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Volumn 361, Issue 1, 2006, Pages 22-32

Structure of the Bet3-Tpc6B Core of TRAPP: Two Tpc6 Paralogs Form Trimeric Complexes with Bet3 and Mum2

Author keywords

Bet3; crystal structure; Tpc6 Trs33; TRAPP; vesicle tethering

Indexed keywords

CARRIER PROTEIN; HETERODIMER; ISOPROTEIN; PROTEIN BET3; PROTEIN MUM2; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 33745907267     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.06.012     Document Type: Article
Times cited : (28)

References (29)
  • 1
    • 0034161259 scopus 로고    scopus 로고
    • TRAPP stably associates with the Golgi and is required for vesicle docking
    • Barrowman J., Sacher M., and Ferro-Novick S. TRAPP stably associates with the Golgi and is required for vesicle docking. EMBO J. 19 (2000) 862-869
    • (2000) EMBO J. , vol.19 , pp. 862-869
    • Barrowman, J.1    Sacher, M.2    Ferro-Novick, S.3
  • 2
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn R., Lang T., and Südhof T.C. Membrane fusion. Cell 112 (2003) 519-533
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Südhof, T.C.3
  • 4
    • 0035139779 scopus 로고    scopus 로고
    • Purification of TRAPP from Saccharomyces cerevisiae and identification of its mammalian counterpart
    • Sacher M., and Ferro-Novick S. Purification of TRAPP from Saccharomyces cerevisiae and identification of its mammalian counterpart. Methods Enzymol. 329 (2001) 234-241
    • (2001) Methods Enzymol. , vol.329 , pp. 234-241
    • Sacher, M.1    Ferro-Novick, S.2
  • 5
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A.-C., Bösche M., Krause R., Grandi P., Marzloch M., Bauer A., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002) 141-147
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.-C.1    Bösche, M.2    Krause, R.3    Grandi, P.4    Marzloch, M.5    Bauer, A.6
  • 6
    • 17244375812 scopus 로고    scopus 로고
    • Mammalian Bet3 functions as a cytosolic factor participating in transport from the ER to the Golgi apparatus
    • Loh E., Peter F., Subramaniam V.N., and Hong W. Mammalian Bet3 functions as a cytosolic factor participating in transport from the ER to the Golgi apparatus. J. Cell Sci. 118 (2005) 1209-1222
    • (2005) J. Cell Sci. , vol.118 , pp. 1209-1222
    • Loh, E.1    Peter, F.2    Subramaniam, V.N.3    Hong, W.4
  • 7
    • 0034597055 scopus 로고    scopus 로고
    • Synbindin, a novel syndecan-2-binding protein in neuronal dendritic spines
    • Ethell I.M., Hagihara K., Miura Y., Irie F., and Yamaguchi Y. Synbindin, a novel syndecan-2-binding protein in neuronal dendritic spines. J. Cell Biol. 151 (2000) 53-67
    • (2000) J. Cell Biol. , vol.151 , pp. 53-67
    • Ethell, I.M.1    Hagihara, K.2    Miura, Y.3    Irie, F.4    Yamaguchi, Y.5
  • 8
    • 25844489089 scopus 로고    scopus 로고
    • Trs85 (Gsg1), a component of the TRAPP complexes, is required for the organization of the preautophagosomal structure during selective autophagy via the Cvt pathway
    • Meiling-Wesse K., Epple U.D., Krick R., Barth H., Appelles A., Voss C., et al. Trs85 (Gsg1), a component of the TRAPP complexes, is required for the organization of the preautophagosomal structure during selective autophagy via the Cvt pathway. J. Biol. Chem. 280 (2005) 33669-33678
    • (2005) J. Biol. Chem. , vol.280 , pp. 33669-33678
    • Meiling-Wesse, K.1    Epple, U.D.2    Krick, R.3    Barth, H.4    Appelles, A.5    Voss, C.6
  • 9
    • 28544431984 scopus 로고    scopus 로고
    • Mutants in trs120 disrupt traffic from the early endosome to the late Golgi
    • Cai H., Zhang Y., Pypaert M., Walker L., and Ferro-Novick S. Mutants in trs120 disrupt traffic from the early endosome to the late Golgi. J. Cell Biol. 171 (2005) 823-833
    • (2005) J. Cell Biol. , vol.171 , pp. 823-833
    • Cai, H.1    Zhang, Y.2    Pypaert, M.3    Walker, L.4    Ferro-Novick, S.5
  • 10
    • 0037147148 scopus 로고    scopus 로고
    • Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda
    • Jang S.B., Kim Y.G., Cho Y.S., Suh P.G., Kim K.H., and Oh B.H. Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda. J. Biol. Chem. 277 (2002) 49863-49869
    • (2002) J. Biol. Chem. , vol.277 , pp. 49863-49869
    • Jang, S.B.1    Kim, Y.G.2    Cho, Y.S.3    Suh, P.G.4    Kim, K.H.5    Oh, B.H.6
  • 11
    • 11444263265 scopus 로고    scopus 로고
    • Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP
    • Kim Y.G., Sohn E.J., Seo J., Lee K.J., Lee H.S., Hwang I., et al. Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP. Nature Struct. Mol. Biol. 12 (2005) 38-45
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 38-45
    • Kim, Y.G.1    Sohn, E.J.2    Seo, J.3    Lee, K.J.4    Lee, H.S.5    Hwang, I.6
  • 12
    • 20144388984 scopus 로고    scopus 로고
    • Structure of palmitoylated BET3: Insights into TRAPP complex assembly and membrane localization
    • Turnbull A.P., Kümmel D., Prinz B., Holz C., Schultchen J., Lang C., et al. Structure of palmitoylated BET3: Insights into TRAPP complex assembly and membrane localization. EMBO J. 24 (2005) 875-884
    • (2005) EMBO J. , vol.24 , pp. 875-884
    • Turnbull, A.P.1    Kümmel, D.2    Prinz, B.3    Holz, C.4    Schultchen, J.5    Lang, C.6
  • 14
    • 27744439889 scopus 로고    scopus 로고
    • Biochemical and crystallographic studies reveal a specific interaction between TRAPP subunits Trs33p and Bet3p
    • Kim M.S., Yi M.J., Lee K.H., Wagner J., Munger C., Kim Y.G., et al. Biochemical and crystallographic studies reveal a specific interaction between TRAPP subunits Trs33p and Bet3p. Traffic 6 (2005) 1183-1195
    • (2005) Traffic , vol.6 , pp. 1183-1195
    • Kim, M.S.1    Yi, M.J.2    Lee, K.H.3    Wagner, J.4    Munger, C.5    Kim, Y.G.6
  • 15
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallog. sect. A 32 (1976) 922-923
    • (1976) Acta Crystallog. sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 16
    • 33748761481 scopus 로고    scopus 로고
    • Detection of protein assemblies in crystals
    • Berthold M.R., et al. (Ed), Springer-Verlag, Berlin Heidelberg, Germany
    • Krissinel E., and Henrick K. Detection of protein assemblies in crystals. In: Berthold M.R., et al. (Ed). CompLife 2005 (2005), Springer-Verlag, Berlin Heidelberg, Germany
    • (2005) CompLife 2005
    • Krissinel, E.1    Henrick, K.2
  • 17
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 19
    • 0142102533 scopus 로고    scopus 로고
    • Membrane traffic fuses with cartilage development
    • Sacher M. Membrane traffic fuses with cartilage development. FEBS Letters 550 (2003) 1-4
    • (2003) FEBS Letters , vol.550 , pp. 1-4
    • Sacher, M.1
  • 20
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange™ site-directed mutagenesis
    • Wang W., and Malcolm B.A. Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange™ site-directed mutagenesis. BioTechniques 26 (1999) 680-682
    • (1999) BioTechniques , vol.26 , pp. 680-682
    • Wang, W.1    Malcolm, B.A.2
  • 21
    • 0037349370 scopus 로고    scopus 로고
    • Facilities and methods for the high-throughput crystal structure analysis of human proteins
    • Heinemann U., Büssow K., Mueller U., and Umbach P. Facilities and methods for the high-throughput crystal structure analysis of human proteins. Acc. Chem. Res. 36 (2001) 157-163
    • (2001) Acc. Chem. Res. , vol.36 , pp. 157-163
    • Heinemann, U.1    Büssow, K.2    Mueller, U.3    Umbach, P.4
  • 22
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26 (1993) 795-800
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 23
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: An automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 25
    • 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 Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 28
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallor. 26 (1993) 283-291
    • (1993) J. Appl. Crystallor. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.