메뉴 건너뛰기




Volumn 13, Issue 3, 2006, Pages 272-277

Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; HEPATOCYTE GROWTH FACTOR REGULATED TYROSINE KINASE SUBSTRATE PROTEIN; PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 33644787880     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1051     Document Type: Article
Times cited : (149)

References (31)
  • 1
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: A signalling connection
    • Di Fiore, P.P., Polo, S. & Hofmann, K. When ubiquitin meets ubiquitin receptors: a signalling connection. Nat. Rev. Mol. Cell Biol. 4, 491-497 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 2
    • 0141704419 scopus 로고    scopus 로고
    • Non-traditional functions of ubiquitin and ubiquitin-binding proteins
    • Schnell, J.D. & Hicke, L. Non-traditional functions of ubiquitin and ubiquitin-binding proteins. J. Biol. Chem. 278, 35857-35860 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 35857-35860
    • Schnell, J.D.1    Hicke, L.2
  • 3
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation
    • Swanson, K.A., Kang, R.S., Stamenova, S.D., Hicke, L. & Radhakrishnan, I. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J. 22, 4597-4606 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3    Hicke, L.4    Radhakrishnan, I.5
  • 4
    • 0038820381 scopus 로고    scopus 로고
    • Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding
    • Kang, R.S. et al. Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Cell 113, 621-630 (2003).
    • (2003) Cell , vol.113 , pp. 621-630
    • Kang, R.S.1
  • 5
    • 2342522100 scopus 로고    scopus 로고
    • Ubiquitin interactions of NZF zinc fingers
    • Alam, S.L. et al. Ubiquitin interactions of NZF zinc fingers. EMBO J. 23, 1411-1421 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1411-1421
    • Alam, S.L.1
  • 6
    • 17044420416 scopus 로고    scopus 로고
    • Structure of the UBA domain of Dsk2p in complex with ubiquitin: Molecular determinants for ubiquitin recognition
    • Ohno, A. et al. Structure of the UBA domain of Dsk2p in complex with ubiquitin: molecular determinants for ubiquitin recognition. Structure 13, 521-532 (2005).
    • (2005) Structure , vol.13 , pp. 521-532
    • Ohno, A.1
  • 7
    • 3142581995 scopus 로고    scopus 로고
    • Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins
    • Teo, H., Veprintsev, D.B. & Williams, R.L. Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins. J. Biol. Chem. 279, 28689-28696 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 28689-28696
    • Teo, H.1    Veprintsev, D.B.2    Williams, R.L.3
  • 8
    • 1842421429 scopus 로고    scopus 로고
    • Ubiquitin recognition by the human TSG101 protein
    • Sundquist, W.I. et al. Ubiquitin recognition by the human TSG101 protein. Mol. Cell 13, 783-789 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 783-789
    • Sundquist, W.I.1
  • 9
    • 17144417404 scopus 로고    scopus 로고
    • Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
    • Wang, Q., Young, P. & Walters, K.J. Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. J. Mol. Biol. 348, 727-739 (2005).
    • (2005) J. Mol. Biol. , vol.348 , pp. 727-739
    • Wang, Q.1    Young, P.2    Walters, K.J.3
  • 10
    • 0141625301 scopus 로고    scopus 로고
    • Structural determinants for the binding of ubiquitin-like domains to the proteasome
    • Mueller, T.D. & Feigon, J. Structural determinants for the binding of ubiquitin-like domains to the proteasome. EMBO J. 22, 4634-4645 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4634-4645
    • Mueller, T.D.1    Feigon, J.2
  • 11
    • 10744226141 scopus 로고    scopus 로고
    • Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B
    • Fujiwara, K. et al. Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B. J. Biol. Chem. 279, 4760-4767 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 4760-4767
    • Fujiwara, K.1
  • 12
    • 21644473663 scopus 로고    scopus 로고
    • Molecular mechanism of ubiquitin recognition by GGA3 GAT domain
    • Kawasaki, M. et al. Molecular mechanism of ubiquitin recognition by GGA3 GAT domain. Genes Cells 10, 639-654 (2005).
    • (2005) Genes Cells , vol.10 , pp. 639-654
    • Kawasaki, M.1
  • 13
    • 0041706190 scopus 로고    scopus 로고
    • Structure and ubiquitin binding of the ubiquitin-interacting motif
    • Fisher, R.D. et al. Structure and ubiquitin binding of the ubiquitin-interacting motif. J. Biol. Chem. 278, 28976-28984 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 28976-28984
    • Fisher, R.D.1
  • 14
    • 0037005404 scopus 로고    scopus 로고
    • Hrs and endocytic sorting of ubiquitinated membrane proteins
    • Raiborg, C. & Stenmark, H. Hrs and endocytic sorting of ubiquitinated membrane proteins. Cell Struct. Funct. 27, 403-408 (2002).
    • (2002) Cell Struct. Funct. , vol.27 , pp. 403-408
    • Raiborg, C.1    Stenmark, H.2
  • 16
    • 0036094538 scopus 로고    scopus 로고
    • Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes
    • Raiborg, C. et al. Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nat. Cell Biol. 4, 394-398 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 394-398
    • Raiborg, C.1
  • 17
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih, S.C. et al. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4, 389-393 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1
  • 18
    • 0038820382 scopus 로고    scopus 로고
    • Mechanism of ubiquitin recognition by the CUE domain of Vps9p
    • Prag, G. et al. Mechanism of ubiquitin recognition by the CUE domain of Vps9p. Cell 113, 609-620 (2003).
    • (2003) Cell , vol.113 , pp. 609-620
    • Prag, G.1
  • 19
    • 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
  • 20
    • 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
  • 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
    • 18244372679 scopus 로고    scopus 로고
    • Ubiquitin-interacting motifs of Epsin are involved in the regulation of insulin-dependent endocytosis
    • Sugiyama, S., Kishida, S., Chayama, K., Koyama, S. & Kikuchi, A. Ubiquitin-interacting motifs of Epsin are involved in the regulation of insulin-dependent endocytosis. J. Biochem. 137, 355-364 (2005).
    • (2005) J. Biochem. , vol.137 , pp. 355-364
    • Sugiyama, S.1    Kishida, S.2    Chayama, K.3    Koyama, S.4    Kikuchi, A.5
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 25
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography & NMR system: a new software for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 50, 869-873 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 29
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 30
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • Bache, K.G., Raiborg, C., Mehlum, A. & Stenmark, H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278, 12513-12521 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.