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Volumn 288, Issue 32, 2013, Pages 23295-23306

Decoupling the role of ubiquitination for the dislocation versus degradation of major histocompatibility complex (MHC) class i proteins during endoplasmic reticulum-associated degradation (ERAD)

Author keywords

[No Author keywords available]

Indexed keywords

DATA SUPPORT; HEAVY CHAIN; LYSINE RESIDUES; MAJOR HISTOCOMPATIBILITY COMPLEX; MAJOR HISTOCOMPATIBILITY COMPLEX CLASS; UBIQUITINATION;

EID: 84881398313     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.482018     Document Type: Article
Times cited : (10)

References (66)
  • 1
  • 2
    • 84865298998 scopus 로고    scopus 로고
    • Finding the will and the way of ERAD substrate retrotranslocation
    • Hampton, R. Y., and Sommer, T. (2012) Finding the will and the way of ERAD substrate retrotranslocation. Curr. Opin. Cell Biol. 24, 460-466
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 460-466
    • Hampton, R.Y.1    Sommer, T.2
  • 5
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart, C. M. (2000) Ubiquitin in chains. Trends Biochem. Sci. 25, 544-548
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 6
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains. E2 enzymes at work
    • Ye, Y., and Rape, M. (2009) Building ubiquitin chains. E2 enzymes at work. Nat. Rev. Mol. Cell. Biol. 10, 755-764
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 7
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik, A. Y., and Hochstrasser, M. (2004) Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 1695, 189-207
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 10
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T., and Cohen, R. E. (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 11
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • Kostova, Z., Tsai, Y. C., and Weissman, A. M. (2007) Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. Semin. Cell Dev. Biol. 18, 770-779
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 13
    • 0035658442 scopus 로고    scopus 로고
    • HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins
    • Bays, N. W., Wilhovsky, S. K., Goradia, A., Hodgkiss-Harlow, K., and Hampton, R. Y. (2001) HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol. Biol. Cell 12, 4114-4128
    • (2001) Mol. Biol. Cell , vol.12 , pp. 4114-4128
    • Bays, N.W.1    Wilhovsky, S.K.2    Goradia, A.3    Hodgkiss-Harlow, K.4    Hampton, R.Y.5
  • 14
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/ p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H. H., and Rapoport, T. A. (2001) The AAA ATPase Cdc48/ p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 16
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Fröhlich, K. U., Diamant, N., and Bar-Nun, S. (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell Biol. 22, 626-634
    • (2002) Mol. Cell Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Fröhlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 18
    • 33749569154 scopus 로고    scopus 로고
    • Ubiquitination of MHC class i heavy chains is essential for dislocation by human cytomegalovirus-encoded US2 but not US11
    • Hassink, G. C., Barel, M. T., Van Voorden, S. B., Kikkert, M., and Wiertz, E. J. (2006) Ubiquitination of MHC class I heavy chains is essential for dislocation by human cytomegalovirus-encoded US2 but not US11. J. Biol. Chem. 281, 30063-30071
    • (2006) J. Biol. Chem. , vol.281 , pp. 30063-30071
    • Hassink, G.C.1    Barel, M.T.2    Van Voorden, S.B.3    Kikkert, M.4    Wiertz, E.J.5
  • 19
    • 84879318837 scopus 로고    scopus 로고
    • Studying ubiquitination of MHC class i molecules
    • Burr, M. L., Boname, J. M., and Lehner, P. J. (2013) Studying ubiquitination of MHC class I molecules. Methods Mol. Biol. 960, 109-125
    • (2013) Methods Mol. Biol. , vol.960 , pp. 109-125
    • Burr, M.L.1    Boname, J.M.2    Lehner, P.J.3
  • 20
    • 0038758918 scopus 로고    scopus 로고
    • Amino acid composition of 1/2 domains and cytoplasmic tail ofMHCclass i molecules determine their susceptibility to human cytomegalovirus US11-mediated down-regulation
    • Barel, M. T., Pizzato, N., van Leeuwen, D., Bouteiller, P. L., Wiertz, E. J., and Lenfant, F. (2003) Amino acid composition of 1/2 domains and cytoplasmic tail ofMHCclass I molecules determine their susceptibility to human cytomegalovirus US11-mediated down-regulation. Eur. J. Immunol. 33, 1707-1716
    • (2003) Eur. J. Immunol. , vol.33 , pp. 1707-1716
    • Barel, M.T.1    Pizzato, N.2    Van Leeuwen, D.3    Bouteiller, P.L.4    Wiertz, E.J.5    Lenfant, F.6
  • 21
    • 0041816452 scopus 로고    scopus 로고
    • Ubiquitinylation of the cytosolic domain of a type i membrane protein is not required to initiate its dislocation from the endoplasmic reticulum
    • Furman, M. H., Loureiro, J., Ploegh, H. L., and Tortorella, D. (2003) Ubiquitinylation of the cytosolic domain of a type I membrane protein is not required to initiate its dislocation from the endoplasmic reticulum. J. Biol. Chem. 278, 34804-34811
    • (2003) J. Biol. Chem. , vol.278 , pp. 34804-34811
    • Furman, M.H.1    Loureiro, J.2    Ploegh, H.L.3    Tortorella, D.4
  • 22
    • 0033523771 scopus 로고    scopus 로고
    • The pathway of US11-dependent degradation of MHC class i heavy chains involves a ubiquitin-conjugated intermediate
    • Shamu, C. E., Story, C. M., Rapoport, T. A., and Ploegh, H. L. (1999) The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate. J. Cell Biol. 147, 45-58
    • (1999) J. Cell Biol. , vol.147 , pp. 45-58
    • Shamu, C.E.1    Story, C.M.2    Rapoport, T.A.3    Ploegh, H.L.4
  • 23
    • 80455164551 scopus 로고    scopus 로고
    • Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant-1 antitrypsin from the endoplasmic reticulum
    • Greenblatt, E. J., Olzmann, J. A., and Kopito, R. R. (2011) Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant-1 antitrypsin from the endoplasmic reticulum. Nat. Struct. Mol. Biol. 18, 1147-1152
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1147-1152
    • Greenblatt, E.J.1    Olzmann, J.A.2    Kopito, R.R.3
  • 24
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by Eeyarestatin i
    • Wang, Q., Li, L., and Ye, Y. (2008) Inhibition of p97-dependent protein degradation by Eeyarestatin I. J. Biol. Chem. 283, 7445-7454
    • (2008) J. Biol. Chem. , vol.283 , pp. 7445-7454
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 25
    • 1642505493 scopus 로고    scopus 로고
    • Dissection of the dislocation pathway for type i membrane proteins with a new small molecule inhibitor, eeyarestatin
    • Fiebiger, E., Hirsch, C., Vyas, J. M., Gordon, E., Ploegh, H. L., and Tortorella, D. (2004) Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin. Mol. Biol. Cell 15, 1635-1646
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1635-1646
    • Fiebiger, E.1    Hirsch, C.2    Vyas, J.M.3    Gordon, E.4    Ploegh, H.L.5    Tortorella, D.6
  • 26
    • 70349778618 scopus 로고    scopus 로고
    • The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
    • Ernst, R., Mueller, B., Ploegh, H. L., and Schlieker, C. (2009) The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol. Cell 36, 28-38
    • (2009) Mol. Cell , vol.36 , pp. 28-38
    • Ernst, R.1    Mueller, B.2    Ploegh, H.L.3    Schlieker, C.4
  • 28
    • 84863620865 scopus 로고    scopus 로고
    • A viral deubiquitylating enzyme restores dislocation of substrates from the endoplasmic reticulum (ER) in semi-intact cells
    • Sanyal, S., Claessen, J. H., and Ploegh, H. L. (2012) A viral deubiquitylating enzyme restores dislocation of substrates from the endoplasmic reticulum (ER) in semi-intact cells. J. Biol. Chem. 287, 23594-23603
    • (2012) J. Biol. Chem. , vol.287 , pp. 23594-23603
    • Sanyal, S.1    Claessen, J.H.2    Ploegh, H.L.3
  • 31
    • 33745207334 scopus 로고    scopus 로고
    • Signal peptide peptidase is required for dislocation from the endoplasmic reticulum
    • Loureiro, J., Lilley, B. N., Spooner, E., Noriega, V., Tortorella, D., and Ploegh, H. L. (2006) Signal peptide peptidase is required for dislocation from the endoplasmic reticulum. Nature 441, 894-897
    • (2006) Nature , vol.441 , pp. 894-897
    • Loureiro, J.1    Lilley, B.N.2    Spooner, E.3    Noriega, V.4    Tortorella, D.5    Ploegh, H.L.6
  • 33
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley, B. N., and Ploegh, H. L. (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429, 834-840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 34
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D., and Rapoport, T. A. (2004) A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429, 841-847
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 35
    • 79952133558 scopus 로고    scopus 로고
    • HRD1 and UBE2J1 target misfoldedMHCclass i heavy chains for endoplasmic reticulum-associated degradation
    • Burr, M. L., Cano, F., Svobodova, S., Boyle, L. H., Boname, J. M., and Lehner, P. J. (2011) HRD1 and UBE2J1 target misfoldedMHCclass I heavy chains for endoplasmic reticulum-associated degradation. Proc. Natl. Acad. Sci. U.S.A. 108, 2034-2039
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2034-2039
    • Burr, M.L.1    Cano, F.2    Svobodova, S.3    Boyle, L.H.4    Boname, J.M.5    Lehner, P.J.6
  • 36
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • Lilley, B. N., and Ploegh, H. L. (2005) Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. U.S.A. 102, 14296-14301
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 37
    • 50449107542 scopus 로고    scopus 로고
    • SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
    • Mueller, B., Klemm, E. J., Spooner, E., Claessen, J. H., and Ploegh, H. L. (2008) SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc. Natl. Acad. Sci. U.S.A. 105, 12325-12330
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 12325-12330
    • Mueller, B.1    Klemm, E.J.2    Spooner, E.3    Claessen, J.H.4    Ploegh, H.L.5
  • 38
    • 34249042608 scopus 로고    scopus 로고
    • Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3
    • Wang, X., Herr, R. A., Chua, W. J., Lybarger, L., Wiertz, E. J., and Hansen, T. H. (2007) Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3. J. Cell Biol. 177, 613-624
    • (2007) J. Cell Biol. , vol.177 , pp. 613-624
    • Wang, X.1    Herr, R.A.2    Chua, W.J.3    Lybarger, L.4    Wiertz, E.J.5    Hansen, T.H.6
  • 39
    • 0344413468 scopus 로고    scopus 로고
    • Retrotranslocation of MHC class i heavy chain from the endoplasmic reticulum to the cytosol is dependent on ATP supply to the ER lumen
    • Albring, J., Koopmann, J. O., HAmmerling, G. J., and Momburg, F. (2004) Retrotranslocation of MHC class I heavy chain from the endoplasmic reticulum to the cytosol is dependent on ATP supply to the ER lumen. Mol. Immunol. 40, 733-741
    • (2004) Mol. Immunol. , vol.40 , pp. 733-741
    • Albring, J.1    Koopmann, J.O.2    Hammerling, G.J.3    Momburg, F.4
  • 40
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class i heavy chains are translocated into the cytoplasm and degraded by the proteasome
    • Hughes, E. A., Hammond, C., and Cresswell, P. (1997) Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. U.S.A. 94, 1896-1901
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1896-1901
    • Hughes, E.A.1    Hammond, C.2    Cresswell, P.3
  • 41
    • 80051975610 scopus 로고    scopus 로고
    • Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation
    • Petris, G., Vecchi, L., Bestagno, M., and Burrone, O. R. (2011) Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation. PLoS One. 6, e23712
    • (2011) PLoS One. , vol.6
    • Petris, G.1    Vecchi, L.2    Bestagno, M.3    Burrone, O.R.4
  • 42
    • 3543104812 scopus 로고    scopus 로고
    • Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class i and the peptide-loading complex
    • Wang, X., Lybarger, L., Connors, R., Harris, M. R., and Hansen, T. H. (2004) Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class I and the peptide-loading complex. J. Virol. 78, 8673-8686
    • (2004) J. Virol. , vol.78 , pp. 8673-8686
    • Wang, X.1    Lybarger, L.2    Connors, R.3    Harris, M.R.4    Hansen, T.H.5
  • 43
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • DuBridge, R. B., Tang, P., Hsia, H. C., Leong, P. M., Miller, J. H., and Calos, M. P. (1987) Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol. Cell Biol. 7, 379-387
    • (1987) Mol. Cell Biol. , vol.7 , pp. 379-387
    • Dubridge, R.B.1    Tang, P.2    Hsia, H.C.3    Leong, P.M.4    Miller, J.H.5    Calos, M.P.6
  • 44
  • 45
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett, D., Kovaleva, E., and Schatz, P. J. (1999) A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8, 921-929
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 46
    • 0029046720 scopus 로고
    • Characterization of class IMHCfolding intermediates and their disparate interactions with peptide and2-microglobulin
    • Smith, J. D., Solheim, J. C., Carreno, B. M., and Hansen, T. H. (1995) Characterization of class IMHCfolding intermediates and their disparate interactions with peptide and2-microglobulin. Mol. Immunol. 32, 531-540
    • (1995) Mol. Immunol. , vol.32 , pp. 531-540
    • Smith, J.D.1    Solheim, J.C.2    Carreno, B.M.3    Hansen, T.H.4
  • 47
    • 0019482402 scopus 로고
    • The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
    • Barker, D. F., and Campbell, A. M. (1981) The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase. J. Mol. Biol. 146, 451-467
    • (1981) J. Mol. Biol. , vol.146 , pp. 451-467
    • Barker, D.F.1    Campbell, A.M.2
  • 48
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda, R., Hoseki, J., Araki, K., Jansen, G., Thomas, D. Y., and Nagata, K. (2008) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321, 569-572
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 49
    • 48249155627 scopus 로고    scopus 로고
    • ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C
    • Dong, M., Bridges, J. P., Apsley, K., Xu, Y., and Weaver, T. E. (2008) ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol. Biol. Cell 19, 2620-2630
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2620-2630
    • Dong, M.1    Bridges, J.P.2    Apsley, K.3    Xu, Y.4    Weaver, T.E.5
  • 51
    • 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 Voorden, S., Wiertz, E., and Rapoport, T. A. (2005) 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, 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 Voorden, S.4    Wiertz, E.5    Rapoport, T.A.6
  • 52
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle. Cdc48p participates in the fusion of ER membranes
    • Latterich, M., Fröhlich, K. U., and Schekman, R. (1995) Membrane fusion and the cell cycle. Cdc48p participates in the fusion of ER membranes. Cell 82, 885-893
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Fröhlich, K.U.2    Schekman, R.3
  • 53
    • 84867011262 scopus 로고    scopus 로고
    • The small molecule inhibitor PR-619 of deubiquitinating enzymes affects the microtubule network and causes protein aggregate formation in neural cells
    • Seiberlich, V., Goldbaum, O., Zhukareva, V., and Richter-Landsberg, C. (2012) The small molecule inhibitor PR-619 of deubiquitinating enzymes affects the microtubule network and causes protein aggregate formation in neural cells. Implications for neurodegenerative diseases. Biochim. Biophys. Acta 1823, 2057-2068
    • (2012) Implications for Neurodegenerative Diseases. Biochim. Biophys. Acta , vol.1823 , pp. 2057-2068
    • Seiberlich, V.1    Goldbaum, O.2    Zhukareva, V.3    Richter-Landsberg, C.4
  • 54
    • 1042278180 scopus 로고    scopus 로고
    • Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates. Roles of endoplamic reticulum-bound P97/Cdc48p and proteasome
    • Elkabetz, Y., Shapira, I., Rabinovich, E., and Bar-Nun, S. (2004) Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates. Roles of endoplamic reticulum-bound p97/Cdc48p and proteasome. J. Biol. Chem. 279, 3980-3989
    • (2004) J. Biol. Chem. , vol.279 , pp. 3980-3989
    • Elkabetz, Y.1    Shapira, I.2    Rabinovich, E.3    Bar-Nun, S.4
  • 57
    • 83255185097 scopus 로고    scopus 로고
    • Ubiquitination of substrates by esterification
    • Wang, X., Herr, R. A., and Hansen, T. H. (2012) Ubiquitination of substrates by esterification. Traffic 13, 19-24
    • (2012) Traffic , vol.13 , pp. 19-24
    • Wang, X.1    Herr, R.A.2    Hansen, T.H.3
  • 58
    • 77954904488 scopus 로고    scopus 로고
    • Serine residues in the cytosolic tail of the T-cell antigen receptor-chain mediate ubiquitination and endoplasmic reticulum-associated degradation of the unassembled protein
    • Ishikura, S., Weissman, A. M., and Bonifacino, J. S. (2010) Serine residues in the cytosolic tail of the T-cell antigen receptor-chain mediate ubiquitination and endoplasmic reticulum-associated degradation of the unassembled protein. J. Biol. Chem. 285, 23916-23924
    • (2010) J. Biol. Chem. , vol.285 , pp. 23916-23924
    • Ishikura, S.1    Weissman, A.M.2    Bonifacino, J.S.3
  • 59
    • 78650253267 scopus 로고    scopus 로고
    • Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids
    • Shimizu, Y., Okuda-Shimizu, Y., and Hendershot, L. M. (2010) Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Mol. Cell 40, 917-926
    • (2010) Mol. Cell , vol.40 , pp. 917-926
    • Shimizu, Y.1    Okuda-Shimizu, Y.2    Hendershot, L.M.3
  • 60
    • 0033601349 scopus 로고    scopus 로고
    • The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor
    • Yu, H., and Kopito, R. R. (1999) The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor. J. Biol. Chem. 274, 36852-36858
    • (1999) J. Biol. Chem. , vol.274 , pp. 36852-36858
    • Yu, H.1    Kopito, R.R.2
  • 63
    • 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
  • 64
    • 84866527405 scopus 로고    scopus 로고
    • Roles of p97-associated deubiquitinases in protein quality control at the endoplasmic reticulum
    • Liu, Y. and Ye, Y. (2012) Roles of p97-associated deubiquitinases in protein quality control at the endoplasmic reticulum. Curr. Protein Pept. Sci. 13, 436-446
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 436-446
    • Liu, Y.1    Ye, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.