메뉴 건너뛰기




Volumn 15, Issue 2, 2003, Pages 184-190

Ubiquitin: Not just for proteasomes anymore

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; NOTCH RECEPTOR; PROTEASOME; UBIQUITIN;

EID: 0037376172     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00010-3     Document Type: Review
Times cited : (147)

References (49)
  • 1
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A.M. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2:2001;169-178.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 2
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2:2001;195-201.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 4
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 5
    • 0037080811 scopus 로고    scopus 로고
    • LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation
    • Identification of an E3 enzyme that modifies Notch, and describes an important mechanism that controls signaling through the Notch pathway
    • Nie J., McGill M.A., Dermer M., Dho S.E., Wolting C.D., McGlade C.J. LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation. EMBO J. 21:2002;93-102 Identification of an E3 enzyme that modifies Notch, and describes an important mechanism that controls signaling through the Notch pathway.
    • (2002) EMBO J. , vol.21 , pp. 93-102
    • Nie, J.1    McGill, M.A.2    Dermer, M.3    Dho, S.E.4    Wolting, C.D.5    McGlade, C.J.6
  • 6
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolytic steps in the Generation of antigenic peptides
    • Goldberg A., Cascio P., Saric T., Rock K. The importance of the proteasome and subsequent proteolytic steps in the Generation of antigenic peptides. Mol. Immunol. 39:2002;147-164.
    • (2002) Mol. Immunol. , vol.39 , pp. 147-164
    • Goldberg, A.1    Cascio, P.2    Saric, T.3    Rock, K.4
  • 7
    • 0037094434 scopus 로고    scopus 로고
    • Nitrogen regulation in Saccharomyces cerevisiae
    • Magasanik B., Kaiser C.A. Nitrogen regulation in Saccharomyces cerevisiae. Gene. 290:2002;1-18.
    • (2002) Gene. , vol.290 , pp. 1-18
    • Magasanik, B.1    Kaiser, C.A.2
  • 10
    • 0032563560 scopus 로고    scopus 로고
    • A large PEST-like sequence directs the ubiquitination, endocytosis, and vacuolar degradation of the yeast a-factor receptor
    • Roth A.F., Sullivan D.M., Davis N.G. A large PEST-like sequence directs the ubiquitination, endocytosis, and vacuolar degradation of the yeast a-factor receptor. J. Cell Biol. 142:1998;949-961.
    • (1998) J. Cell Biol. , vol.142 , pp. 949-961
    • Roth, A.F.1    Sullivan, D.M.2    Davis, N.G.3
  • 11
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • Hicke L. Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J. 11:1997;1215-1226.
    • (1997) FASEB J. , vol.11 , pp. 1215-1226
    • Hicke, L.1
  • 12
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • Rotin D., Staub O., Haguenauer-Tsapis R. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J. Membr. Biol. 176:2000;1-17.
    • (2000) J. Membr. Biol. , vol.176 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 13
    • 0034949705 scopus 로고    scopus 로고
    • C-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route
    • This paper provides evidence about where c-Cbl and the epidermal growth factor receptor associate, and convincingly demonstrates a role for c-Cbl in clathrin-dependent endocytosis
    • de Melker A.A., van der Horst G., Calafat J., Jansen H., Borst J. c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route. J. Cell Sci. 114:2001;2167-2178 This paper provides evidence about where c-Cbl and the epidermal growth factor receptor associate, and convincingly demonstrates a role for c-Cbl in clathrin-dependent endocytosis.
    • (2001) J. Cell Sci. , vol.114 , pp. 2167-2178
    • De Melker, A.A.1    Van der Horst, G.2    Calafat, J.3    Jansen, H.4    Borst, J.5
  • 14
    • 0037125983 scopus 로고    scopus 로고
    • Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors
    • Haglund K., Shimokawa N., Szymkiewicz I., Dikic I. Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. Proc. Natl. Acad. Sci. U.S.A. 99:2002;12191-12196.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12191-12196
    • Haglund, K.1    Shimokawa, N.2    Szymkiewicz, I.3    Dikic, I.4
  • 15
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • ••], this paper reveals an interplay between receptor tyrosine kinases, c-Cbl, CIN85, and endophilin. Evidence from two-hybrid and biochemical characterization of the interactions in yeast is complemented by the consequences of complex-formation on signal transduction
    • ••], this paper reveals an interplay between receptor tyrosine kinases, c-Cbl, CIN85, and endophilin. Evidence from two-hybrid and biochemical characterization of the interactions in yeast is complemented by the consequences of complex-formation on signal transduction.
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 16
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J. Cell Biol. 155:2001;193-200.
    • (2001) J. Cell Biol. , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De Camilli, P.6
  • 19
    • 0037069388 scopus 로고    scopus 로고
    • Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3
    • Qiu X.B., Goldberg A.L. Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3. Proc. Natl. Acad. Sci. U.S.A. 99:2002;14843-14848.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14843-14848
    • Qiu, X.B.1    Goldberg, A.L.2
  • 21
    • 0035369556 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
    • Bioinformatics study that defined the ubiquitin interaction motif (UIM), a novel ubiquitin-binding domain, and identified UIMs in many components of the cytoplasmic endocytic machinery
    • Hofmann K., Falquet L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem. Sci. 26:2001;347-350 Bioinformatics study that defined the ubiquitin interaction motif (UIM), a novel ubiquitin-binding domain, and identified UIMs in many components of the cytoplasmic endocytic machinery.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 347-350
    • Hofmann, K.1    Falquet, L.2
  • 22
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • Demonstrated ubiquitin modification of components of the endocytic machinery that requires the ubiquitin interaction motif
    • Polo S., Sigismund S., Faretta M., Guidi M., Capua M.R., Bossi G., Chen H., De Camilli P., Di Fiore P.P. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature. 416:2002;451-455 Demonstrated ubiquitin modification of components of the endocytic machinery that requires the ubiquitin interaction motif.
    • (2002) Nature , vol.416 , 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 Fiore, P.P.9
  • 24
    • 0037046805 scopus 로고    scopus 로고
    • The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination
    • Oldham C.E., Mohney R.P., Miller S.L., Hanes R.N., O'Bryan J.P. The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination. Curr. Biol. 12:2002;1112-1116.
    • (2002) Curr. Biol. , vol.12 , pp. 1112-1116
    • Oldham, C.E.1    Mohney, R.P.2    Miller, S.L.3    Hanes, R.N.4    O'Bryan, J.P.5
  • 25
    • 0037010119 scopus 로고    scopus 로고
    • Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function
    • Strous G., Gent J. Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function. FEBS Lett. 529:2002;102-109.
    • (2002) FEBS Lett. , vol.529 , pp. 102-109
    • Strous, G.1    Gent, J.2
  • 28
    • 0036696444 scopus 로고    scopus 로고
    • The endocytic protein alpha-adaptin is required for Numb-mediated asymmetric cell division in Drosophila
    • The authors provide the first physiologically relevant evidence for Numb-mediated ubiquitin-dependent downregulation of Notch
    • Berdnik D., Torok T., Gonzalez-Gaitan M., Knoblich J.A. The endocytic protein alpha-adaptin is required for Numb-mediated asymmetric cell division in Drosophila. Dev. Cell. 3:2002;221-231 The authors provide the first physiologically relevant evidence for Numb-mediated ubiquitin-dependent downregulation of Notch.
    • (2002) Dev. Cell , vol.3 , pp. 221-231
    • Berdnik, D.1    Torok, T.2    Gonzalez-Gaitan, M.3    Knoblich, J.A.4
  • 30
    • 0035650895 scopus 로고    scopus 로고
    • Xenopus neuralized is a ubiquitin ligase that interacts with XDelta1 and regulates Notch signaling
    • •]) demonstrate a role for the E3 ligase Neuralized in the downregulation of Delta. This shows that ubiquitin can downregulate ligands (e.g. Delta) in addition to receptors (e.g. Notch)
    • •]) demonstrate a role for the E3 ligase Neuralized in the downregulation of Delta. This shows that ubiquitin can downregulate ligands (e.g. Delta) in addition to receptors (e.g. Notch).
    • (2001) Dev. Cell , vol.1 , pp. 795-806
    • Deblandre, G.A.1    Lai, E.C.2    Kintner, C.3
  • 33
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Demonstration of the ubiquitin-binding activity of the ubiquitin interaction motifs (UIMs) of two components of the endocytic machinery: one that functions at the plasma membrane, and another that functions at multivesicular bodies. UIM function was identified as critical in sorting at the multivesicular body
    • Shih S.C., Katzmann D.J., Schnell J.D., Sutanto M., Emr S.D., Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4:2002;389-393 Demonstration of the ubiquitin-binding activity of the ubiquitin interaction motifs (UIMs) of two components of the endocytic machinery: one that functions at the plasma membrane, and another that functions at multivesicular bodies. UIM function was identified as critical in sorting at the multivesicular body.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 34
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • The first description of cytosolic machinery that controls formation of multivesicular body lumenal vesicles and ubiquitin-dependent sorting of cargo into these vesicles
    • Katzmann D.J., Babst M., Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell. 106:2001;145-155 The first description of cytosolic machinery that controls formation of multivesicular body lumenal vesicles and ubiquitin-dependent sorting of cargo into these vesicles.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 35
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • A description of how HIV co-opts the lumenal vesicle-budding machinery of multivesicuar bodies for budding from the plasma membrane of infected cells
    • Garrus J.E., von Schwedler U.K., Pornillos O.W., Morham S.G., Zavitz K.H., Wang H.E., Wettstein D.A., Stray K.M., Cote M., Rich R.L.et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell. 107:2001;55-65 A description of how HIV co-opts the lumenal vesicle-budding machinery of multivesicuar bodies for budding from the plasma membrane of infected cells.
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1    Von Schwedler, U.K.2    Pornillos, O.W.3    Morham, S.G.4    Zavitz, K.H.5    Wang, H.E.6    Wettstein, D.A.7    Stray, K.M.8    Cote, M.9    Rich, R.L.10
  • 36
    • 0036080376 scopus 로고    scopus 로고
    • Regulated SUMOylation and ubiquitination of DdMEK1 is required for proper chemotaxis
    • Shows the dynamics of antagonistic functions of ubiquitin and SUMO for nuclear transport in connection with downregulation of signal transduction
    • Sobko A., Ma H., Firtel R.A. Regulated SUMOylation and ubiquitination of DdMEK1 is required for proper chemotaxis. Dev. Cell. 2:2002;745-756 Shows the dynamics of antagonistic functions of ubiquitin and SUMO for nuclear transport in connection with downregulation of signal transduction.
    • (2002) Dev. Cell , vol.2 , pp. 745-756
    • Sobko, A.1    Ma, H.2    Firtel, R.A.3
  • 37
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • Conaway R.C., Brower C.S., Conaway J.W. Emerging roles of ubiquitin in transcription regulation. Science. 296:2002;1254-1258.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 38
    • 0036348150 scopus 로고    scopus 로고
    • Dual regulation of the Met4 transcription factor by ubiquitin-dependent degradation and inhibition of promoter recruitment
    • Uncovers growth-condition-specific regulation of Met4 and shows in some cases that ubiquitin-Met4 is not degraded, but instead exerts differential activity on distinct promoters
    • Kuras L., Rouillon A., Lee T., Barbey R., Tyers M., Thomas D. Dual regulation of the Met4 transcription factor by ubiquitin-dependent degradation and inhibition of promoter recruitment. Mol Cell. 10:2002;69-80 Uncovers growth-condition-specific regulation of Met4 and shows in some cases that ubiquitin-Met4 is not degraded, but instead exerts differential activity on distinct promoters.
    • (2002) Mol Cell , vol.10 , pp. 69-80
    • Kuras, L.1    Rouillon, A.2    Lee, T.3    Barbey, R.4    Tyers, M.5    Thomas, D.6
  • 39
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K., Recht J., Osley M.A. Rad6-dependent ubiquitination of histone H2B in yeast. Science. 287:2000;501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 40
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and Gene. silencing in yeast
    • This work demonstrates the synergistic effects between ubiquitination and methylation of histones in controlling transcription
    • Sun Z.W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and Gene. silencing in yeast. Nature. 418:2002;104-108 This work demonstrates the synergistic effects between ubiquitination and methylation of histones in controlling transcription.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 41
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • This paper provides compelling evidence for a proteasome-independent ubiquitin-mediated mechanism for regulation transcription factors
    • Salghetti S.E., Caudy A.A., Chenoweth J.G., Tansey W.P. Regulation of transcriptional activation domain function by ubiquitin. Science. 293:2001;1651-1653 This paper provides compelling evidence for a proteasome-independent ubiquitin-mediated mechanism for regulation transcription factors.
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 42
    • 0036237383 scopus 로고    scopus 로고
    • Versatile protein tag, SUMO: Its enzymology and biological function
    • Kim K.I., Baek S.H., Chung C.H. Versatile protein tag, SUMO: its enzymology and biological function. J. Cell Physiol. 191:2002;257-268.
    • (2002) J. Cell Physiol. , vol.191 , pp. 257-268
    • Kim, K.I.1    Baek, S.H.2    Chung, C.H.3
  • 43
    • 0035478483 scopus 로고    scopus 로고
    • COP9 signalosome revisited: A novel mediator of protein degradation
    • Schwechheimer C., Deng X.W. COP9 signalosome revisited: a novel mediator of protein degradation. Trends Cell Biol. 11:2001;420-426.
    • (2001) Trends Cell Biol. , vol.11 , pp. 420-426
    • Schwechheimer, C.1    Deng, X.W.2
  • 44
    • 0037192523 scopus 로고    scopus 로고
    • Role of a ubiquitin-like modification in polarized morphogenesis
    • Dittmar G.A., Wilkinson C.R., Jedrzejewski P.T., Finley D. Role of a ubiquitin-like modification in polarized morphogenesis. Science. 295:2002;2442-2446.
    • (2002) Science , vol.295 , pp. 2442-2446
    • Dittmar, G.A.1    Wilkinson, C.R.2    Jedrzejewski, P.T.3    Finley, D.4
  • 45
    • 0037177798 scopus 로고    scopus 로고
    • Lipopolysaccharide activates the expression of ISG15-specific protease UBP43 via interferon regulatory factor 3
    • Malakhova O., Malakhov M., Hetherington C., Zhang D.E. Lipopolysaccharide activates the expression of ISG15-specific protease UBP43 via interferon regulatory factor 3. J. Biol. Chem. 277:2002;14703-14711.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14703-14711
    • Malakhova, O.1    Malakhov, M.2    Hetherington, C.3    Zhang, D.E.4
  • 46
    • 0036702197 scopus 로고    scopus 로고
    • Molecular machinery required for autophagy and the cytoplasm to vacuole targeting (Cvt) pathway in S. cerevisiae
    • Khalfan W., Klionsky D. Molecular machinery required for autophagy and the cytoplasm to vacuole targeting (Cvt) pathway in S. cerevisiae. Curr Opin Cell Biol. 14:2002;468-475.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 468-475
    • Khalfan, W.1    Klionsky, D.2
  • 47
    • 0037072667 scopus 로고    scopus 로고
    • Ubiquitin lives up to its name
    • Marx J. Ubiquitin lives up to its name. Science. 297:2002;1792-1794.
    • (2002) Science , vol.297 , pp. 1792-1794
    • Marx, J.1
  • 48
    • 0036900545 scopus 로고    scopus 로고
    • New tricks for ubiquitin and friends
    • Wilkinson C. New tricks for ubiquitin and friends. Trends Cell Biol. 12:2002;545-546.
    • (2002) Trends Cell Biol. , vol.12 , pp. 545-546
    • Wilkinson, C.1
  • 49
    • 0036902408 scopus 로고    scopus 로고
    • Ubiquitin branches out
    • Johnson E.S. Ubiquitin branches out. Nat. Cell Biol. 4:2002;E295-E298.
    • (2002) Nat. Cell Biol. , vol.4
    • Johnson, E.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.