메뉴 건너뛰기




Volumn 460, Issue A, 2009, Pages 413-422

Chapter 21 Ubiquitination of Chemokine Receptors

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOKINE RECEPTOR; CHEMOKINE RECEPTOR CXCR4; G PROTEIN COUPLED RECEPTOR; PROTEASOME; UBIQUITIN PROTEIN LIGASE E3; ITCH PROTEIN, HUMAN; REPRESSOR PROTEIN; STROMAL CELL DERIVED FACTOR 1; UBIQUITIN PROTEIN LIGASE;

EID: 65549095888     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)05221-5     Document Type: Review
Times cited : (13)

References (23)
  • 1
    • 37549035071 scopus 로고    scopus 로고
    • Arrestin-2 Interacts with the Ubiquitin-Protein Isopeptide Ligase Atrophin-interacting Protein 4 and Mediates Endosomal Sorting of the Chemokine Receptor CXCR4
    • Bhandari D., Trejo J., Benovic J.L., and Marchese A. Arrestin-2 Interacts with the Ubiquitin-Protein Isopeptide Ligase Atrophin-interacting Protein 4 and Mediates Endosomal Sorting of the Chemokine Receptor CXCR4. J. Biol. Chem. 282 (2007) 36971-36979
    • (2007) J. Biol. Chem. , vol.282 , pp. 36971-36979
    • Bhandari, D.1    Trejo, J.2    Benovic, J.L.3    Marchese, A.4
  • 3
    • 33748751670 scopus 로고    scopus 로고
    • Trafficking of G. protein-coupled receptors
    • Drake M.T., Shenoy S.K., and Lefkowitz R.J. Trafficking of G. protein-coupled receptors. Circ Res. 99 (2006) 570-582
    • (2006) Circ Res. , vol.99 , pp. 570-582
    • Drake, M.T.1    Shenoy, S.K.2    Lefkowitz, R.J.3
  • 4
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn R., and Hicke L. Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 276 (2001) 25974-25981
    • (2001) J. Biol. Chem. , vol.276 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 5
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of GPCRs by endocytic membrane trafficking and its potential implications
    • Hanyaloglu A.C., and von Zastrow M. Regulation of GPCRs by endocytic membrane trafficking and its potential implications. Annu. Rev. Pharmacol. Toxicol. 48 (2008) 537-568
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    von Zastrow, M.2
  • 7
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse J.M., Scheffner M., Beaudenon S., and Howley P.M. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA 92 (1995) 2563-2567
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 9
    • 1842591240 scopus 로고    scopus 로고
    • The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture
    • Ingham R.J., Gish G., and Pawson T. The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture. Oncogene 23 (2004) 1972-1984
    • (2004) Oncogene , vol.23 , pp. 1972-1984
    • Ingham, R.J.1    Gish, G.2    Pawson, T.3
  • 11
    • 44949231368 scopus 로고    scopus 로고
    • Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling
    • Li W., Bengtson M.H., Ulbrich A., Matsuda A., Reddy V.A., Orth A., Chanda S.K., Batalov S., and Joazeiro C.A. Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling. PLoS ONE 3 (2008) e1487
    • (2008) PLoS ONE , vol.3
    • Li, W.1    Bengtson, M.H.2    Ulbrich, A.3    Matsuda, A.4    Reddy, V.A.5    Orth, A.6    Chanda, S.K.7    Batalov, S.8    Joazeiro, C.A.9
  • 13
    • 0035824563 scopus 로고    scopus 로고
    • Agonist-promoted ubiquitination of the G. protein-coupled receptor CXCR4 mediates lysosomal sorting
    • Marchese A., and Benovic J.L. Agonist-promoted ubiquitination of the G. protein-coupled receptor CXCR4 mediates lysosomal sorting. J. Biol. Chem. 276 (2001) 45509-45512
    • (2001) J. Biol. Chem. , vol.276 , pp. 45509-45512
    • Marchese, A.1    Benovic, J.L.2
  • 14
    • 4043140225 scopus 로고    scopus 로고
    • Ubiquitination of G. protein-coupled receptors
    • Marchese A., and Benovic J.L. Ubiquitination of G. protein-coupled receptors. Methods Mol. Biol. 259 (2004) 299-306
    • (2004) Methods Mol. Biol. , vol.259 , pp. 299-306
    • Marchese, A.1    Benovic, J.L.2
  • 16
    • 0242362743 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G. protein-coupled receptor CXCR4
    • Marchese A., Raiborg C., Santini F., Keen J.H., Stenmark H., and Benovic J.L. The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G. protein-coupled receptor CXCR4. Dev. Cell. 5 (2003) 709-722
    • (2003) Dev. Cell. , vol.5 , pp. 709-722
    • Marchese, A.1    Raiborg, C.2    Santini, F.3    Keen, J.H.4    Stenmark, H.5    Benovic, J.L.6
  • 17
    • 45549098590 scopus 로고    scopus 로고
    • The chemokine receptor CXCR3 is degraded following internalization and is replenished at the cell surface by de novo synthesis of receptor
    • Meiser A., Mueller A., Wise E.L., McDonagh E.M., Petit S.J., Saran N., Clark P.C., Williams T.J., and Pease J.E. The chemokine receptor CXCR3 is degraded following internalization and is replenished at the cell surface by de novo synthesis of receptor. J. Immunol. 180 (2008) 6713-6724
    • (2008) J. Immunol. , vol.180 , pp. 6713-6724
    • Meiser, A.1    Mueller, A.2    Wise, E.L.3    McDonagh, E.M.4    Petit, S.J.5    Saran, N.6    Clark, P.C.7    Williams, T.J.8    Pease, J.E.9
  • 18
    • 33947314576 scopus 로고    scopus 로고
    • Regulation of Receptor Trafficking by GRKs and Arrestins
    • Moore C.A., Milano S.K., and Benovic J.L. Regulation of Receptor Trafficking by GRKs and Arrestins. Annu. Rev. Physiol. 69 (2006) 451-482
    • (2006) Annu. Rev. Physiol. , vol.69 , pp. 451-482
    • Moore, C.A.1    Milano, S.K.2    Benovic, J.L.3
  • 20
    • 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
  • 22
    • 52049117442 scopus 로고    scopus 로고
    • Nedd4 Mediates Agonist-dependent Ubiquitination, Lysosomal Targeting, and Degradation of the {beta}2-Adrenergic Receptor
    • Shenoy S.K., Xiao K., Venkataramanan V., Snyder P.M., Freedman N.J., and Weissman A.M. Nedd4 Mediates Agonist-dependent Ubiquitination, Lysosomal Targeting, and Degradation of the {beta}2-Adrenergic Receptor. J. Biol. Chem. 283 (2008) 22166-22176
    • (2008) J. Biol. Chem. , vol.283 , pp. 22166-22176
    • Shenoy, S.K.1    Xiao, K.2    Venkataramanan, V.3    Snyder, P.M.4    Freedman, N.J.5    Weissman, A.M.6
  • 23
    • 28844472114 scopus 로고    scopus 로고
    • Increased CXCR4-dependent HIV-1 fusion in activated T cells: Role of CD4/CXCR4 association
    • Zaitseva M., Romantseva T., Manischewitz J., Wang J., Goucher D., and Golding H. Increased CXCR4-dependent HIV-1 fusion in activated T cells: Role of CD4/CXCR4 association. J. Leukoc Biol. 78 (2005) 1306-1317
    • (2005) J. Leukoc Biol. , vol.78 , pp. 1306-1317
    • Zaitseva, M.1    Romantseva, T.2    Manischewitz, J.3    Wang, J.4    Goucher, D.5    Golding, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.