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Volumn 287, Issue 19, 2012, Pages 15533-15543

Ubc13 and COOH terminus of Hsp70-interacting protein (CHIP) are required for growth hormone receptor endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACES; CHAIN FORMATION; CYTOSOLIC; GROWTH HORMONE RECEPTORS; MULTIMERIC; POLYUBIQUITINATION; SPECIFIC INTERACTION; TRANSDUCIN; UBIQUITIN; UBIQUITIN LIGASES; UBIQUITINATION;

EID: 84860868165     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.302521     Document Type: Article
Times cited : (27)

References (60)
  • 2
    • 0037162458 scopus 로고    scopus 로고
    • Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis
    • DOI 10.1073/pnas.152294299
    • Gent, J., van Kerkhof, P., Roza, M., Bu, G., and Strous, G. J. (2002) Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis. Proc. Natl. Acad. Sci. U.S.A. 99, 9858-9863 (Pubitemid 34831137)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.15 , pp. 9858-9863
    • Gent, J.1    Van Kerkhof, P.2    Roza, M.3    Bu, G.4    Strous, G.J.5
  • 3
    • 0034907888 scopus 로고    scopus 로고
    • Signal transduction via the growth hormone receptor
    • DOI 10.1016/S0898-6568(01)00186-3, PII S0898656801001863
    • Zhu, T., Goh, E. L., Graichen, R., Ling, L., and Lobie, P. E. (2001) Signal transduction via the growth hormone receptor. Cell Signal. 13, 599-616 (Pubitemid 32734097)
    • (2001) Cellular Signalling , vol.13 , Issue.9 , pp. 599-616
    • Zhu, T.1    Goh, E.L.K.2    Graichen, R.3    Ling, L.4    Lobie, P.E.5
  • 4
    • 84871711670 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 5
    • 0033521670 scopus 로고    scopus 로고
    • Identification of a novel ubiquitin conjugation motif, required for ligand-induced internalization of the growth hormone receptor
    • DOI 10.1093/emboj/18.1.28
    • Govers, R., ten Broeke, T., van Kerkhof, P., Schwartz, A. L., and Strous, G. J. (1999) Identification of a novel ubiquitin conjugation motif, required for ligand-induced internalization of the growth hormone receptor. EMBO J. 18, 28-36 (Pubitemid 29005020)
    • (1999) EMBO Journal , vol.18 , Issue.1 , pp. 28-36
    • Govers, R.1    Ten, B.T.2    Van Kerkhof, P.3    Schwartz, A.L.4    Strous, G.J.5
  • 6
    • 34547115036 scopus 로고    scopus 로고
    • The ubiquitin ligase SCF(βTrCP) regulates the degradation of the growth hormone receptor
    • DOI 10.1074/jbc.M702610200
    • van Kerkhof, P., Putters, J., and Strous, G. J. (2007) The ubiquitin ligase SCF(βTrCP) regulates the degradation of the growth hormone receptor. J. Biol. Chem. 282, 20475-20483 (Pubitemid 47099991)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20475-20483
    • Van Kerkhof, P.1    Putters, J.2    Strous, G.J.3
  • 8
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the I≲καππα∀B kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., and Chen, Z. J. (2000) Activation of the I≲κα ππα∀B kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103, 351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 10
    • 77951221830 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitination of the dopamine transporter requires WW3 and WW4 domains of Nedd4-2 and UBE2D ubiquitin-conjugating enzymes
    • Vina-Vilaseca, A., and Sorkin, A. (2010) Lysine 63-linked polyubiquitination of the dopamine transporter requires WW3 and WW4 domains of Nedd4-2 and UBE2D ubiquitin-conjugating enzymes. J. Biol. Chem. 285, 7645-7656
    • (2010) J. Biol. Chem. , vol.285 , pp. 7645-7656
    • Vina-Vilaseca, A.1    Sorkin, A.2
  • 11
    • 78650775634 scopus 로고    scopus 로고
    • UEV-1 is an ubiquitin-conjugating enzyme variant that regulates glutamate receptor trafficking in C. elegans neurons
    • Kramer, L. B., Shim, J., Previtera, M. L., Isack, N. R., Lee, M. C., Firestein, B. L., and Rongo, C. (2010) UEV-1 is an ubiquitin-conjugating enzyme variant that regulates glutamate receptor trafficking in C. elegans neurons. PLoS ONE 5, e14291
    • (2010) PLoS ONE , vol.5
    • Kramer, L.B.1    Shim, J.2    Previtera, M.L.3    Isack, N.R.4    Lee, M.C.5    Firestein, B.L.6    Rongo, C.7
  • 12
    • 67749127761 scopus 로고    scopus 로고
    • Glucose-induced ubiquitylation and endocytosis of the yeast Jen1 transporter. Role of lysine 63-linked ubiquitin chains
    • Paiva, S., Vieira, N., Nondier, I., Haguenauer-Tsapis, R., Casal, M., and Urban-Grimal, D. (2009) Glucose-induced ubiquitylation and endocytosis of the yeast Jen1 transporter. Role of lysine 63-linked ubiquitin chains. J. Biol. Chem. 284, 19228-19236
    • (2009) J. Biol. Chem. , vol.284 , pp. 19228-19236
    • Paiva, S.1    Vieira, N.2    Nondier, I.3    Haguenauer-Tsapis, R.4    Casal, M.5    Urban-Grimal, D.6
  • 15
    • 44349182079 scopus 로고    scopus 로고
    • Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes
    • Xu, Z., Kohli, E., Devlin, K. I., Bold, M., Nix, J. C., and Misra, S. (2008) Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes. BMC Struct. Biol. 8, 26
    • (2008) BMC Struct. Biol. , vol.8 , pp. 26
    • Xu, Z.1    Kohli, E.2    Devlin, K.I.3    Bold, M.4    Nix, J.C.5    Misra, S.6
  • 16
    • 27944495299 scopus 로고    scopus 로고
    • Chaperoned ubiquitylation - Crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex
    • DOI 10.1016/j.molcel.2005.09.023, PII S1097276505016448
    • Zhang, M., Windheim, M., Roe, S. M., Peggie, M., Cohen, P., Prodromou, C., and Pearl, L. H. (2005) Chaperoned ubiquitylation. Crystal structures of the CHIPUbox E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. Mol. Cell 20, 525-538 (Pubitemid 41668638)
    • (2005) Molecular Cell , vol.20 , Issue.4 , pp. 525-538
    • Zhang, M.1    Windheim, M.2    Roe, S.M.3    Peggie, M.4    Cohen, P.5    Prodromou, C.6    Pearl, L.H.7
  • 17
    • 79958694800 scopus 로고    scopus 로고
    • E2 conjugating enzyme selectivity and requirements for function of the E3 ubiquitin ligase CHIP
    • Soss, S. E., Yue, Y., Dhe-Paganon, S., and Chazin, W. J. (2011) E2 conjugating enzyme selectivity and requirements for function of the E3 ubiquitin ligase CHIP. J. Biol. Chem. 286, 21277-21286
    • (2011) J. Biol. Chem. , vol.286 , pp. 21277-21286
    • Soss, S.E.1    Yue, Y.2    Dhe-Paganon, S.3    Chazin, W.J.4
  • 18
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger, C. A., Connell, P., Wu, Y., Hu, Z., Thompson, L. J., Yin, L. Y., and Patterson, C. (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19, 4535-4545 (Pubitemid 29242026)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.6 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.-Y.6    Patterson, C.7
  • 19
    • 77949371541 scopus 로고    scopus 로고
    • Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes
    • Graf, C., Stankiewicz, M., Nikolay, R., and Mayer, M. P. (2010) Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes. Biochemistry 49, 2121-2129
    • (2010) Biochemistry , vol.49 , pp. 2121-2129
    • Graf, C.1    Stankiewicz, M.2    Nikolay, R.3    Mayer, M.P.4
  • 20
    • 79955538576 scopus 로고    scopus 로고
    • Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP)
    • Wang, L., Liu, Y. T., Hao, R., Chen, L., Chang, Z., Wang, H. R., Wang, Z. X., and Wu, J. W. (2011) Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP). J. Biol. Chem. 286, 15883-15894
    • (2011) J. Biol. Chem. , vol.286 , pp. 15883-15894
    • Wang, L.1    Liu, Y.T.2    Hao, R.3    Chen, L.4    Chang, Z.5    Wang, H.R.6    Wang, Z.X.7    Wu, J.W.8
  • 22
    • 33746009937 scopus 로고    scopus 로고
    • A novel route for F-box protein-mediated ubiquitination links CHIP to glycoprotein quality control
    • DOI 10.1074/jbc.M602423200
    • Nelson, R. F., Glenn, K. A., Miller, V. M., Wen, H., and Paulson, H. L. (2006) A novel route for F-box protein-mediated ubiquitination links CHIP to glycoprotein quality control. J. Biol. Chem. 281, 20242-20251 (Pubitemid 44065799)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.29 , pp. 20242-20251
    • Nelson, R.F.1    Glenn, K.A.2    Miller, V.M.3    Wen, H.4    Paulson, H.L.5
  • 23
    • 38149018579 scopus 로고    scopus 로고
    • Ubiquitination and degradation of Tal1/SCL are induced by notch signaling and depend on Skp2 and CHIP
    • Nie, L., Wu, H., and Sun, X. H. (2008) Ubiquitination and degradation of Tal1/SCL are induced by notch signaling and depend on Skp2 and CHIP. J. Biol. Chem. 283, 684-692
    • (2008) J. Biol. Chem. , vol.283 , pp. 684-692
    • Nie, L.1    Wu, H.2    Sun, X.H.3
  • 24
    • 39549106043 scopus 로고    scopus 로고
    • CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins
    • DOI 10.1016/j.molcel.2007.12.027, PII S1097276508000956
    • Parsons, J. L., Tait, P. S., Finch, D., Dianova, I. I., Allinson, S. L., and Dianov, G. L. (2008) CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins. Mol. Cell 29, 477-487 (Pubitemid 351282540)
    • (2008) Molecular Cell , vol.29 , Issue.4 , pp. 477-487
    • Parsons, J.L.1    Tait, P.S.2    Finch, D.3    Dianova, I.I.4    Allinson, S.L.5    Dianov, G.L.6
  • 26
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous, G. J., van Kerkhof, P., Govers, R., Ciechanover, A., and Schwartz, A. L. (1996) The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J. 15, 3806-3812 (Pubitemid 26289790)
    • (1996) EMBO Journal , vol.15 , Issue.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.L.5
  • 27
    • 0042569021 scopus 로고    scopus 로고
    • Small glutamine-rich tetratricopeptide repeat-containing protein (SGT) interacts with the ubiquitin-dependent endocytosis (UbE) motif of the growth hormone receptor
    • DOI 10.1042/BJ20021591
    • Schantl, J. A., Roza, M., De Jong, A. P., and Strous, G. J. (2003) Small glutamine-rich tetratricopeptide repeat-containing protein (SGT) interacts with the ubiquitin-dependent endocytosis (UbE) motif of the growth hormone receptor. Biochem. J. 373, 855-863 (Pubitemid 36981095)
    • (2003) Biochemical Journal , vol.373 , Issue.3 , pp. 855-863
    • Schantl, J.A.1    Roza, M.2    De Jong, A.P.3    Strous, G.J.4
  • 28
    • 67949091245 scopus 로고    scopus 로고
    • Vps-C complexes. Gatekeepers of endolysosomal traffic
    • Nickerson, D. P., Brett, C. L., and Merz, A. J. (2009) Vps-C complexes. Gatekeepers of endolysosomal traffic. Curr Opin Cell Biol. 21, 543-551
    • (2009) Curr Opin Cell Biol. , vol.21 , pp. 543-551
    • Nickerson, D.P.1    Brett, C.L.2    Merz, A.J.3
  • 29
    • 0037073739 scopus 로고    scopus 로고
    • Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways
    • DOI 10.1074/jbc.M206271200
    • van Dam, E. M., Ten Broeke, T., Jansen, K., Spijkers, P., and Stoorvogel, W. (2002) Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways. J. Biol. Chem. 277, 48876-48883 (Pubitemid 35470856)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48876-48883
    • Van Dam, E.M.1    Ten, B.T.2    Jansen, K.3    Spijkers, P.4    Stoorvogel, W.5
  • 30
    • 0021960815 scopus 로고
    • Measurement of growth hormone and prolactin receptor turnover in rat liver
    • Baxter, R. C. (1985) Measurement of growth hormone and prolactin receptor turnover in rat liver. Endocrinology 117, 650-655
    • (1985) Endocrinology , vol.117 , pp. 650-655
    • Baxter, R.C.1
  • 31
    • 0021209107 scopus 로고
    • The mouse fibroblast growth hormone receptor: Ligand processing and receptor modulation and turnover
    • Murphy, L. J., and Lazarus, L. (1984) The mouse fibroblast growth hormone receptor. Ligand processing and receptor modulation and turnover. Endocrinology 115, 1625-1632 (Pubitemid 14000335)
    • (1984) Endocrinology , vol.115 , Issue.4 , pp. 1625-1632
    • Murphy, L.J.1    Lazarus, L.2
  • 32
    • 0023949967 scopus 로고
    • Intracellular processing of growth hormone receptors by adipocytes in primary culture
    • Roupas, P., and Herington, A. C. (1988) Intracellular processing of growth hormone receptors by adipocytes in primary culture. Mol. Cell. Endocrinol. 57, 93-99
    • (1988) Mol. Cell. Endocrinol. , vol.57 , pp. 93-99
    • Roupas, P.1    Herington, A.C.2
  • 33
    • 0036215093 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway regulates the availability of the GH receptor
    • DOI 10.1210/en.143.4.1243
    • van Kerkhof, P., Smeets, M., and Strous, G. J. (2002) The ubiquitin-proteasome pathway regulates the availability of the GH receptor. Endocrinology 143, 1243-1252 (Pubitemid 34274353)
    • (2002) Endocrinology , vol.143 , Issue.4 , pp. 1243-1252
    • Van Kerkhof, P.1    Smeets, M.2    Strous, G.J.3
  • 34
    • 70350236409 scopus 로고    scopus 로고
    • Mechanisms for rescue of correctable folding defects in CFTRΔ F508
    • Grove, D. E., Rosser, M. F., Ren, H. Y., Naren, A. P., and Cyr, D. M. (2009) Mechanisms for rescue of correctable folding defects in CFTRΔ F508. Mol. Biol. Cell 20, 4059-4069
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4059-4069
    • Grove, D.E.1    Rosser, M.F.2    Ren, H.Y.3    Naren, A.P.4    Cyr, D.M.5
  • 35
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • DOI 10.1038/35050509
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., and Cyr, D. M. (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 3, 100-105 (Pubitemid 32114840)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 36
    • 33748309115 scopus 로고    scopus 로고
    • Disulfide bonds determine growth hormone receptor folding, dimerisation and ligand binding
    • DOI 10.1242/jcs.03036
    • van den Eijnden, M. J., Lahaye, L. L., and Strous, G. J. (2006) Disulfide bonds determine growth hormone receptor folding, dimerisation and ligand binding. J. Cell Sci. 119, 3078-3086 (Pubitemid 44322122)
    • (2006) Journal of Cell Science , vol.119 , Issue.15 , pp. 3078-3086
    • Van den, E.M.J.M.1    Lahaye, L.L.2    Strous, G.J.3
  • 37
    • 0033529537 scopus 로고    scopus 로고
    • The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor
    • Waterman, H., Levkowitz, G., Alroy, I., and Yarden, Y. (1999) The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor. J. Biol. Chem. 274, 22151-22154
    • (1999) J. Biol. Chem. , vol.274 , pp. 22151-22154
    • Waterman, H.1    Levkowitz, G.2    Alroy, I.3    Yarden, Y.4
  • 41
    • 33748969492 scopus 로고    scopus 로고
    • Endocytic adaptors: recruiters, coordinators and regulators
    • DOI 10.1016/j.tcb.2006.08.001, PII S0962892406001978, Membrane Dynamics
    • Maldonado-Báez, L., and Wendland, B. (2006) Endocytic adaptors. Recruiters, coordinators and regulators. Trends Cell Biol. 16, 505-513 (Pubitemid 44442957)
    • (2006) Trends in Cell Biology , vol.16 , Issue.10 , pp. 505-513
    • Maldonado-Baez, L.1    Wendland, B.2
  • 42
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • DOI 10.1038/416451a
    • Polo, S., Sigismund, S., Faretta, M., Guidi, M., Capua, M. R., Bossi, G., Chen, H., De Camilli, P., and Di Fiore, P. P. (2002) A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451-455 (Pubitemid 34272882)
    • (2002) Nature , vol.416 , Issue.6879 , pp. 451-455
    • Polo, S.1    Sigismund, S.2    Faretta, M.3    Guidi, M.4    Capua, M.R.5    Bossi, G.6    Chen, H.7    De Camilli, P.8    Di, F.P.P.9
  • 45
    • 78651093198 scopus 로고    scopus 로고
    • The multiple facets of ubiquitination in the regulation of notch signaling pathway
    • Le Bras, S., Loyer, N., and Le Borgne, R. (2011) The multiple facets of ubiquitination in the regulation of notch signaling pathway. Traffic 12, 149-161
    • (2011) Traffic , vol.12 , pp. 149-161
    • Le Bras, S.1    Loyer, N.2    Le Borgne, R.3
  • 48
    • 79955828987 scopus 로고    scopus 로고
    • Molecular mechanisms of ubiquitin-dependent membrane traffic
    • Hurley, J. H., and Stenmark, H. (2011) Molecular mechanisms of ubiquitin-dependent membrane traffic. Annu Rev. Biophys. 40, 119-142
    • (2011) Annu Rev. Biophys. , vol.40 , pp. 119-142
    • Hurley, J.H.1    Stenmark, H.2
  • 50
    • 48649110734 scopus 로고    scopus 로고
    • Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis
    • Sehat, B., Andersson, S., Girnita, L., and Larsson, O. (2008) Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis. Cancer Res. 68, 5669-5677
    • (2008) Cancer Res. , vol.68 , pp. 5669-5677
    • Sehat, B.1    Andersson, S.2    Girnita, L.3    Larsson, O.4
  • 51
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • DOI 10.1016/j.molcel.2006.02.018, PII S1097276506001201
    • Huang, F., Kirkpatrick, D., Jiang, X., Gygi, S., and Sorkin, A. (2006) Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 21, 737-748 (Pubitemid 43376125)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 53
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M., and Haguenauer-Tsapis, R. (1997) Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein.EMBOJ. 16, 5847-5854
    • (1997) EMBOJ. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 54
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • DOI 10.1038/nature00991
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141 (Pubitemid 35025438)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 55
    • 0035159679 scopus 로고    scopus 로고
    • Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins
    • van Kerkhof, P., Alves dos Santos, C. M., Sachse, M., Klumperman, J., Bu, G., and Strous, G. J. (2001) Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins. Mol. Biol. Cell 12, 2556-2566 (Pubitemid 33051975)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2556-2566
    • Van Kerkhof, P.1    Alves, D.S.C.M.2    Sachse, M.3    Klumperman, J.4    Bu, G.5    Strous, G.J.6
  • 56
    • 38949212916 scopus 로고    scopus 로고
    • Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology
    • DOI 10.1042/BJ20071338
    • Windheim, M., Peggie, M., and Cohen, P. (2008) Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology. Biochem. J. 409, 723-729 (Pubitemid 351214198)
    • (2008) Biochemical Journal , vol.409 , Issue.3 , pp. 723-729
    • Windheim, M.1    Peggie, M.2    Cohen, P.3
  • 57
    • 78149456945 scopus 로고    scopus 로고
    • WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins
    • Pashkova, N., Gakhar, L., Winistorfer, S. C., Yu, L., Ramaswamy, S., and Piper, R. C. (2010) WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol. Cell 40, 433-443
    • (2010) Mol. Cell , vol.40 , pp. 433-443
    • Pashkova, N.1    Gakhar, L.2    Winistorfer, S.C.3    Yu, L.4    Ramaswamy, S.5    Piper, R.C.6
  • 58
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • DOI 10.1016/S0968-0004(02)02125-4, PII S0968000402021254
    • Cyr, D. M., Höhfeld, J., and Patterson, C. (2002) Protein quality control. U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27, 368-375 (Pubitemid 34756520)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.7 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 59
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality-control E3 ligase collaborating with molecular chaperones
    • DOI 10.1016/S1357-2725(02)00394-1
    • Murata, S., Chiba, T., and Tanaka, K. (2003) CHIP. A quality-control E3 ligase collaborating with molecular chaperones. Int. J. Biochem. Cell Biol. 35, 572-578 (Pubitemid 36369506)
    • (2003) International Journal of Biochemistry and Cell Biology , vol.35 , Issue.5 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3


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