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Volumn 1843, Issue 1, 2014, Pages 205-215

Create and preserve: Proteostasis in development and aging is governed by Cdc48/p97/VCP

Author keywords

Age related disease; Autophagy; Cdc48 CDC 48 p97 VCP; Protein aggregation; Proteostasis; Ubiquitin proteasome system

Indexed keywords

CELL CYCLE PROTEIN; CELL DIVISION CYCLE PROTEIN 48; UNCLASSIFIED DRUG;

EID: 84890229110     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.03.031     Document Type: Review
Times cited : (45)

References (178)
  • 1
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: process and function
    • Mizushima N. Autophagy: process and function. Genes Dev. 2007, 21:2861-2873.
    • (2007) Genes Dev. , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 2
    • 78049383942 scopus 로고    scopus 로고
    • Protein homeostasis in models of aging and age-related conformational disease
    • Kikis E.A., Gidalevitz T., Morimoto R.I. Protein homeostasis in models of aging and age-related conformational disease. Adv. Exp. Med. Biol. 2010, 694:138-159.
    • (2010) Adv. Exp. Med. Biol. , vol.694 , pp. 138-159
    • Kikis, E.A.1    Gidalevitz, T.2    Morimoto, R.I.3
  • 3
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner M., Nuber U., Huibregtse J.M. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 1995, 373:81-83.
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 4
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H.D., Mayer T.U., Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999, 96:635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 5
    • 16244373679 scopus 로고    scopus 로고
    • Multiubiquitylation by E4 enzymes: 'one size' doesn't fit all
    • Hoppe T. Multiubiquitylation by E4 enzymes: 'one size' doesn't fit all. Trends Biochem. Sci. 2005, 30:183-187.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 183-187
    • Hoppe, T.1
  • 10
    • 33846471122 scopus 로고    scopus 로고
    • Proteasome-independent functions of ubiquitin in endocytosis and signaling
    • Mukhopadhyay D., Riezman H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 2007, 315:201-205.
    • (2007) Science , vol.315 , pp. 201-205
    • Mukhopadhyay, D.1    Riezman, H.2
  • 11
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark A.P., Hofmann R.M., Tsui C., Pickart C.M., Wolberger C. Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell 2001, 105:711-720.
    • (2001) Cell , vol.105 , pp. 711-720
    • VanDemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 12
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H., Rape M., Braun S., Rumpf S., Hoege C., Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 2005, 120:73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 18
    • 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., Meyer H.H. Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin. Nature 2007, 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
  • 19
    • 84856620090 scopus 로고    scopus 로고
    • The p97 ATPase associates with EEA1 to regulate the size of early endosomes
    • Ramanathan H.N., Ye Y. The p97 ATPase associates with EEA1 to regulate the size of early endosomes. Cell Res. 2011, 22:346-359.
    • (2011) Cell Res. , vol.22 , pp. 346-359
    • Ramanathan, H.N.1    Ye, Y.2
  • 20
    • 73349115264 scopus 로고    scopus 로고
    • A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex
    • Wilcox A.J., Laney J.D. A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex. Nat. Cell Biol. 2009, 11:1481-1486.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1481-1486
    • Wilcox, A.J.1    Laney, J.D.2
  • 21
    • 84865094127 scopus 로고    scopus 로고
    • Identification of the Cdc48*20S proteasome as an ancient AAA+ proteolytic machine
    • Barthelme D., Sauer R.T. Identification of the Cdc48*20S proteasome as an ancient AAA+ proteolytic machine. Science 2012, 337:843-846.
    • (2012) Science , vol.337 , pp. 843-846
    • Barthelme, D.1    Sauer, R.T.2
  • 22
    • 84874452437 scopus 로고    scopus 로고
    • Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase
    • Barthelme D., Sauer R.T. Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:3327-3332.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 3327-3332
    • Barthelme, D.1    Sauer, R.T.2
  • 23
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters J.M., Walsh M.J., Franke W.W. An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J. 1990, 9:1757-1767.
    • (1990) EMBO J. , vol.9 , pp. 1757-1767
    • Peters, J.M.1    Walsh, M.J.2    Franke, W.W.3
  • 24
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • Ghislain M., Dohmen R.J., Levy F., Varshavsky A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 1996, 15:4884-4899.
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 25
    • 84864385646 scopus 로고    scopus 로고
    • Expanding into new markets-VCP/p97 in endocytosis and autophagy
    • Bug M., Meyer H. Expanding into new markets-VCP/p97 in endocytosis and autophagy. J. Struct. Biol. 2012, 179:78-82.
    • (2012) J. Struct. Biol. , vol.179 , pp. 78-82
    • Bug, M.1    Meyer, H.2
  • 26
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer H., Bug M., Bremer S. Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 2012, 14:117-123.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 27
    • 84855206731 scopus 로고    scopus 로고
    • Recent advances in p97/VCP/Cdc48 cellular functions
    • Yamanaka K., Sasagawa Y., Ogura T. Recent advances in p97/VCP/Cdc48 cellular functions. Biochim. Biophys. Acta 2011, 1823:130-137.
    • (2011) Biochim. Biophys. Acta , vol.1823 , pp. 130-137
    • Yamanaka, K.1    Sasagawa, Y.2    Ogura, T.3
  • 28
    • 58549085208 scopus 로고    scopus 로고
    • The ubiquitin-selective chaperone CDC-48/p97, a new player in DNA replication
    • Deichsel A., Mouysset J., Hoppe T. The ubiquitin-selective chaperone CDC-48/p97, a new player in DNA replication. Cell Cycle 2009, 8:185-190.
    • (2009) Cell Cycle , vol.8 , pp. 185-190
    • Deichsel, A.1    Mouysset, J.2    Hoppe, T.3
  • 30
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase
    • Ye Y. Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J. Struct. Biol. 2006, 156:29-40.
    • (2006) J. Struct. Biol. , vol.156 , pp. 29-40
    • Ye, Y.1
  • 31
    • 49249130739 scopus 로고    scopus 로고
    • UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
    • Schuberth C., Buchberger A. UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell. Mol. Life Sci. 2008, 65:2360-2371.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2360-2371
    • Schuberth, C.1    Buchberger, A.2
  • 32
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    • Rumpf S., Jentsch S. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol. Cell 2006, 21:261-269.
    • (2006) Mol. Cell , vol.21 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2
  • 34
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4
    • Meyer H.H., Wang Y., Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 2002, 21:5645-5652.
    • (2002) EMBO J. , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 36
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa M.E., Bennett E.J., Gygi S.P., Harper J.W. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009, 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
  • 37
    • 80053345641 scopus 로고    scopus 로고
    • Proteasomal degradation of ubiquitinated proteins in oocyte meiosis and fertilization in mammals
    • Karabinova P., Kubelka M., Susor A. Proteasomal degradation of ubiquitinated proteins in oocyte meiosis and fertilization in mammals. Cell Tissue Res. 2011, 346:1-9.
    • (2011) Cell Tissue Res. , vol.346 , pp. 1-9
    • Karabinova, P.1    Kubelka, M.2    Susor, A.3
  • 39
    • 84864395981 scopus 로고    scopus 로고
    • CDC-48/p97 is required for proper meiotic chromosome segregation via controlling AIR-2/Aurora B kinase localization in Caenorhabditis elegans
    • Sasagawa Y., Higashitani A., Urano T., Ogura T., Yamanaka K. CDC-48/p97 is required for proper meiotic chromosome segregation via controlling AIR-2/Aurora B kinase localization in Caenorhabditis elegans. J. Struct. Biol. 2012, 179:104-111.
    • (2012) J. Struct. Biol. , vol.179 , pp. 104-111
    • Sasagawa, Y.1    Higashitani, A.2    Urano, T.3    Ogura, T.4    Yamanaka, K.5
  • 41
    • 84873909937 scopus 로고    scopus 로고
    • The budding yeast cdc48(shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (glc7)
    • Bohm S., Buchberger A. The budding yeast cdc48(shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (glc7). PLoS One 2013, 8:e56486.
    • (2013) PLoS One , vol.8
    • Bohm, S.1    Buchberger, A.2
  • 42
    • 53249109785 scopus 로고    scopus 로고
    • An Afg2/Spaf-related Cdc48-like AAA ATPase regulates the stability and activity of the C. elegans Aurora B kinase AIR-2
    • Heallen T.R., Adams H.P., Furuta T., Verbrugghe K.J., Schumacher J.M. An Afg2/Spaf-related Cdc48-like AAA ATPase regulates the stability and activity of the C. elegans Aurora B kinase AIR-2. Dev. Cell 2008, 15:603-616.
    • (2008) Dev. Cell , vol.15 , pp. 603-616
    • Heallen, T.R.1    Adams, H.P.2    Furuta, T.3    Verbrugghe, K.J.4    Schumacher, J.M.5
  • 46
    • 0027364578 scopus 로고
    • AFG2, an essential gene in yeast, encodes a new member of the Sec18p, Pas1p, Cdc48p, TBP-1 family of putative ATPases
    • Thorsness P.E., White K.H., Ong W.C. AFG2, an essential gene in yeast, encodes a new member of the Sec18p, Pas1p, Cdc48p, TBP-1 family of putative ATPases. Yeast 1993, 9:1267-1271.
    • (1993) Yeast , vol.9 , pp. 1267-1271
    • Thorsness, P.E.1    White, K.H.2    Ong, W.C.3
  • 47
    • 0020120095 scopus 로고
    • Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies
    • Moir D., Stewart S.E., Osmond B.C., Botstein D. Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies. Genetics 1982, 100:547-563.
    • (1982) Genetics , vol.100 , pp. 547-563
    • Moir, D.1    Stewart, S.E.2    Osmond, B.C.3    Botstein, D.4
  • 48
    • 77953586259 scopus 로고    scopus 로고
    • The AAA-ATPase Cdc48 and cofactor Shp1 promote chromosome bi-orientation by balancing Aurora B activity
    • Cheng Y.L., Chen R.H. The AAA-ATPase Cdc48 and cofactor Shp1 promote chromosome bi-orientation by balancing Aurora B activity. J. Cell Sci. 2010, 123:2025-2034.
    • (2010) J. Cell Sci. , vol.123 , pp. 2025-2034
    • Cheng, Y.L.1    Chen, R.H.2
  • 49
    • 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., Zheng Y. The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell 2003, 115:355-367.
    • (2003) Cell , vol.115 , pp. 355-367
    • Cao, K.1    Nakajima, R.2    Meyer, H.H.3    Zheng, Y.4
  • 50
    • 34249112641 scopus 로고    scopus 로고
    • The AAA-ATPase p97-Ufd1-Npl4 is required for ERAD but not for spindle disassembly in Xenopus egg extracts
    • Heubes S., Stemmann O. The AAA-ATPase p97-Ufd1-Npl4 is required for ERAD but not for spindle disassembly in Xenopus egg extracts. J. Cell Sci. 2007, 120:1325-1329.
    • (2007) J. Cell Sci. , vol.120 , pp. 1325-1329
    • Heubes, S.1    Stemmann, O.2
  • 51
    • 33749246525 scopus 로고    scopus 로고
    • Cdc48 is required for the stability of Cut1/separase in mitotic anaphase
    • Ikai N., Yanagida M. Cdc48 is required for the stability of Cut1/separase in mitotic anaphase. J. Struct. Biol. 2006, 156:50-61.
    • (2006) J. Struct. Biol. , vol.156 , pp. 50-61
    • Ikai, N.1    Yanagida, M.2
  • 52
    • 80053606383 scopus 로고    scopus 로고
    • CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication
    • Franz A., Orth M., Pirson P.A., Sonneville R., Blow J.J., Gartner A., Stemmann O., Hoppe T. CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication. Mol. Cell 2011, 44:85-96.
    • (2011) Mol. Cell , vol.44 , pp. 85-96
    • Franz, A.1    Orth, M.2    Pirson, P.A.3    Sonneville, R.4    Blow, J.J.5    Gartner, A.6    Stemmann, O.7    Hoppe, T.8
  • 53
    • 80053583606 scopus 로고    scopus 로고
    • A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction
    • Raman M., Havens C.G., Walter J.C., Harper J.W. A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction. Mol. Cell 2011, 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
  • 54
    • 52549115459 scopus 로고    scopus 로고
    • Replication licensing and cancer-a fatal entanglement?
    • Blow J.J., Gillespie P.J. Replication licensing and cancer-a fatal entanglement?. Nat. Rev. Cancer 2008, 8:799-806.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 799-806
    • Blow, J.J.1    Gillespie, P.J.2
  • 55
    • 33748305620 scopus 로고    scopus 로고
    • Deregulation of Cdt1 induces chromosomal damage without rereplication and leads to chromosomal instability
    • Tatsumi Y., Sugimoto N., Yugawa T., Narisawa-Saito M., Kiyono T., Fujita M. Deregulation of Cdt1 induces chromosomal damage without rereplication and leads to chromosomal instability. J. Cell Sci. 2006, 119:3128-3140.
    • (2006) J. Cell Sci. , vol.119 , pp. 3128-3140
    • Tatsumi, Y.1    Sugimoto, N.2    Yugawa, T.3    Narisawa-Saito, M.4    Kiyono, T.5    Fujita, M.6
  • 59
    • 84865475874 scopus 로고    scopus 로고
    • Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions
    • Nie M., Aslanian A., Prudden J., Heideker J., Vashisht A.A., Wohlschlegel J.A., Yates J.R., Boddy M.N. Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions. J. Biol. Chem. 2012, 287:29610-29619.
    • (2012) J. Biol. Chem. , vol.287 , pp. 29610-29619
    • Nie, M.1    Aslanian, A.2    Prudden, J.3    Heideker, J.4    Vashisht, A.A.5    Wohlschlegel, J.A.6    Yates, J.R.7    Boddy, M.N.8
  • 62
    • 84858735947 scopus 로고    scopus 로고
    • P97/VCP- and Lys48-linked polyubiquitination form a new signaling pathway in DNA damage response
    • Ramadan K. p97/VCP- and Lys48-linked polyubiquitination form a new signaling pathway in DNA damage response. Cell Cycle 2012, 11:1062-1069.
    • (2012) Cell Cycle , vol.11 , pp. 1062-1069
    • Ramadan, K.1
  • 63
    • 84865602944 scopus 로고    scopus 로고
    • Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin
    • Dantuma N.P., Hoppe T. Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin. Trends Cell Biol. 2012, 22:483-491.
    • (2012) Trends Cell Biol. , vol.22 , pp. 483-491
    • Dantuma, N.P.1    Hoppe, T.2
  • 64
    • 70350349890 scopus 로고    scopus 로고
    • Caenorhabditis elegans p97 controls germline-specific sex determination by controlling the TRA-1 level in a CUL-2-dependent manner
    • Sasagawa Y., Otani M., Higashitani N., Higashitani A., Sato K., Ogura T., Yamanaka K. Caenorhabditis elegans p97 controls germline-specific sex determination by controlling the TRA-1 level in a CUL-2-dependent manner. J. Cell Sci. 2009, 122:3663-3672.
    • (2009) J. Cell Sci. , vol.122 , pp. 3663-3672
    • Sasagawa, Y.1    Otani, M.2    Higashitani, N.3    Higashitani, A.4    Sato, K.5    Ogura, T.6    Yamanaka, K.7
  • 65
    • 78649715872 scopus 로고    scopus 로고
    • Caenorhabditis elegans UBX cofactors for CDC-48/p97 control spermatogenesis
    • Sasagawa Y., Yamanaka K., Saito-Sasagawa Y., Ogura T. Caenorhabditis elegans UBX cofactors for CDC-48/p97 control spermatogenesis. Genes Cells 2010, 15:1201-1215.
    • (2010) Genes Cells , vol.15 , pp. 1201-1215
    • Sasagawa, Y.1    Yamanaka, K.2    Saito-Sasagawa, Y.3    Ogura, T.4
  • 66
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe T., Matuschewski K., Rape M., Schlenker S., Ulrich H.D., Jentsch S. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 2000, 102:577-586.
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 67
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • Rape M., Hoppe T., Gorr I., Kalocay M., Richly H., Jentsch S. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 2001, 107:667-677.
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 68
    • 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., Deshaies R.J. UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 2008, 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
  • 69
    • 84860120476 scopus 로고    scopus 로고
    • UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation
    • Bandau S., Knebel A., Gage Z.O., Wood N.T., Alexandru G. UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation. BMC Biol. 2012, 10:36.
    • (2012) BMC Biol. , vol.10 , pp. 36
    • Bandau, S.1    Knebel, A.2    Gage, Z.O.3    Wood, N.T.4    Alexandru, G.5
  • 70
    • 44649176937 scopus 로고    scopus 로고
    • Protein quality control gets muscle into shape
    • Kim J., Lowe T., Hoppe T. Protein quality control gets muscle into shape. Trends Cell Biol. 2008, 18:264-272.
    • (2008) Trends Cell Biol. , vol.18 , pp. 264-272
    • Kim, J.1    Lowe, T.2    Hoppe, T.3
  • 71
    • 0037169028 scopus 로고    scopus 로고
    • Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
    • Barral J.M., Hutagalung A.H., Brinker A., Hartl F.U., Epstein H.F. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 2002, 295:669-671.
    • (2002) Science , vol.295 , pp. 669-671
    • Barral, J.M.1    Hutagalung, A.H.2    Brinker, A.3    Hartl, F.U.4    Epstein, H.F.5
  • 72
    • 4043096960 scopus 로고    scopus 로고
    • Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans
    • Hoppe T., Cassata G., Barral J.M., Springer W., Hutagalung A.H., Epstein H.F., Baumeister R. Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans. Cell 2004, 118:337-349.
    • (2004) Cell , vol.118 , pp. 337-349
    • Hoppe, T.1    Cassata, G.2    Barral, J.M.3    Springer, W.4    Hutagalung, A.H.5    Epstein, H.F.6    Baumeister, R.7
  • 75
    • 84864874006 scopus 로고    scopus 로고
    • The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins
    • Piccirillo R., Goldberg A.L. The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins. EMBO J. 2012, 31:3334-3350.
    • (2012) EMBO J. , vol.31 , pp. 3334-3350
    • Piccirillo, R.1    Goldberg, A.L.2
  • 76
    • 79952255326 scopus 로고    scopus 로고
    • Pathogenic VCP/TER94 alleles are dominant actives and contribute to neurodegeneration by altering cellular ATP level in a Drosophila IBMPFD model
    • Chang Y.C., Hung W.T., Chang H.C., Wu C.L., Chiang A.S., Jackson G.R., Sang T.K. Pathogenic VCP/TER94 alleles are dominant actives and contribute to neurodegeneration by altering cellular ATP level in a Drosophila IBMPFD model. PLoS Genet. 2011, 7:e1001288.
    • (2011) PLoS Genet. , vol.7
    • Chang, Y.C.1    Hung, W.T.2    Chang, H.C.3    Wu, C.L.4    Chiang, A.S.5    Jackson, G.R.6    Sang, T.K.7
  • 77
    • 77952486387 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone
    • Custer S.K., Neumann M., Lu H., Wright A.C., Taylor J.P. Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone. Hum. Mol. Genet. 2010, 19:1741-1755.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1741-1755
    • Custer, S.K.1    Neumann, M.2    Lu, H.3    Wright, A.C.4    Taylor, J.P.5
  • 78
    • 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., Pestronk A. Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice. Hum. Mol. Genet. 2007, 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
  • 80
    • 79955128860 scopus 로고    scopus 로고
    • Neuronal remodeling and apoptosis require VCP-dependent degradation of the apoptosis inhibitor DIAP1
    • Rumpf S., Lee S.B., Jan L.Y., Jan Y.N. Neuronal remodeling and apoptosis require VCP-dependent degradation of the apoptosis inhibitor DIAP1. Development 2011, 138:1153-1160.
    • (2011) Development , vol.138 , pp. 1153-1160
    • Rumpf, S.1    Lee, S.B.2    Jan, L.Y.3    Jan, Y.N.4
  • 81
    • 84055217030 scopus 로고    scopus 로고
    • Valosin-containing protein and neurofibromin interact to regulate dendritic spine density
    • Wang H.F., Shih Y.T., Chen C.Y., Chao H.W., Lee M.J., Hsueh Y.P. Valosin-containing protein and neurofibromin interact to regulate dendritic spine density. J. Clin. Invest. 2011, 121:4820-4837.
    • (2011) J. Clin. Invest. , vol.121 , pp. 4820-4837
    • Wang, H.F.1    Shih, Y.T.2    Chen, C.Y.3    Chao, H.W.4    Lee, M.J.5    Hsueh, Y.P.6
  • 82
    • 84055191106 scopus 로고    scopus 로고
    • Another VCP interactor: NF is enough
    • Weihl C.C. Another VCP interactor: NF is enough. J. Clin. Invest. 2011, 121:4627-4630.
    • (2011) J. Clin. Invest. , vol.121 , pp. 4627-4630
    • Weihl, C.C.1
  • 83
    • 0344614600 scopus 로고    scopus 로고
    • Identification of TER94, an AAA ATPase protein, as a Bam-dependent component of the Drosophila fusome
    • Leon A., McKearin D. Identification of TER94, an AAA ATPase protein, as a Bam-dependent component of the Drosophila fusome. Mol. Biol. Cell 1999, 10:3825-3834.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3825-3834
    • Leon, A.1    McKearin, D.2
  • 84
    • 0034651727 scopus 로고    scopus 로고
    • Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber
    • Ruden D.M., Sollars V., Wang X., Mori D., Alterman M., Lu X. Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber. Dev. Biol. 2000, 218:314-325.
    • (2000) Dev. Biol. , vol.218 , pp. 314-325
    • Ruden, D.M.1    Sollars, V.2    Wang, X.3    Mori, D.4    Alterman, M.5    Lu, X.6
  • 85
    • 0024834128 scopus 로고
    • A gradient of nuclear localization of the dorsal protein determines dorsoventral pattern in the Drosophila embryo
    • Roth S., Stein D., Nusslein-Volhard C. A gradient of nuclear localization of the dorsal protein determines dorsoventral pattern in the Drosophila embryo. Cell 1989, 59:1189-1202.
    • (1989) Cell , vol.59 , pp. 1189-1202
    • Roth, S.1    Stein, D.2    Nusslein-Volhard, C.3
  • 86
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IkappaBalpha and 26S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha
    • Dai R.M., Chen E., Longo D.L., Gorbea C.M., Li C.C. Involvement of valosin-containing protein, an ATPase co-purified with IkappaBalpha and 26S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. J. Biol. Chem. 1998, 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
  • 87
    • 1642576087 scopus 로고    scopus 로고
    • Fas-associated factor-1 inhibits nuclear factor-kappaB (NF-kappaB) activity by interfering with nuclear translocation of the RelA (p65) subunit of NF-kappaB
    • Park M.Y., Jang H.D., Lee S.Y., Lee K.J., Kim E. Fas-associated factor-1 inhibits nuclear factor-kappaB (NF-kappaB) activity by interfering with nuclear translocation of the RelA (p65) subunit of NF-kappaB. J. Biol. Chem. 2004, 279:2544-2549.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2544-2549
    • Park, M.Y.1    Jang, H.D.2    Lee, S.Y.3    Lee, K.J.4    Kim, E.5
  • 88
    • 34948844687 scopus 로고    scopus 로고
    • FAF1 suppresses IkappaB kinase (IKK) activation by disrupting the IKK complex assembly
    • Park M.Y., Moon J.H., Lee K.S., Choi H.I., Chung J., Hong H.J., Kim E. FAF1 suppresses IkappaB kinase (IKK) activation by disrupting the IKK complex assembly. J. Biol. Chem. 2007, 282:27572-27577.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27572-27577
    • Park, M.Y.1    Moon, J.H.2    Lee, K.S.3    Choi, H.I.4    Chung, J.5    Hong, H.J.6    Kim, E.7
  • 89
    • 84876076016 scopus 로고    scopus 로고
    • Aging and the aggregating proteome
    • David D.C. Aging and the aggregating proteome. Front. Genet. 2012, 3:247.
    • (2012) Front. Genet. , vol.3 , pp. 247
    • David, D.C.1
  • 90
    • 33846119369 scopus 로고    scopus 로고
    • The genetics and epigenetics of altered proliferative homeostasis in ageing and cancer
    • Martin G.M. The genetics and epigenetics of altered proliferative homeostasis in ageing and cancer. Mech. Ageing Dev. 2007, 128:9-12.
    • (2007) Mech. Ageing Dev. , vol.128 , pp. 9-12
    • Martin, G.M.1
  • 91
    • 70349507340 scopus 로고    scopus 로고
    • The shock of aging: molecular chaperones and the heat shock response in longevity and aging-a mini-review
    • Calderwood S.K., Murshid A., Prince T. The shock of aging: molecular chaperones and the heat shock response in longevity and aging-a mini-review. Gerontology 2009, 55:550-558.
    • (2009) Gerontology , vol.55 , pp. 550-558
    • Calderwood, S.K.1    Murshid, A.2    Prince, T.3
  • 92
    • 77950200010 scopus 로고    scopus 로고
    • The genetics of ageing
    • Kenyon C.J. The genetics of ageing. Nature 2010, 464:504-512.
    • (2010) Nature , vol.464 , pp. 504-512
    • Kenyon, C.J.1
  • 93
    • 84864622015 scopus 로고    scopus 로고
    • Induction of cytoprotective pathways is central to the extension of lifespan conferred by multiple longevity pathways
    • Shore D.E., Carr C.E., Ruvkun G. Induction of cytoprotective pathways is central to the extension of lifespan conferred by multiple longevity pathways. PLoS Genet. 2012, 8:e1002792.
    • (2012) PLoS Genet. , vol.8
    • Shore, D.E.1    Carr, C.E.2    Ruvkun, G.3
  • 94
    • 84878199302 scopus 로고    scopus 로고
    • Worms under stress: C. elegans stress response and its relevance to complex human disease and aging
    • in press
    • Rodriguez M., Snoek L.B., De Bono M., Kammenga J.E. Worms under stress: C. elegans stress response and its relevance to complex human disease and aging. Trends Genet. 2013, in press. 10.1016/j.tig.2013.01.010.
    • (2013) Trends Genet.
    • Rodriguez, M.1    Snoek, L.B.2    De Bono, M.3    Kammenga, J.E.4
  • 97
    • 84866544628 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress response in aging and age-related diseases
    • Brown M.K., Naidoo N. The endoplasmic reticulum stress response in aging and age-related diseases. Front. Physiol. 2012, 3:263.
    • (2012) Front. Physiol. , vol.3 , pp. 263
    • Brown, M.K.1    Naidoo, N.2
  • 98
    • 84855188325 scopus 로고    scopus 로고
    • The Cdc48 machine in endoplasmic reticulum associated protein degradation
    • Wolf D.H., Stolz A. The Cdc48 machine in endoplasmic reticulum associated protein degradation. Biochim. Biophys. Acta 2012, 1823:117-124.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 117-124
    • Wolf, D.H.1    Stolz, A.2
  • 100
    • 27144539523 scopus 로고    scopus 로고
    • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
    • Schuberth C., Buchberger A. Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nat. Cell Biol. 2005, 7:999-1006.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 999-1006
    • Schuberth, C.1    Buchberger, A.2
  • 103
    • 34548440339 scopus 로고    scopus 로고
    • ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play important roles in ERAD and developmental growth in Caenorhabditis elegans
    • Sasagawa Y., Yamanaka K., Ogura T. ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play important roles in ERAD and developmental growth in Caenorhabditis elegans. Genes Cells 2007, 12:1063-1073.
    • (2007) Genes Cells , vol.12 , pp. 1063-1073
    • Sasagawa, Y.1    Yamanaka, K.2    Ogura, T.3
  • 104
    • 33749258342 scopus 로고    scopus 로고
    • A conserved role of Caenorhabditis elegans CDC-48 in ER-associated protein degradation
    • Mouysset J., Kahler C., Hoppe T. A conserved role of Caenorhabditis elegans CDC-48 in ER-associated protein degradation. J. Struct. Biol. 2006, 156:41-49.
    • (2006) J. Struct. Biol. , vol.156 , pp. 41-49
    • Mouysset, J.1    Kahler, C.2    Hoppe, T.3
  • 105
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald M.L., Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev. 2008, 22:3308-3319.
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 106
    • 80053352130 scopus 로고    scopus 로고
    • Mitochondrial quality control by the ubiquitin-proteasome system
    • Taylor E.B., Rutter J. Mitochondrial quality control by the ubiquitin-proteasome system. Biochem. Soc. Trans. 2011, 39:1509-1513.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1509-1513
    • Taylor, E.B.1    Rutter, J.2
  • 107
    • 84864382366 scopus 로고    scopus 로고
    • Cdc48p/p97-mediated regulation of mitochondrial morphology is Vms1p-independent
    • Esaki M., Ogura T. Cdc48p/p97-mediated regulation of mitochondrial morphology is Vms1p-independent. J. Struct. Biol. 2012, 179:112-120.
    • (2012) J. Struct. Biol. , vol.179 , pp. 112-120
    • Esaki, M.1    Ogura, T.2
  • 108
    • 79551663809 scopus 로고    scopus 로고
    • The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
    • Xu S., Peng G., Wang Y., Fang S., Karbowski M. The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover. Mol. Biol. Cell 2011, 22:291-300.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 291-300
    • Xu, S.1    Peng, G.2    Wang, Y.3    Fang, S.4    Karbowski, M.5
  • 109
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E., Tao R.N., Whitworth A.J. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:5018-5023.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 111
    • 79959415069 scopus 로고    scopus 로고
    • Biogenesis and cargo selectivity of autophagosomes
    • Weidberg H., Shvets E., Elazar Z. Biogenesis and cargo selectivity of autophagosomes. Annu. Rev. Biochem. 2011, 80:125-156.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 125-156
    • Weidberg, H.1    Shvets, E.2    Elazar, Z.3
  • 112
    • 76249090337 scopus 로고    scopus 로고
    • Macroautophagy and its role in nutrient homeostasis
    • Stipanuk M.H. Macroautophagy and its role in nutrient homeostasis. Nutr. Rev. 2009, 67:677-689.
    • (2009) Nutr. Rev. , vol.67 , pp. 677-689
    • Stipanuk, M.H.1
  • 113
    • 67650234499 scopus 로고    scopus 로고
    • NBR1 cooperates with p62 in selective autophagy of ubiquitinated targets
    • Kirkin V., Lamark T., Johansen T., Dikic I. NBR1 cooperates with p62 in selective autophagy of ubiquitinated targets. Autophagy 2009, 5:732-733.
    • (2009) Autophagy , vol.5 , pp. 732-733
    • Kirkin, V.1    Lamark, T.2    Johansen, T.3    Dikic, I.4
  • 115
    • 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., Taylor J.P. VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 2010, 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
  • 119
    • 0027493180 scopus 로고
    • Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein
    • Pleasure I.T., Black M.M., Keen J.H. Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein. Nature 1993, 365:459-462.
    • (1993) Nature , vol.365 , pp. 459-462
    • Pleasure, I.T.1    Black, M.M.2    Keen, J.H.3
  • 121
    • 0032555641 scopus 로고    scopus 로고
    • Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes
    • Berg T.O., Fengsrud M., Stromhaug P.E., Berg T., Seglen P.O. Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes. J. Biol. Chem. 1998, 273:21883-21892.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21883-21892
    • Berg, T.O.1    Fengsrud, M.2    Stromhaug, P.E.3    Berg, T.4    Seglen, P.O.5
  • 122
    • 65349155174 scopus 로고    scopus 로고
    • Early endosomes and endosomal coatomer are required for autophagy
    • Razi M., Chan E.Y., Tooze S.A. Early endosomes and endosomal coatomer are required for autophagy. J. Cell Biol. 2009, 185:305-321.
    • (2009) J. Cell Biol. , vol.185 , pp. 305-321
    • Razi, M.1    Chan, E.Y.2    Tooze, S.A.3
  • 123
    • 0025362656 scopus 로고
    • In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome
    • Tooze J., Hollinshead M., Ludwig T., Howell K., Hoflack B., Kern H. In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome. J. Cell Biol. 1990, 111:329-345.
    • (1990) J. Cell Biol. , vol.111 , pp. 329-345
    • Tooze, J.1    Hollinshead, M.2    Ludwig, T.3    Howell, K.4    Hoflack, B.5    Kern, H.6
  • 124
    • 84876099899 scopus 로고    scopus 로고
    • Dynamic regulation of autophagy and endocytosis for cell remodeling during early development
    • Sato M., Sato K. Dynamic regulation of autophagy and endocytosis for cell remodeling during early development. Traffic 2013, 14:479-486.
    • (2013) Traffic , vol.14 , pp. 479-486
    • Sato, M.1    Sato, K.2
  • 125
    • 84872554899 scopus 로고    scopus 로고
    • The role of autophagy in Drosophila metamorphosis
    • Tracy K., Baehrecke E.H. The role of autophagy in Drosophila metamorphosis. Curr. Top. Dev. Biol. 2013, 103:101-125.
    • (2013) Curr. Top. Dev. Biol. , vol.103 , pp. 101-125
    • Tracy, K.1    Baehrecke, E.H.2
  • 126
    • 1642340527 scopus 로고    scopus 로고
    • Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation
    • Yamanaka K., Okubo Y., Suzaki T., Ogura T. Analysis of the two p97/VCP/Cdc48p proteins of Caenorhabditis elegans and their suppression of polyglutamine-induced protein aggregation. J. Struct. Biol. 2004, 146:242-250.
    • (2004) J. Struct. Biol. , vol.146 , pp. 242-250
    • Yamanaka, K.1    Okubo, Y.2    Suzaki, T.3    Ogura, T.4
  • 127
    • 48649085488 scopus 로고    scopus 로고
    • P97 homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeat
    • Nishikori S., Yamanaka K., Sakurai T., Esaki M., Ogura T. p97 homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeat. Genes Cells 2008, 13:827-838.
    • (2008) Genes Cells , vol.13 , pp. 827-838
    • Nishikori, S.1    Yamanaka, K.2    Sakurai, T.3    Esaki, M.4    Ogura, T.5
  • 128
    • 34250735508 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein (VCP)/p97 in the formation and clearance of abnormal protein aggregates
    • Kobayashi T., Manno A., Kakizuka A. Involvement of valosin-containing protein (VCP)/p97 in the formation and clearance of abnormal protein aggregates. Genes Cells 2007, 12:889-901.
    • (2007) Genes Cells , vol.12 , pp. 889-901
    • Kobayashi, T.1    Manno, A.2    Kakizuka, A.3
  • 130
    • 57649198447 scopus 로고    scopus 로고
    • Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease
    • Ju J.S., Miller S.E., Hanson P.I., Weihl C.C. Impaired protein aggregate handling and clearance underlie the pathogenesis of p97/VCP-associated disease. J. Biol. Chem. 2008, 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
  • 133
    • 0037024380 scopus 로고    scopus 로고
    • Cdc48 can distinguish between native and non-native proteins in the absence of cofactors
    • Thoms S. Cdc48 can distinguish between native and non-native proteins in the absence of cofactors. FEBS Lett. 2002, 520:107-110.
    • (2002) FEBS Lett. , vol.520 , pp. 107-110
    • Thoms, S.1
  • 134
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang H., Liu C., Zhong Y., Luo S., Monteiro M.J., Fang S. Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS One 2010, 5:e8905.
    • (2010) PLoS One , vol.5
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 135
    • 0037986563 scopus 로고    scopus 로고
    • Vacuole-creating protein in neurodegenerative diseases in humans
    • Mizuno Y., Hori S., Kakizuka A., Okamoto K. Vacuole-creating protein in neurodegenerative diseases in humans. Neurosci. Lett. 2003, 343:77-80.
    • (2003) Neurosci. Lett. , vol.343 , pp. 77-80
    • Mizuno, Y.1    Hori, S.2    Kakizuka, A.3    Okamoto, K.4
  • 136
    • 79951625225 scopus 로고    scopus 로고
    • The complexities of p97 function in health and disease
    • Chapman E., Fry A.N., Kang M. The complexities of p97 function in health and disease. Mol. Biosyst. 2011, 7:700-710.
    • (2011) Mol. Biosyst. , vol.7 , pp. 700-710
    • Chapman, E.1    Fry, A.N.2    Kang, M.3
  • 137
    • 77951653609 scopus 로고    scopus 로고
    • Identification of Caspase-6-mediated processing of the valosin containing protein (p97) in Alzheimer's disease: a novel link to dysfunction in ubiquitin proteasome system-mediated protein degradation
    • Halawani D., Tessier S., Anzellotti D., Bennett D.A., Latterich M., LeBlanc A.C. Identification of Caspase-6-mediated processing of the valosin containing protein (p97) in Alzheimer's disease: a novel link to dysfunction in ubiquitin proteasome system-mediated protein degradation. J. Neurosci. 2010, 30:6132-6142.
    • (2010) J. Neurosci. , vol.30 , pp. 6132-6142
    • Halawani, D.1    Tessier, S.2    Anzellotti, D.3    Bennett, D.A.4    Latterich, M.5    LeBlanc, A.C.6
  • 139
    • 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., Kimonis V.E. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat. Genet. 2004, 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
  • 141
    • 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., Watts G. VCP disease associated with myopathy, Paget disease of bone and frontotemporal dementia: review of a unique disorder. Biochim. Biophys. Acta 2008, 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
  • 144
    • 77953180920 scopus 로고    scopus 로고
    • P97/VCP at the intersection of the autophagy and the ubiquitin proteasome system
    • Ju J.S., Weihl C.C. p97/VCP at the intersection of the autophagy and the ubiquitin proteasome system. Autophagy 2010, 6:283-285.
    • (2010) Autophagy , vol.6 , pp. 283-285
    • Ju, J.S.1    Weihl, C.C.2
  • 146
    • 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., Latterich M. 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. 2009, 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
  • 147
    • 77953894192 scopus 로고    scopus 로고
    • Inclusion body myopathy, Paget's disease of the bone and fronto-temporal dementia: a disorder of autophagy
    • Ju J.S., Weihl C.C. Inclusion body myopathy, Paget's disease of the bone and fronto-temporal dementia: a disorder of autophagy. Hum. Mol. Genet. 2010, 19:R38-R45.
    • (2010) Hum. Mol. Genet. , vol.19
    • Ju, J.S.1    Weihl, C.C.2
  • 148
    • 77953121380 scopus 로고    scopus 로고
    • Imbalances in p97 co-factor interactions in human proteinopathy
    • Fernandez-Saiz V., Buchberger A. Imbalances in p97 co-factor interactions in human proteinopathy. EMBO Rep. 2010, 11:479-485.
    • (2010) EMBO Rep. , vol.11 , pp. 479-485
    • Fernandez-Saiz, V.1    Buchberger, A.2
  • 149
    • 77954957347 scopus 로고    scopus 로고
    • A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants
    • Tang W.K., Li D., Li C.C., Esser L., Dai R., Guo L., Xia D. A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. EMBO J. 2010, 29:2217-2229.
    • (2010) EMBO J. , vol.29 , pp. 2217-2229
    • Tang, W.K.1    Li, D.2    Li, C.C.3    Esser, L.4    Dai, R.5    Guo, L.6    Xia, D.7
  • 151
    • 77954724848 scopus 로고    scopus 로고
    • Enhanced ATPase activities as a primary defect of mutant valosin-containing proteins that cause inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia
    • Manno A., Noguchi M., Fukushi J., Motohashi Y., Kakizuka A. Enhanced ATPase activities as a primary defect of mutant valosin-containing proteins that cause inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia. Genes Cells 2010, 15:911-922.
    • (2010) Genes Cells , vol.15 , pp. 911-922
    • Manno, A.1    Noguchi, M.2    Fukushi, J.3    Motohashi, Y.4    Kakizuka, A.5
  • 152
    • 31144470450 scopus 로고    scopus 로고
    • Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation
    • Weihl C.C., Dalal S., Pestronk A., Hanson P.I. Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation. Hum. Mol. Genet. 2006, 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
  • 153
    • 84863332342 scopus 로고    scopus 로고
    • Protective role of cell division cycle 48 (CDC48) protein against neurodegeneration via ubiquitin-proteasome system dysfunction during zebrafish development
    • Imamura S., Yabu T., Yamashita M. Protective role of cell division cycle 48 (CDC48) protein against neurodegeneration via ubiquitin-proteasome system dysfunction during zebrafish development. J. Biol. Chem. 2012, 287:23047-23056.
    • (2012) J. Biol. Chem. , vol.287 , pp. 23047-23056
    • Imamura, S.1    Yabu, T.2    Yamashita, M.3
  • 156
    • 84877330289 scopus 로고    scopus 로고
    • Rapamycin-induced autophagy aggravates pathology and weakness in a mouse model of VCP-associated myopathy
    • Ching J.K., Weihl C.C. Rapamycin-induced autophagy aggravates pathology and weakness in a mouse model of VCP-associated myopathy. Autophagy 2013, 9.
    • (2013) Autophagy , vol.9
    • Ching, J.K.1    Weihl, C.C.2
  • 157
    • 84874529071 scopus 로고    scopus 로고
    • MTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy
    • Ching J.K., Elizabeth S.V., Ju J.S., Lusk C., Pittman S.K., Weihl C.C. mTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy. Hum. Mol. Genet. 2013, 22:1167-1179.
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 1167-1179
    • Ching, J.K.1    Elizabeth, S.V.2    Ju, J.S.3    Lusk, C.4    Pittman, S.K.5    Weihl, C.C.6
  • 158
    • 65449117176 scopus 로고    scopus 로고
    • Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
    • Gamerdinger M., Hajieva P., Kaya A.M., Wolfrum U., Hartl F.U., Behl C. Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. EMBO J. 2009, 28:889-901.
    • (2009) EMBO J. , vol.28 , pp. 889-901
    • Gamerdinger, M.1    Hajieva, P.2    Kaya, A.M.3    Wolfrum, U.4    Hartl, F.U.5    Behl, C.6
  • 162
    • 84873473364 scopus 로고    scopus 로고
    • Screening of VCP mutations in Chinese amyotrophic lateral sclerosis patients
    • (e1513-1514)
    • Zou Z.Y., Liu M.S., Li X.G., Cui L.Y. Screening of VCP mutations in Chinese amyotrophic lateral sclerosis patients. Neurobiol. Aging 2013, 34:1519. (e1513-1514).
    • (2013) Neurobiol. Aging , vol.34 , pp. 1519
    • Zou, Z.Y.1    Liu, M.S.2    Li, X.G.3    Cui, L.Y.4
  • 164
    • 84869742069 scopus 로고    scopus 로고
    • Autophagy and its comprehensive impact on ALS
    • Song C.Y., Guo J.F., Liu Y., Tang B.S. Autophagy and its comprehensive impact on ALS. Int. J. Neurosci. 2012, 122:695-703.
    • (2012) Int. J. Neurosci. , vol.122 , pp. 695-703
    • Song, C.Y.1    Guo, J.F.2    Liu, Y.3    Tang, B.S.4
  • 165
    • 84867278911 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a regulator of translesion synthesis
    • Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J. Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a regulator of translesion synthesis. J. Biol. Chem. 2012, 287:34225-34233.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34225-34233
    • Ghosal, G.1    Leung, J.W.2    Nair, B.C.3    Fong, K.W.4    Chen, J.5
  • 166
    • 79952834859 scopus 로고    scopus 로고
    • P97-containing complexes in proliferation control and cancer: emerging culprits or guilt by association?
    • Haines D.S. p97-containing complexes in proliferation control and cancer: emerging culprits or guilt by association?. Genes Cancer 2010, 1:753-763.
    • (2010) Genes Cancer , vol.1 , pp. 753-763
    • Haines, D.S.1
  • 167
    • 84860004853 scopus 로고    scopus 로고
    • VCP/p97, down-regulated by microRNA-129-5p, could regulate the progression of hepatocellular carcinoma
    • Liu Y., Hei Y., Shu Q., Dong J., Gao Y., Fu H., Zheng X., Yang G. VCP/p97, down-regulated by microRNA-129-5p, could regulate the progression of hepatocellular carcinoma. PLoS One 2012, 7:e35800.
    • (2012) PLoS One , vol.7
    • Liu, Y.1    Hei, Y.2    Shu, Q.3    Dong, J.4    Gao, Y.5    Fu, H.6    Zheng, X.7    Yang, G.8
  • 168
    • 0036240410 scopus 로고    scopus 로고
    • VCP (p97) regulates NFkappaB signaling pathway, which is important for metastasis of osteosarcoma cell line
    • Asai T., Tomita Y., Nakatsuka S., Hoshida Y., Myoui A., Yoshikawa H., Aozasa K. VCP (p97) regulates NFkappaB signaling pathway, which is important for metastasis of osteosarcoma cell line. Jpn. J. Cancer Res. 2002, 93:296-304.
    • (2002) Jpn. J. Cancer Res. , vol.93 , pp. 296-304
    • Asai, T.1    Tomita, Y.2    Nakatsuka, S.3    Hoshida, Y.4    Myoui, A.5    Yoshikawa, H.6    Aozasa, K.7
  • 169
    • 0037313833 scopus 로고    scopus 로고
    • Elevated expression of valosin-containing protein (p97) in hepatocellular carcinoma is correlated with increased incidence of tumor recurrence
    • Yamamoto S., Tomita Y., Nakamori S., Hoshida Y., Nagano H., Dono K., Umeshita K., Sakon M., Monden M., Aozasa K. Elevated expression of valosin-containing protein (p97) in hepatocellular carcinoma is correlated with increased incidence of tumor recurrence. J. Clin. Oncol. 2003, 21:447-452.
    • (2003) J. Clin. Oncol. , vol.21 , pp. 447-452
    • Yamamoto, S.1    Tomita, Y.2    Nakamori, S.3    Hoshida, Y.4    Nagano, H.5    Dono, K.6    Umeshita, K.7    Sakon, M.8    Monden, M.9    Aozasa, K.10
  • 170
    • 84055172732 scopus 로고    scopus 로고
    • Critical role of VCP/p97 in the pathogenesis and progression of non-small cell lung carcinoma
    • Valle C.W., Min T., Bodas M., Mazur S., Begum S., Tang D., Vij N. Critical role of VCP/p97 in the pathogenesis and progression of non-small cell lung carcinoma. PLoS One 2011, 6:e29073.
    • (2011) PLoS One , vol.6
    • Valle, C.W.1    Min, T.2    Bodas, M.3    Mazur, S.4    Begum, S.5    Tang, D.6    Vij, N.7
  • 171
    • 84869091005 scopus 로고    scopus 로고
    • Valosin containing protein (VCP/p97) is a novel substrate for the protein tyrosine phosphatase PTPL1
    • Abaan O.D., Hendriks W., Uren A., Toretsky J.A., Erkizan H.V. Valosin containing protein (VCP/p97) is a novel substrate for the protein tyrosine phosphatase PTPL1. Exp. Cell Res. 2012, 319:1-11.
    • (2012) Exp. Cell Res. , vol.319 , pp. 1-11
    • Abaan, O.D.1    Hendriks, W.2    Uren, A.3    Toretsky, J.A.4    Erkizan, H.V.5
  • 173
    • 77955457544 scopus 로고    scopus 로고
    • Retroviral Rem protein requires processing by signal peptidase and retrotranslocation for nuclear function
    • Byun H., Halani N., Mertz J.A., Ali A.F., Lozano M.M., Dudley J.P. Retroviral Rem protein requires processing by signal peptidase and retrotranslocation for nuclear function. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:12287-12292.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 12287-12292
    • Byun, H.1    Halani, N.2    Mertz, J.A.3    Ali, A.F.4    Lozano, M.M.5    Dudley, J.P.6
  • 175
    • 75349101096 scopus 로고    scopus 로고
    • Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97
    • Ewens C.A., Kloppsteck P., Forster A., Zhang X., Freemont P.S. Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97. Biochem. Cell Biol. 2010, 88:41-48.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 41-48
    • Ewens, C.A.1    Kloppsteck, P.2    Forster, A.3    Zhang, X.4    Freemont, P.S.5


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