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Volumn 314, Issue 14, 2008, Pages 2715-2723

Analysis of Npl4 deletion mutants in mammalian cells unravels new Ufd1-interacting motifs and suggests a regulatory role of Npl4 in ERAD

Author keywords

Endoplasmic reticulum associated degradation (ERAD); Npl4; p97; Ufd1; Valosin containing protein (VCP)

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GLUCOSE REGULATED PROTEIN 78; HETERODIMER; LIGASE; PROTEASOME; PROTEIN; PROTEIN NPL4; PROTEIN P97; PROTEIN UFD1; TRANSCRIPTION FACTOR ETV6; VALOSIN CONTAINING PROTEIN; X BOX BINDING PROTEIN 1;

EID: 48849099592     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.06.008     Document Type: Article
Times cited : (12)

References (49)
  • 2
    • 27144549993 scopus 로고    scopus 로고
    • Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors
    • Alzayady K.J., Panning M.M., Kelley G.G., and Wojcikiewicz R.J. Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors. J. Biol. Chem. 280 (2005) 34530-34537
    • (2005) J. Biol. Chem. , vol.280 , pp. 34530-34537
    • Alzayady, K.J.1    Panning, M.M.2    Kelley, G.G.3    Wojcikiewicz, R.J.4
  • 3
    • 0042233815 scopus 로고    scopus 로고
    • Analysis of intracellular distribution and apoptosis involvement of the Ufd1l gene product by over-expression studies
    • Amati F., Condo I., Conti E., Sangiuolo F., Dallapiccola B., Testi R., and Novelli G. Analysis of intracellular distribution and apoptosis involvement of the Ufd1l gene product by over-expression studies. Cell Biochem. Funct. 21 (2003) 263-267
    • (2003) Cell Biochem. Funct. , vol.21 , pp. 263-267
    • Amati, F.1    Condo, I.2    Conti, E.3    Sangiuolo, F.4    Dallapiccola, B.5    Testi, R.6    Novelli, G.7
  • 5
    • 0035812287 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding human NPL4, a protein interacting with the ubiquitin fusion-degradation protein (UFD1L)
    • Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B., and Novelli G. Cloning and characterization of the gene encoding human NPL4, a protein interacting with the ubiquitin fusion-degradation protein (UFD1L). Gene 275 (2001) 39-46
    • (2001) Gene , vol.275 , pp. 39-46
    • Botta, A.1    Tandoi, C.2    Fini, G.3    Calabrese, G.4    Dallapiccola, B.5    Novelli, G.6
  • 6
    • 33645154135 scopus 로고    scopus 로고
    • Cellular response to endoplasmic reticulum stress: a matter of life or death
    • Boyce M., and Yuan J. Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death. Differ. 133 (2006) 363-373
    • (2006) Cell Death. Differ. , vol.133 , pp. 363-373
    • Boyce, M.1    Yuan, J.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48(UFD1/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun S., Matuschewski K., Rape M., Thoms S., and Jentsch S. Role of the ubiquitin-selective CDC48(UFD1/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21 (2002) 615-621
    • (2002) EMBO J. , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 9
    • 9644255751 scopus 로고    scopus 로고
    • The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism 28
    • Bruderer R.M., Brasseur C., and Meyer H.H. The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism 28. J. Biol. Chem. 279 (2004) 49609-49616
    • (2004) J. Biol. Chem. , vol.279 , pp. 49609-49616
    • Bruderer, R.M.1    Brasseur, C.2    Meyer, H.H.3
  • 10
    • 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. The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of mitosis. Cell 115 (2003) 355-367
    • (2003) Cell , vol.115 , pp. 355-367
    • Cao, K.1    Nakajima, R.2    Meyer, H.H.3    Zheng, Y.4
  • 11
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 12
    • 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. Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene. Mol. Biol. Cell 7 (1996) 1835-1855
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1835-1855
    • DeHoratius, C.1    Silver, P.A.2
  • 13
    • 0037320333 scopus 로고    scopus 로고
    • IRE1: a role in UPREgulation of ER degradation
    • Hampton R.Y. IRE1: a role in UPREgulation of ER degradation. Dev. Cell 4 (2003) 144-146
    • (2003) Dev. Cell , vol.4 , pp. 144-146
    • Hampton, R.Y.1
  • 14
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • Harding H.P., Calfon M., Urano F., Novoa I., and Ron D. Transcriptional and translational control in the Mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18 (2002) 575-599
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 17
    • 0242300110 scopus 로고    scopus 로고
    • A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery
    • Hitchcock A.L., Auld K., Gygi S.P., and Silver P.A. A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc. Natl. Acad. Sci. U.S.A 100 (2003) 12735-12740
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 12735-12740
    • Hitchcock, A.L.1    Auld, K.2    Gygi, S.P.3    Silver, P.A.4
  • 18
    • 0034746779 scopus 로고    scopus 로고
    • The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation
    • Hitchcock A.L., Krebber H., Frietze S., Lin A., Latterich M., and Silver P.A. The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol. Biol. Cell 12 (2001) 3226-3241
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3226-3241
    • Hitchcock, A.L.1    Krebber, H.2    Frietze, S.3    Lin, A.4    Latterich, M.5    Silver, P.A.6
  • 20
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson E.S., Ma P.C., Ota I.M., and Varshavsky A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270 (1995) 17442-17456
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 22
    • 23044460010 scopus 로고    scopus 로고
    • Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate
    • Kothe M., Ye Y., Wagner J.S., De Luca H.E., Kern E., Rapoport T.A., and Lencer W.I. Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate. J. Biol. Chem. 280 (2005) 28127-28132
    • (2005) J. Biol. Chem. , vol.280 , pp. 28127-28132
    • Kothe, M.1    Ye, Y.2    Wagner, J.S.3    De Luca, H.E.4    Kern, E.5    Rapoport, T.A.6    Lencer, W.I.7
  • 23
    • 34248561455 scopus 로고    scopus 로고
    • A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum
    • Lass A., McConnell E., Nowis D., Mechref Y., Kang P., Novotny M.V., and Wojcik C. A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Arch. Biochem. Biophys. 462 (2007) 62-73
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 62-73
    • Lass, A.1    McConnell, E.2    Nowis, D.3    Mechref, Y.4    Kang, P.5    Novotny, M.V.6    Wojcik, C.7
  • 24
    • 0036556684 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum as a sensor for cellular stress
    • Ma Y., and Hendershot L.M. The mammalian endoplasmic reticulum as a sensor for cellular stress. Cell Stress. Chaperones. 7 (2002) 222-229
    • (2002) Cell Stress. Chaperones. , vol.7 , pp. 222-229
    • Ma, Y.1    Hendershot, L.M.2
  • 25
    • 33847673103 scopus 로고    scopus 로고
    • Ufd1-Npl4 is a negative regulator of cholera toxin retrotranslocation
    • McConnell E., Lass A., and Wojcik C. Ufd1-Npl4 is a negative regulator of cholera toxin retrotranslocation. Biochem. Biophys. Res Commun. 355 (2007) 1087-1090
    • (2007) Biochem. Biophys. Res Commun. , vol.355 , pp. 1087-1090
    • McConnell, E.1    Lass, A.2    Wojcik, C.3
  • 26
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer H.H., Shorter J.G., Seemann J., Pappin D., and Warren G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19 (2000) 2181-2192
    • (2000) EMBO J. , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 27
    • 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., and Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 21 (2002) 5645-5652
    • (2002) EMBO J. , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 28
    • 0034632033 scopus 로고    scopus 로고
    • The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
    • Ng D.T., Spear E.D., and Walter P. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J. Cell Biol. 150 (2000) 77-88
    • (2000) J. Cell Biol. , vol.150 , pp. 77-88
    • Ng, D.T.1    Spear, E.D.2    Walter, P.3
  • 29
    • 33747371085 scopus 로고    scopus 로고
    • Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates
    • Nowis D., McConnell E., and Wojcik C. Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates. Exp. Cell Res. 312 (2006) 2921-2932
    • (2006) Exp. Cell Res. , vol.312 , pp. 2921-2932
    • Nowis, D.1    McConnell, E.2    Wojcik, C.3
  • 31
    • 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., and Jentsch S. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107 (2001) 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
  • 32
    • 33846705026 scopus 로고    scopus 로고
    • Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors 10
    • Shcherbik N., and Haines D.S. Cdc48p(Npl4p/Ufd1p) binds and segregates membrane-anchored/tethered complexes via a polyubiquitin signal present on the anchors 10. Mol. Cell 25 (2007) 385-397
    • (2007) Mol. Cell , vol.25 , pp. 385-397
    • Shcherbik, N.1    Haines, D.S.2
  • 33
    • 4444232905 scopus 로고    scopus 로고
    • The unfolded protein response-a stress signaling pathway of the endoplasmic reticulum
    • Shen X., Zhang K., and Kaufman R.J. The unfolded protein response-a stress signaling pathway of the endoplasmic reticulum. J. Chem. Neuroanat. 28 (2004) 79-92
    • (2004) J. Chem. Neuroanat. , vol.28 , pp. 79-92
    • Shen, X.1    Zhang, K.2    Kaufman, R.J.3
  • 34
    • 37349114505 scopus 로고    scopus 로고
    • Characterization of the aggregation-prevention activity of p97/valosin-containing protein
    • Song C., Wang Q., and Li C.C. Characterization of the aggregation-prevention activity of p97/valosin-containing protein. Biochemistry 46 (2007) 14889-14898
    • (2007) Biochemistry , vol.46 , pp. 14889-14898
    • Song, C.1    Wang, Q.2    Li, C.C.3
  • 35
    • 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. 520 (2002) 107-110
    • (2002) FEBS Lett. , vol.520 , pp. 107-110
    • Thoms, S.1
  • 36
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., and Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101 (2000) 249-258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 37
    • 28544453333 scopus 로고    scopus 로고
    • Chromosome alignment and segregation regulated by ubiquitination of survivin
    • Vong Q.P., Cao K., Li H.Y., Iglesias P.A., and Zheng Y. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science 310 (2005) 1499-1504
    • (2005) Science , vol.310 , pp. 1499-1504
    • Vong, Q.P.1    Cao, K.2    Li, H.Y.3    Iglesias, P.A.4    Zheng, Y.5
  • 39
    • 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., and Hanson P.I. Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation. Hum. Mol. Genet. 15 (2006) 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
  • 40
    • 33750528166 scopus 로고    scopus 로고
    • Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells
    • Wojcik C., Rowicka M., Kudlicki A., Nowis D., McConnell E., Kujawa M., and DeMartino G.N. Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells. Mol. Biol. Cell 17 (2006) 4606-4618
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4606-4618
    • Wojcik, C.1    Rowicka, M.2    Kudlicki, A.3    Nowis, D.4    McConnell, E.5    Kujawa, M.6    DeMartino, G.N.7
  • 41
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the Unfolded Protein Response
    • Wu J., and Kaufman R.J. From acute ER stress to physiological roles of the Unfolded Protein Response. Cell Death. Differ. 13 (2006) 374-384
    • (2006) Cell Death. Differ. , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 42
    • 33846696670 scopus 로고    scopus 로고
    • Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin
    • Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C., Monteiro M.J., and Fang S. Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin. Exp. Cell Res. 313 (2007) 538-550
    • (2007) Exp. Cell Res. , vol.313 , pp. 538-550
    • Yang, H.1    Zhong, X.2    Ballar, P.3    Luo, S.4    Shen, Y.5    Rubinsztein, D.C.6    Monteiro, M.J.7    Fang, S.8
  • 43
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
    • Yang M., Omura S., Bonifacino J.S., and Weissman A.M. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J. Exp. Med. 187 (1998) 835-846
    • (1998) J. Exp. Med. , vol.187 , pp. 835-846
    • Yang, M.1    Omura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 44
    • 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. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414 (2001) 652-656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 45
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y., Meyer H.H., and Rapoport T.A. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162 (2003) 71-84
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 46
    • 26444621357 scopus 로고    scopus 로고
    • Inaugural article: recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane
    • Ye Y., Shibata Y., Kikkert M., van V.S., Wiertz E., and Rapoport T.A. Inaugural article: recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 14132-14138
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14132-14138
    • Ye, Y.1    Shibata, Y.2    Kikkert, M.3    van, V.S.4    Wiertz, E.5    Rapoport, T.A.6
  • 48
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., and Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107 (2001) 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 49
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu H., Kaung G., Kobayashi S., and Kopito R.R. Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J. Biol. Chem. 272 (1997) 20800-20804
    • (1997) J. Biol. Chem. , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4


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