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Volumn 5, Issue 5, 2003, Pages 461-466

Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; LIGAND; PLATELET DERIVED GROWTH FACTOR RECEPTOR; POLYUBIQUITIN; PROTEASOME; TYROSINE KINASE RECEPTOR; UBIQUITIN;

EID: 0038394715     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb983     Document Type: Article
Times cited : (684)

References (30)
  • 1
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman, A. M. Themes and variations on ubiquitylation. Nature Rev. Mol. Cell Biol. 2, 169-178 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 2
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptations to regulate protein tyrosine kinases
    • Thien, C. B. & Langdon, W. Y. Cbl: many adaptations to regulate protein tyrosine kinases. Nature Rev. Mol. Cell Biol. 2, 294-307 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 3
    • 0035895664 scopus 로고    scopus 로고
    • Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases
    • Waterman, H. & Yarden, Y. Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases. FEBS Lett. 490, 142-152 (2001).
    • (2001) FEBS Lett. , vol.490 , pp. 142-152
    • Waterman, H.1    Yarden, Y.2
  • 4
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart, C. M. Ubiquitin in chains. Trends Biochem. Sci. 25, 544-548 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 5
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. Protein regulation by monoubiquitin. Nature Rev. Mol. Cell Biol. 2, 195-201 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 6
    • 0034607805 scopus 로고    scopus 로고
    • Polyubiquitination of the epidermal growth factor receptor occurs at the plasma membrane upon ligand-induced activation
    • Stang, E., Johannessen, L. E., Knardal, S. L. & Madshus, I. H. Polyubiquitination of the epidermal growth factor receptor occurs at the plasma membrane upon ligand-induced activation. J. Biol. Chem. 275, 13940-13947 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 13940-13947
    • Stang, E.1    Johannessen, L.E.2    Knardal, S.L.3    Madshus, I.H.4
  • 7
    • 0034949705 scopus 로고    scopus 로고
    • c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route
    • 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, 2167-2178 (2001).
    • (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
  • 8
    • 0032217156 scopus 로고    scopus 로고
    • c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz, G. et al. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12, 3663-3674 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3663-3674
    • Levkowitz, G.1
  • 9
    • 0037018146 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
    • Longva, K. E. et al. Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J. Cell Biol. 156, 843-854 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 843-854
    • Longva, K.E.1
  • 10
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L. & Riezman, H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84, 277-287 (1996).
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 11
    • 0036094538 scopus 로고    scopus 로고
    • Hrs sorts ubiquitinated protein into clathrin-coated microdomains of early endosomes
    • Raiborg, C. et al. Hrs sorts ubiquitinated protein into clathrin-coated microdomains of early endosomes. Nature Cell Biol. 4, 394-398 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 394-398
    • Raiborg, C.1
  • 12
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-1
    • 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-1. Cell 106, 145-155 (2001).
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 13
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • Polo, S. et al. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451-455 (2002).
    • (2002) Nature , vol.416 , pp. 451-455
    • Polo, S.1
  • 14
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason, T. & Ellison, M. J. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol. 14, 7876-7883 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 15
    • 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. USA 99, 12191-12196 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12191-12196
    • Haglund, K.1    Shimokawa, N.2    Szymkiewicz, I.3    Dikic, I.4
  • 16
    • 0024324505 scopus 로고
    • Epidermal growth factor and transforming growth factor alpha bind differently to the epidermal growth factor receptor
    • Winkler, M. E., O'Connor, L., Winget, M. & Fendly, B. Epidermal growth factor and transforming growth factor alpha bind differently to the epidermal growth factor receptor. Biochemistry 28, 6373-6378 ( 1989).
    • (1989) Biochemistry , vol.28 , pp. 6373-6378
    • Winkler, M.E.1    O'Connor, L.2    Winget, M.3    Fendly, B.4
  • 17
    • 0037075606 scopus 로고    scopus 로고
    • The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met
    • Petrelli, A. et al. The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met. Nature 416, 187-190 (2002).
    • (2002) Nature , vol.416 , pp. 187-190
    • Petrelli, A.1
  • 18
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • Soubeyran, P., Kowanetz, K., Szymkiewicz, I., Langdon, W. Y. & Dikic, I. Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416, 183-187 (2002).
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 19
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih, S. C., Sloper-Mould, K. E. & Hicke, L. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. EMBO J. 19, 187-198 (2000).
    • (2000) EMBO J. , vol.19 , pp. 187-198
    • Shih, S.C.1    Sloper-Mould, K.E.2    Hicke, L.3
  • 20
    • 0034714368 scopus 로고    scopus 로고
    • A Di-leucine signal in the ubiquitin moiety. Possible involvement in ubiquitination-mediated endocytosis
    • Nakatsu, F. et al. A Di-leucine signal in the ubiquitin moiety. Possible involvement in ubiquitination-mediated endocytosis. J. Biol. Chem. 275, 26213-26219 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26213-26219
    • Nakatsu, F.1
  • 21
    • 0035369556 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
    • Hofmann, K. & Falquet, L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem. Sci. 26, 347-350 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 347-350
    • Hofmann, K.1    Falquet, L.2
  • 22
    • 0031452290 scopus 로고    scopus 로고
    • Eps15 and Eps15R are essential components of the endocytic pathway
    • Carbone, R. et al. Eps15 and Eps15R are essential components of the endocytic pathway. Cancer Res. 57, 5498-5504 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 5498-5504
    • Carbone, R.1
  • 23
    • 0034698787 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis
    • Confalonieri, S., Salcini, A. E., Puri, C., Tacchetti, C. & Di Fiore, P. P. Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis. J. Cell Biol. 150, 905-912 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 905-912
    • Confalonieri, S.1    Salcini, A.E.2    Puri, C.3    Tacchetti, C.4    Di Fiore, P.P.5
  • 24
    • 0032552056 scopus 로고    scopus 로고
    • Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
    • Chen, H. et al. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 394, 793-797 (1998).
    • (1998) Nature , vol.394 , pp. 793-797
    • Chen, H.1
  • 25
    • 0031467675 scopus 로고    scopus 로고
    • Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15
    • Cupers, P., ter Haar, E., Boll, W. & Kirchhausen T. Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15. J. Biol. Chem. 272, 33430-33434 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 33430-33434
    • Cupers, P.1    ter Haar, E.2    Boll, W.3    Kirchhausen, T.4
  • 26
    • 0036392305 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins
    • Shekhtman, A. & Cowburn, D. A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins. Biochem. Biophys. Res. Commun. 296, 1222-1227 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 1222-1227
    • Shekhtman, A.1    Cowburn, D.2
  • 27
    • 0035954425 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of endocytic proteins
    • Vecchi, M. et al. Nucleocytoplasmic shuttling of endocytic proteins. J. Cell Biol. 153, 1511-1517 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1511-1517
    • Vecchi, M.1
  • 28
    • 0037131177 scopus 로고    scopus 로고
    • CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases
    • Szymkiewicz, I. et al. CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases. J. Biol. Chem. 277, 39666-39672 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39666-39672
    • Szymkiewicz, I.1
  • 29
    • 0025320158 scopus 로고
    • EGF receptor and erbB-2 tyrosine kinase domains confer cell specificity for mitogenic signaling
    • Di Fiore, P. P., Segatto, O., Taylor, W. G., Aaronson, S. A. & Pierce, J. H. EGF receptor and erbB-2 tyrosine kinase domains confer cell specificity for mitogenic signaling. Science 248, 79-83 (1990).
    • (1990) Science , vol.248 , pp. 79-83
    • Di Fiore, P.P.1    Segatto, O.2    Taylor, W.G.3    Aaronson, S.A.4    Pierce, J.H.5
  • 30
    • 0025352187 scopus 로고
    • Advanced mammalian gene transfer: High titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line
    • Morgenstern, J. P. & Land, H. Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line, Nucleic Acids Res. 18, 3587-3596 (1990).
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3587-3596
    • Morgenstern, J.P.1    Land, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.