factor interactions in human proteinopathy
    • Ferna´ndez-Sa´iz, V. and Buchberger, A. (2010). Imbalances in p97 co-factor interactions in human proteinopathy. EMBO Rep. 11, 479-485.
    • (2010) EMBO Rep. , vol.11 , pp. 479-485
    • Ferna´ndez-Sa´iz, V.1    Buchberger, A.2
  • 26
    • 0142059989 scopus 로고    scopus 로고
    • Cdc48p is required for the cell cycle commitment point at Start via degradation of the G1-CDK inhibitor Far1p
    • Fu, X., Ng, C., Feng, D. and Liang, C. (2003). Cdc48p is required for the cell cycle commitment point at Start via degradation of the G1-CDK inhibitor Far1p. J. Cell Biol. 163, 21-26.
    • (2003) J. Cell Biol. , vol.163 , pp. 21-26
    • Fu, X.1    Ng, C.2    Feng, D.3    Liang, C.4
  • 27
    • 84861913529 scopus 로고    scopus 로고
    • 40S subunit dissociation and proteasome-dependent RNA degradation in nonfunctional 25S rRNA decay
    • Fujii, K., Kitabatake, M., Sakata, T. and Ohno, M. (2012). 40S subunit dissociation and proteasome-dependent RNA degradation in nonfunctional 25S rRNA decay. EMBO J. 31, 2579-2589.
    • (2012) EMBO J. , vol.31 , pp. 2579-2589
    • Fujii, K.1    Kitabatake, M.2    Sakata, T.3    Ohno, M.4
  • 28
    • 84899728488 scopus 로고    scopus 로고
    • The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility
    • Gallagher, P. S., Clowes Candadai, S. V. and Gardner, R. G. (2014). The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility. J. Cell Sci. 127, 1980-1991.
    • (2014) J. Cell Sci. , vol.127 , pp. 1980-1991
    • Gallagher, P.S.1    Clowes Candadai, S.V.2    Gardner, R.G.3
  • 29
    • 77957352000 scopus 로고    scopus 로고
    • Inactivation of VCP/ter94 suppresses retinal pathology caused by misfolded rhodopsin in Drosophila
    • Griciuc, A., Aron, L., Roux, M. J., Klein, R., Giangrande, A. and Ueffing, M. (2010). Inactivation of VCP/ter94 suppresses retinal pathology caused by misfolded rhodopsin in Drosophila. PLoS Genet. 6, e1001075.
    • (2010) PLoS Genet. , vol.6 , pp. e1001075
    • Griciuc, A.1    Aron, L.2    Roux, M.J.3    Klein, R.4    Giangrande, A.5    Ueffing, M.6
  • 32
    • 68949098348 scopus 로고    scopus 로고
    • Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation
    • Halawani, D., LeBlanc, A. C., Rouiller, I., Michnick, S. W., Servant, M. J. and Latterich, M. (2009). Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation. Mol. Cell. Biol. 29, 4484-4494.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4484-4494
    • Halawani, D.1    LeBlanc, A.C.2    Rouiller, I.3    Michnick, S.W.4    Servant, M.J.5    Latterich, M.6
  • 35
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?
    • Jentsch, S. and Rumpf, S. (2007). Cdc48 (p97): a ''molecular gearbox'' in the ubiquitin pathway? Trends Biochem. Sci. 32, 6-11.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 36
    • 77953180920 scopus 로고    scopus 로고
    • p97/VCP at the intersection of the autophagy and the ubiquitin proteasome system
    • Ju, J. S. and Weihl, C. C. (2010). p97/VCP at the intersection of the autophagy and the ubiquitin proteasome system. Autophagy 6, 283-285.
    • (2010) Autophagy , vol.6 , pp. 283-285
    • Ju, J.S.1    Weihl, C.C.2
  • 37
    • 57649198447 scopus 로고    scopus 로고
    • Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCPassociated disease
    • Ju, J. S., Miller, S. E., Hanson, P. I. and Weihl, C. C. (2008). Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCPassociated disease. J. Biol. Chem. 283, 30289-30299.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30289-30299
    • Ju, J.S.1    Miller, S.E.2    Hanson, P.I.3    Weihl, C.C.4
  • 41
    • 56449111307 scopus 로고    scopus 로고
    • VCP disease associated with myopathy, Paget disease of bone and frontotemporal dementia: review of a unique disorder
    • Kimonis, V. E., Fulchiero, E., Vesa, J. and Watts, G. (2008). VCP disease associated with myopathy, Paget disease of bone and frontotemporal dementia: review of a unique disorder. Biochim. Biophys. Acta 1782, 744-748.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 744-748
    • Kimonis, V.E.1    Fulchiero, E.2    Vesa, J.3    Watts, G.4
  • 44
    • 18244381306 scopus 로고    scopus 로고
    • Clinical delineation and localization to chromosome 9p13.3-p12 of a unique dominant disorder in four families: hereditary inclusion body myopathy, Paget disease of bone, and frontotemporal dementia
    • Kovach, M. J., Waggoner, B., Leal, S. M., Gelber, D., Khardori, R., Levenstien, M. A., Shanks, C. A., Gregg, G., Al-Lozi, M. T., Miller, T. et al. (2001). Clinical delineation and localization to chromosome 9p13.3-p12 of a unique dominant disorder in four families: hereditary inclusion body myopathy, Paget disease of bone, and frontotemporal dementia. Mol. Genet. Metab. 74, 458-475.
    • (2001) Mol. Genet. Metab. , vol.74 , pp. 458-475
    • Kovach, M.J.1    Waggoner, B.2    Leal, S.M.3    Gelber, D.4    Khardori, R.5    Levenstien, M.A.6    Shanks, C.A.7    Gregg, G.8    Al-Lozi, M.T.9    Miller, T.10
  • 46
    • 77957200921 scopus 로고    scopus 로고
    • Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8
    • Krick, R., Bremer, S., Welter, E., Schlotterhose, P., Muehe, Y., Eskelinen, E. L. and Thumm, M. (2010). Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8. J. Cell Biol. 190, 965-973.
    • (2010) J. Cell Biol. , vol.190 , pp. 965-973
    • Krick, R.1    Bremer, S.2    Welter, E.3    Schlotterhose, P.4    Muehe, Y.5    Eskelinen, E.L.6    Thumm, M.7
  • 47
    • 30044436220 scopus 로고    scopus 로고
    • Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ
    • Kruse, K. B., Brodsky, J. L. and McCracken, A. A. (2006). Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ. Mol. Biol. Cell 17, 203-212.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 203-212
    • Kruse, K.B.1    Brodsky, J.L.2    McCracken, A.A.3
  • 48
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation-the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu, Y. and Komander, D. (2012). Atypical ubiquitylation-the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat. Rev. Mol. Cell Biol. 13, 508-523.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 50
    • 0036094026 scopus 로고    scopus 로고
    • Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone
    • Laurin, N., Brown, J. P., Morissette, J. and Raymond, V. (2002). Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone. Am. J. Hum. Genet. 70, 1582-1588.
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 1582-1588
    • Laurin, N.1    Brown, J.P.2    Morissette, J.3    Raymond, V.4
  • 51
    • 84892448171 scopus 로고    scopus 로고
    • The p97- UFD1L-NPL4 protein complex mediates cytokine-induced IkBa proteolysis
    • Li, J. M., Wu, H., Zhang, W., Blackburn, M. R. and Jin, J. (2014). The p97- UFD1L-NPL4 protein complex mediates cytokine-induced IkBa proteolysis. Mol. Cell. Biol. 34, 335-347.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 335-347
    • Li, J.M.1    Wu, H.2    Zhang, W.3    Blackburn, M.R.4    Jin, J.5
  • 52
    • 84894085209 scopus 로고    scopus 로고
    • Protecting the proteome: Eukaryotic cotranslational quality control pathways
    • Lykke-Andersen, J. and Bennett, E. J. (2014). Protecting the proteome: Eukaryotic cotranslational quality control pathways. J. Cell Biol. 204, 467-476.
    • (2014) J. Cell Biol. , vol.204 , pp. 467-476
    • Lykke-Andersen, J.1    Bennett, E.J.2
  • 55
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger, M. B., Hristova, V. A. and Weissman, A. M. (2012). HECT and RING finger families of E3 ubiquitin ligases at a glance. J. Cell Sci. 125, 531-537.
    • (2012) J. Cell Sci. , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 56
    • 20444400839 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, 108-119.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 108-119
    • Meyer, H.H.1
  • 57
    • 84861970930 scopus 로고    scopus 로고
    • p97 complexes as signal integration hubs
    • Meyer, H. (2012). p97 complexes as signal integration hubs. BMC Biol. 10, 48.
    • (2012) BMC Biol. , vol.10 , pp. 48
    • Meyer, H.1
  • 58
    • 84900337781 scopus 로고    scopus 로고
    • Enhanced protein degradation by branched ubiquitin chains
    • Meyer, H. J. and Rape, M. (2014). Enhanced protein degradation by branched ubiquitin chains. Cell 157, 910-921.
    • (2014) Cell , vol.157 , pp. 910-921
    • Meyer, H.J.1    Rape, M.2
  • 59
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer, H., Bug, M. and Bremer, S. (2012). Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14, 117-123.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 63
    • 84896393480 scopus 로고    scopus 로고
    • Ubiquitin signals proteolysisindependent stripping of transcription factors
    • Ndoja, A., Cohen, R. E. and Yao, T. (2014). Ubiquitin signals proteolysisindependent stripping of transcription factors. Mol. Cell 53, 893-903.
    • (2014) Mol. Cell , vol.53 , pp. 893-903
    • Ndoja, A.1    Cohen, R.E.2    Yao, T.3
  • 65
    • 84863272299 scopus 로고    scopus 로고
    • The role of the N-domain in the ATPase activity of the mammalian AAA ATPase p97/VCP
    • Niwa, H., Ewens, C. A., Tsang, C., Yeung, H. O., Zhang, X. and Freemont, P. S. (2012). The role of the N-domain in the ATPase activity of the mammalian AAA ATPase p97/VCP. J. Biol. Chem. 287, 8561-8570.
    • (2012) J. Biol. Chem. , vol.287 , pp. 8561-8570
    • Niwa, H.1    Ewens, C.A.2    Tsang, C.3    Yeung, H.O.4    Zhang, X.5    Freemont, P.S.6
  • 66
    • 84872840929 scopus 로고    scopus 로고
    • Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover
    • Olzmann, J. A., Richter, C. M. and Kopito, R. R. (2013). Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc. Natl. Acad. Sci. USA 110, 1345-1350.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1345-1350
    • Olzmann, J.A.1    Richter, C.M.2    Kopito, R.R.3
  • 70
    • 84898769387 scopus 로고    scopus 로고
    • p97- dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition
    • Radhakrishnan, S. K., den Besten, W. and Deshaies, R. J. (2014). p97- dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition. eLife 3, e01856.
    • (2014) eLife , vol.3 , pp. e01856
    • Radhakrishnan, S.K.1    den Besten, W.2    Deshaies, R.J.3
  • 71
    • 37549068963 scopus 로고    scopus 로고
    • Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin
    • Ramadan, K., Bruderer, R., Spiga, F. M., Popp, O., Baur, T., Gotta, M. and Meyer, H. H. (2007). Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin. Nature 450, 1258-1262.
    • (2007) Nature , vol.450 , pp. 1258-1262
    • Ramadan, K.1    Bruderer, R.2    Spiga, F.M.3    Popp, O.4    Baur, T.5    Gotta, M.6    Meyer, H.H.7
  • 72
    • 80053583606 scopus 로고    scopus 로고
    • A genomewide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction
    • Raman, M., Havens, C. G., Walter, J. C. and Harper, J. W. (2011). A genomewide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction. Mol. Cell 44, 72-84.
    • (2011) Mol. Cell , vol.44 , pp. 72-84
    • Raman, M.1    Havens, C.G.2    Walter, J.C.3    Harper, J.W.4
  • 73
    • 84897980111 scopus 로고    scopus 로고
    • The p97-Ufd1-Npl4 ATPase complex ensures robustness of the G2/M checkpoint by facilitating CDC25A degradation
    • Riemer, A., Dobrynin, G., Dressler, A., Bremer, S., Soni, A., Iliakis, G. and Meyer, H. (2014). The p97-Ufd1-Npl4 ATPase complex ensures robustness of the G2/M checkpoint by facilitating CDC25A degradation. Cell Cycle 13, 919- 927.
    • (2014) Cell Cycle , vol.13 , pp. 919-927
    • Riemer, A.1    Dobrynin, G.2    Dressler, A.3    Bremer, S.4    Soni, A.5    Iliakis, G.6    Meyer, H.7
  • 74
    • 80052451417 scopus 로고    scopus 로고
    • Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations
    • Ritz, D., Vuk, M., Kirchner, P., Bug, M., Schu¨ tz, S., Hayer, A., Bremer, S., Lusk, C., Baloh, R. H., Lee, H. et al. (2011). Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations. Nat. Cell Biol. 13, 1116-1123.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1116-1123
    • Ritz, D.1    Vuk, M.2    Kirchner, P.3    Bug, M.4    Schu¨tz, S.5    Hayer, A.6    Bremer, S.7    Lusk, C.8    Baloh, R.H.9    Lee, H.10
  • 77
    • 49249130739 scopus 로고    scopus 로고
    • UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
    • Schuberth, C. and Buchberger, A. (2008). UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell. Mol. Life Sci. 65, 2360-2371.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2360-2371
    • Schuberth, C.1    Buchberger, A.2
  • 80
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P. and Harper, J. W. (2009). Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 84
  • 85
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T. P., Dantuma, N. P. and Taylor, J. P. (2010). VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6, 217-227.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8
  • 87
    • 84886387458 scopus 로고    scopus 로고
    • Role of p97/VCP (Cdc48) in genome stability
    • Vaz, B., Halder, S. and Ramadan, K. (2013). Role of p97/VCP (Cdc48) in genome stability. Front. Genet. 4, 60.
    • (2013) Front. Genet. , vol.4 , pp. 60
    • Vaz, B.1    Halder, S.2    Ramadan, K.3
  • 88
    • 78650733298 scopus 로고    scopus 로고
    • Cdc48/p97 mediates UV-dependent turnover of RNA Pol II
    • Verma, R., Oania, R., Fang, R., Smith, G. T. and Deshaies, R. J. (2011). Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol. Cell 41, 82-92.
    • (2011) Mol. Cell , vol.41 , pp. 82-92
    • Verma, R.1    Oania, R.2    Fang, R.3    Smith, G.T.4    Deshaies, R.J.5
  • 89
    • 84879034688 scopus 로고    scopus 로고
    • Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome
    • Verma, R., Oania, R. S., Kolawa, N. J. and Deshaies, R. J. (2013). Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome. eLife 2, e00308.
    • (2013) eLife , vol.2 , pp. e00308
    • Verma, R.1    Oania, R.S.2    Kolawa, N.J.3    Deshaies, R.J.4
  • 92
    • 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
  • 93
    • 31144470450 scopus 로고    scopus 로고
    • Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulumassociated degradation
    • Weihl, C. C., Dalal, S., Pestronk, A. and Hanson, P. I. (2006). Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulumassociated degradation. Hum. Mol. Genet. 15, 189-199.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 189-199
    • Weihl, C.C.1    Dalal, S.2    Pestronk, A.3    Hanson, P.I.4
  • 94
    • 34447093377 scopus 로고    scopus 로고
    • Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice
    • Weihl, C. C., Miller, S. E., Hanson, P. I. and Pestronk, A. (2007). Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice. Hum. Mol. Genet. 16, 919-928.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 919-928
    • Weihl, C.C.1    Miller, S.E.2    Hanson, P.I.3    Pestronk, A.4
  • 96
    • 67349090057 scopus 로고    scopus 로고
    • Valosin-containing protein disease: inclusion body myopathy with Paget's disease of the bone and frontotemporal dementia
    • Weihl, C. C., Pestronk, A. and Kimonis, V. E. (2009). Valosin-containing protein disease: inclusion body myopathy with Paget's disease of the bone and frontotemporal dementia. Neuromuscul. Disord. 19, 308-315.
    • (2009) Neuromuscul. Disord. , vol.19 , pp. 308-315
    • Weihl, C.C.1    Pestronk, A.2    Kimonis, V.E.3
  • 97
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman, A. M. (2001). Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2, 169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 98
    • 84855206731 scopus 로고    scopus 로고
    • Recent advances in p97/VCP/Cdc48 cellular functions
    • Yamanaka, K., Sasagawa, Y. and Ogura, T. (2012). Recent advances in p97/VCP/Cdc48 cellular functions. Biochim. Biophys. Acta 1823, 130-137.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 130-137
    • Yamanaka, K.1    Sasagawa, Y.2    Ogura, T.3
  • 99
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase
    • Ye, Y. (2006). Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J. Struct. Biol. 156, 29-40.
    • (2006) J. Struct. Biol. , vol.156 , pp. 29-40
    • Ye, Y.1
  • 101
    • 80855154135 scopus 로고    scopus 로고
    • A Protein Epitope Signature Tag (PrEST) library allows SILAC-based absolute quantification and multiplexed determination of protein copy numbers in cell lines
    • 009613
    • c Lundberg, E., Uhlen, M. and Mann, M. (2012). A Protein Epitope Signature Tag (PrEST) library allows SILAC-based absolute quantification and multiplexed determination of protein copy numbers in cell lines. Mol. Cell Proteomics 11, O111 009613.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. O111
    • Zeiler, M.1    Straube, W.L.2    Lundberg, E.3    Uhlen, M.4    Mann, M.5
  • 102
    • 84877263936 scopus 로고    scopus 로고
    • The p97-UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated HuR from mRNP
    • Zhou, H. L., Geng, C., Luo, G. and Lou, H. (2013). The p97-UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated HuR from mRNP. Genes Dev. 27, 1046-1058.
    • (2013) Genes Dev. , vol.27 , pp. 1046-1058
    • Zhou, H.L.1    Geng, C.2    Luo, G.3    Lou, H.4


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