메뉴 건너뛰기




Volumn 12, Issue 6, 2007, Pages 973-986

The Vps27/Hse1 Complex Is a GAT Domain-Based Scaffold for Ubiquitin-Dependent Sorting

Author keywords

CELLBIO; PROTEINS

Indexed keywords

CARRIER PROTEIN; HETEROOLIGOMERIC PROTEIN; MEMBRANE PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VACUOLAR PROTEIN;

EID: 34249674993     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.devcel.2007.04.013     Document Type: Article
Times cited : (63)

References (77)
  • 3
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst M. A protein's final ESCRT. Traffic 6 (2005) 2-9
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 4
    • 0036304360 scopus 로고    scopus 로고
    • The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting
    • Bilodeau P.S., Urbanowski J.L., Winistorfer S.C., and Piper R.C. The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat. Cell Biol. 4 (2002) 534-539
    • (2002) Nat. Cell Biol. , vol.4 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 5
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • Bilodeau P.S., Winistorfer S.C., Kearney W.R., Robertson A.D., and Piper R.C. Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J. Cell Biol. 163 (2003) 237-243
    • (2003) J. Cell Biol. , vol.163 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 6
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: adaptors on the move
    • Bonifacino J.S. The GGA proteins: adaptors on the move. Nat. Rev. Mol. Cell Biol. 5 (2004) 23-32
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 7
    • 0003362844 scopus 로고    scopus 로고
    • Protein labeling and immunoprecipitation
    • Bonifacino J.S., Dasso M., Harford J.B., Lippincott-Schwartz J., and Yamada K.M. (Eds), John Wiley and Sons, Inc., New York
    • Bonifacino J.S., and Dell'Angelica E.C. Protein labeling and immunoprecipitation. In: Bonifacino J.S., Dasso M., Harford J.B., Lippincott-Schwartz J., and Yamada K.M. (Eds). Current Protocols in Cell Biology (1998), John Wiley and Sons, Inc., New York 7.2.1-7.2.14
    • (1998) Current Protocols in Cell Biology
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 8
    • 20544447129 scopus 로고    scopus 로고
    • Protein transport from the late Golgi to the vacuole in the yeast Saccharomyces cerevisiae
    • Bowers K., and Stevens T.H. Protein transport from the late Golgi to the vacuole in the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1744 (2005) 438-454
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 438-454
    • Bowers, K.1    Stevens, T.H.2
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. A 50 (1994) 760-763
    • (1994) Acta Crystallogr. A , vol.50 , pp. 760-763
  • 12
    • 0034794184 scopus 로고    scopus 로고
    • The interface of receptor trafficking and signalling
    • Clague M.J., and Urbe S. The interface of receptor trafficking and signalling. J. Cell Sci. 114 (2001) 3075-3081
    • (2001) J. Cell Sci. , vol.114 , pp. 3075-3081
    • Clague, M.J.1    Urbe, S.2
  • 13
    • 0037343940 scopus 로고    scopus 로고
    • The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs
    • Collins B.M., Watson P.J., and Owen D.J. The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs. Dev. Cell 4 (2003) 321-332
    • (2003) Dev. Cell , vol.4 , pp. 321-332
    • Collins, B.M.1    Watson, P.J.2    Owen, D.J.3
  • 14
  • 15
    • 0345700741 scopus 로고    scopus 로고
    • Computer modeling of the membrane interaction of FYVE domains
    • Diraviyam K., Stahelin R.V., Cho W., and Murray D. Computer modeling of the membrane interaction of FYVE domains. J. Mol. Biol. 328 (2003) 721-736
    • (2003) J. Mol. Biol. , vol.328 , pp. 721-736
    • Diraviyam, K.1    Stahelin, R.V.2    Cho, W.3    Murray, D.4
  • 18
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: a program package for processing and analyzing diffraction data from macromolecules
    • Furey W., and Swaminathan S. PHASES-95: a program package for processing and analyzing diffraction data from macromolecules. Methods Enzymol. 277 (1997) 590-608
    • (1997) Methods Enzymol. , vol.277 , pp. 590-608
    • Furey, W.1    Swaminathan, S.2
  • 19
  • 20
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund K., Di Fiore P.P., and Dikic I. Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 28 (2003) 598-603
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.P.2    Dikic, I.3
  • 21
    • 33646064427 scopus 로고    scopus 로고
    • Structural complexity in ubiquitin recognition
    • Harper J.W., and Schulman B.A. Structural complexity in ubiquitin recognition. Cell 124 (2006) 1133-1136
    • (2006) Cell , vol.124 , pp. 1133-1136
    • Harper, J.W.1    Schulman, B.A.2
  • 23
    • 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
  • 26
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems. Nat. Cell Biol. 2 (2000) E153-E157
    • (2000) Nat. Cell Biol. , vol.2
    • Hochstrasser, M.1
  • 27
    • 0028871926 scopus 로고
    • Dali: a network tool for protein-structure comparison
    • Holm L., and Sander C. Dali: a network tool for protein-structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 28
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: structure and mechanism of a membrane-trafficking network
    • Hurley J.H., and Emr S.D. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 277-298
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 29
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin binding domains
    • Hurley J.H., Lee S., and Prag G. Ubiquitin binding domains. Biochem. J. 399 (2006) 361-372
    • (2006) Biochem. J. , vol.399 , pp. 361-372
    • Hurley, J.H.1    Lee, S.2    Prag, G.3
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
    • 0346850829 scopus 로고    scopus 로고
    • Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain
    • Kaneko T., Kumasaka T., Ganbe T., Sato T., Miyazawa K., Kitamura N., and Tanaka N. Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain. J. Biol. Chem. 278 (2003) 48162-48168
    • (2003) J. Biol. Chem. , vol.278 , pp. 48162-48168
    • Kaneko, T.1    Kumasaka, T.2    Ganbe, T.3    Sato, T.4    Miyazawa, K.5    Kitamura, N.6    Tanaka, N.7
  • 32
    • 0034535340 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
    • Kato M., Miyazawa K., and Kitamura N. A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J. Biol. Chem. 275 (2000) 37481-37487
    • (2000) J. Biol. Chem. , vol.275 , pp. 37481-37487
    • Kato, M.1    Miyazawa, K.2    Kitamura, N.3
  • 33
    • 2642553077 scopus 로고    scopus 로고
    • Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes
    • Katoh Y., Shiba Y., Mitsuhashi H., Yanagida Y., Takatsu H., and Nakayama K. Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes. J. Biol. Chem. 279 (2004) 24435-24443
    • (2004) J. Biol. Chem. , vol.279 , pp. 24435-24443
    • Katoh, Y.1    Shiba, Y.2    Mitsuhashi, H.3    Yanagida, Y.4    Takatsu, H.5    Nakayama, K.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
    • Katzmann D.J., Babst M., and 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
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 36
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • Katzmann D.J., Stefan C.J., Babst M., and Emr S.D. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J. Cell Biol. 162 (2003) 413-423
    • (2003) J. Cell Biol. , vol.162 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 38
    • 17044391532 scopus 로고    scopus 로고
    • The Hrs/STAM complex in the downregulation of receptor tyrosine kinases
    • Komada M., and Kitamura N. The Hrs/STAM complex in the downregulation of receptor tyrosine kinases. J. Biochem. (Tokyo) 137 (2005) 1-8
    • (2005) J. Biochem. (Tokyo) , vol.137 , pp. 1-8
    • Komada, M.1    Kitamura, N.2
  • 39
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: as domains continue to swap
    • Liu Y., and Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci. 11 (2002) 1285-1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 40
    • 0037169336 scopus 로고    scopus 로고
    • Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila
    • Lloyd T.E., Atkinson R., Wu M.N., Zhou Y., Pennetta G., and Bellen H.J. Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila. Cell 108 (2002) 261-269
    • (2002) Cell , vol.108 , pp. 261-269
    • Lloyd, T.E.1    Atkinson, R.2    Wu, M.N.3    Zhou, Y.4    Pennetta, G.5    Bellen, H.J.6
  • 41
    • 0037596749 scopus 로고    scopus 로고
    • TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation
    • Lu Q., Hope L.W.Q., Brasch M., Reinhard C., and Cohen S.N. TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation. Proc. Natl. Acad. Sci. USA 100 (2003) 7626-7631
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7626-7631
    • Lu, Q.1    Hope, L.W.Q.2    Brasch, M.3    Reinhard, C.4    Cohen, S.N.5
  • 42
    • 0034681262 scopus 로고    scopus 로고
    • Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
    • Mao Y.X., Nickitenko A., Duan X.Q., Lloyd T.E., Wu M.N., Bellen H., and Quiocho F.A. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell 100 (2000) 447-456
    • (2000) Cell , vol.100 , pp. 447-456
    • Mao, Y.X.1    Nickitenko, A.2    Duan, X.Q.3    Lloyd, T.E.4    Wu, M.N.5    Bellen, H.6    Quiocho, F.A.7
  • 43
    • 3843118843 scopus 로고    scopus 로고
    • The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites
    • Mattera R., Puertollano R., Smith W.J., and Bonifacino J.S. The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites. J. Biol. Chem. 279 (2004) 31409-31418
    • (2004) J. Biol. Chem. , vol.279 , pp. 31409-31418
    • Mattera, R.1    Puertollano, R.2    Smith, W.J.3    Bonifacino, J.S.4
  • 44
    • 30944464589 scopus 로고    scopus 로고
    • Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery
    • McCullough J., Row P.E., Lorenzo O., Doherty M., Beynon R., Clague M.J., and Urbe S. Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery. Curr. Biol. 16 (2006) 160-165
    • (2006) Curr. Biol. , vol.16 , pp. 160-165
    • McCullough, J.1    Row, P.E.2    Lorenzo, O.3    Doherty, M.4    Beynon, R.5    Clague, M.J.6    Urbe, S.7
  • 45
    • 0033612372 scopus 로고    scopus 로고
    • Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p
    • Misra S., and Hurley J.H. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell 97 (1999) 657-666
    • (1999) Cell , vol.97 , pp. 657-666
    • Misra, S.1    Hurley, J.H.2
  • 46
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable pair term and an unfavorable high packing density term, for simulation and threading
    • Miyazawa K., and Jernigan R.L. Residue-residue potentials with a favorable pair term and an unfavorable high packing density term, for simulation and threading. J. Mol. Biol. 256 (1996) 623-644
    • (1996) J. Mol. Biol. , vol.256 , pp. 623-644
    • Miyazawa, K.1    Jernigan, R.L.2
  • 47
    • 1942488230 scopus 로고    scopus 로고
    • Association with Hrs is required for the early endosomal localization, stability, and function of STAM
    • Mizuno E., Kawahata K., Okamoto A., Kitamura N., and Komada M. Association with Hrs is required for the early endosomal localization, stability, and function of STAM. J. Biochem. (Tokyo) 135 (2004) 385-396
    • (2004) J. Biochem. (Tokyo) , vol.135 , pp. 385-396
    • Mizuno, E.1    Kawahata, K.2    Okamoto, A.3    Kitamura, N.4    Komada, M.5
  • 49
    • 0035170896 scopus 로고    scopus 로고
    • Structural requirements for function of Yeast GGAs in vacuolar protein sorting, α-factor maturation, and interactions with clathrin
    • Mullins C., and Bonifacino J.S. Structural requirements for function of Yeast GGAs in vacuolar protein sorting, α-factor maturation, and interactions with clathrin. Mol. Cell. Biol. 21 (2001) 7981-7994
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7981-7994
    • Mullins, C.1    Bonifacino, J.S.2
  • 50
    • 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
  • 51
    • 0034846497 scopus 로고    scopus 로고
    • Late endosomes: sorting and partitioning in multivesicular bodies
    • Piper R.C., and Luzio J.P. Late endosomes: sorting and partitioning in multivesicular bodies. Traffic 2 (2001) 612-621
    • (2001) Traffic , vol.2 , pp. 612-621
    • Piper, R.C.1    Luzio, J.P.2
  • 52
    • 0028800173 scopus 로고
    • Vps27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper R.C., Cooper A.A., Yang H., and Stevens T.H. Vps27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J. Cell Biol. 131 (1995) 603-617
    • (1995) J. Cell Biol. , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 53
    • 14044278879 scopus 로고    scopus 로고
    • Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, γ-ear-containing, ADP-ribosylation-factor-binding proteins
    • Prag G., Lee S.H., Mattera R., Arighi C.N., Beach B.M., Bonifacino J.S., and Hurley J.H. Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, γ-ear-containing, ADP-ribosylation-factor-binding proteins. Proc. Natl. Acad. Sci. USA 102 (2005) 2334-2339
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2334-2339
    • Prag, G.1    Lee, S.H.2    Mattera, R.3    Arighi, C.N.4    Beach, B.M.5    Bonifacino, J.S.6    Hurley, J.H.7
  • 54
    • 15744404468 scopus 로고    scopus 로고
    • Interactions of Tom1L1 with the multivesicular body sorting machinery
    • Puertollano R. Interactions of Tom1L1 with the multivesicular body sorting machinery. J. Biol. Chem. 280 (2005) 9258-9264
    • (2005) J. Biol. Chem. , vol.280 , pp. 9258-9264
    • Puertollano, R.1
  • 55
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • Puertollano R., and Bonifacino J.S. Interactions of GGA3 with the ubiquitin sorting machinery. Nat. Cell Biol. 6 (2004) 244-251
    • (2004) Nat. Cell Biol. , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 60
    • 33746092492 scopus 로고    scopus 로고
    • Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains
    • Raiborg C., Wesche J., Malerod L., and Stenmark H. Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains. J. Cell Sci. 119 (2006) 2414-2424
    • (2006) J. Cell Sci. , vol.119 , pp. 2414-2424
    • Raiborg, C.1    Wesche, J.2    Malerod, L.3    Stenmark, H.4
  • 61
    • 33846137688 scopus 로고    scopus 로고
    • Hse1, a component of the yeast Hrs-STAM ubiquitin sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies
    • Ren J., Kee Y., Huibergtse J.M., and Piper R.C. Hse1, a component of the yeast Hrs-STAM ubiquitin sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies. Mol. Biol. Cell 18 (2007) 324-335
    • (2007) Mol. Biol. Cell , vol.18 , pp. 324-335
    • Ren, J.1    Kee, Y.2    Huibergtse, J.M.3    Piper, R.C.4
  • 62
    • 0041620432 scopus 로고    scopus 로고
    • The PredictProtein server
    • Rost B., and Liu J.F. The PredictProtein server. Nucleic Acids Res. 31 (2003) 3300-3304
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3300-3304
    • Rost, B.1    Liu, J.F.2
  • 63
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck P. On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal. Biochem. 320 (2003) 104-124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 67
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih S.C., Katzmann D.J., Schnell J.D., Sutanto M., Emr S.D., and Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4 (2002) 389-393
    • (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
  • 69
    • 0037135529 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs
    • Stahelin R.V., Long F., Diraviyam K., Bruzik K.S., Murray D., and Cho W. Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem. 277 (2002) 26379-26388
    • (2002) J. Biol. Chem. , vol.277 , pp. 26379-26388
    • Stahelin, R.V.1    Long, F.2    Diraviyam, K.3    Bruzik, K.S.4    Murray, D.5    Cho, W.6
  • 70
    • 0037446843 scopus 로고    scopus 로고
    • Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor
    • Suer S., Misra S., Saidi L.F., and Hurley J.H. Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor. Proc. Natl. Acad. Sci. USA 100 (2003) 4451-4456
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4451-4456
    • Suer, S.1    Misra, S.2    Saidi, L.F.3    Hurley, J.H.4
  • 71
    • 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., and Radhakrishnan I. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J. 22 (2003) 4597-4606
    • (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
  • 72
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • Tan S. A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli. Protein Expr. Purif. 21 (2001) 224-234
    • (2001) Protein Expr. Purif. , vol.21 , pp. 224-234
    • Tan, S.1
  • 74
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks C.M., and Miller R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32 (1999) 120-124
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 75
    • 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
  • 76
    • 0347362792 scopus 로고    scopus 로고
    • Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin
    • Yamakami M., Yoshimori T., and Yokosawa H. Tom1, a VHS domain-containing protein, interacts with tollip, ubiquitin, and clathrin. J. Biol. Chem. 278 (2003) 52865-52872
    • (2003) J. Biol. Chem. , vol.278 , pp. 52865-52872
    • Yamakami, M.1    Yoshimori, T.2    Yokosawa, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.