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Volumn 82, Issue 9, 2014, Pages 2282-2287

Crystal structure of a Chlamydomonas reinhardtii flagellar RabGAP TBC-domain at 1.8 Å resolution

Author keywords

Cilium; Flagellum; GTPase; Intraflagellar transport; RabGAP; Tre2 Bub2 Cdc16 domain

Indexed keywords

RAB PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN;

EID: 84906316846     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24597     Document Type: Article
Times cited : (3)

References (36)
  • 1
    • 79953032655 scopus 로고    scopus 로고
    • Ciliogenesis: building the cell's antenna
    • Ishikawa H, Marshall WF. Ciliogenesis: building the cell's antenna. Nat Rev Mol Cell Biol 2011;12:222-234.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 222-234
    • Ishikawa, H.1    Marshall, W.F.2
  • 2
  • 5
    • 84906313385 scopus 로고    scopus 로고
    • An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier
    • Breslow DK, Koslover EF, Seydel F, Spakowitz AJ, Nachury MV. An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier. J Cell Biol 2013;111:807-816.
    • (2013) J Cell Biol , vol.111 , pp. 807-816
    • Breslow, D.K.1    Koslover, E.F.2    Seydel, F.3    Spakowitz, A.J.4    Nachury, M.V.5
  • 6
    • 77956388187 scopus 로고    scopus 로고
    • CEP290 tethers flagellar transition zone microtubules to the membrane and regulates flagellar protein content
    • Craige B, Tsao CC, Diener DR, Hou Y, Lechtreck KF, Rosenbaum JL, Witman GB. CEP290 tethers flagellar transition zone microtubules to the membrane and regulates flagellar protein content. J Cell Biol 2010;190:927-940.
    • (2010) J Cell Biol , vol.190 , pp. 927-940
    • Craige, B.1    Tsao, C.C.2    Diener, D.R.3    Hou, Y.4    Lechtreck, K.F.5    Rosenbaum, J.L.6    Witman, G.B.7
  • 7
    • 84863327175 scopus 로고    scopus 로고
    • The base of the cilium: roles for transition fibres and the transition zone in ciliary formation, maintenance and compartmentalization
    • Reiter JF, Blacque OE, Leroux MR. The base of the cilium: roles for transition fibres and the transition zone in ciliary formation, maintenance and compartmentalization. EMBO Rep 2012;13:608-618
    • (2012) EMBO Rep , vol.13 , pp. 608-618
    • Reiter, J.F.1    Blacque, O.E.2    Leroux, M.R.3
  • 11
    • 38349000827 scopus 로고    scopus 로고
    • Intraflagellar transport motors in cilia: moving along the cell's antenna
    • Scholey JM. Intraflagellar transport motors in cilia: moving along the cell's antenna. J Cell Biol 2008;180:23-29.
    • (2008) J Cell Biol , vol.180 , pp. 23-29
    • Scholey, J.M.1
  • 12
    • 84856343802 scopus 로고    scopus 로고
    • Architecture and function of IFT complex proteins in ciliogenesis
    • Taschner M, Bhogaraju S, Lorentzen E. Architecture and function of IFT complex proteins in ciliogenesis. Differentiation 2012;83:S12-S22.
    • (2012) Differentiation , vol.83
    • Taschner, M.1    Bhogaraju, S.2    Lorentzen, E.3
  • 13
    • 84889019584 scopus 로고    scopus 로고
    • Intraflagellar transport complex structure and cargo interactions
    • Bhogaraju S, Engel BD, Lorentzen E. Intraflagellar transport complex structure and cargo interactions. Cilia 2013;2:10.
    • (2013) Cilia , vol.2 , pp. 10
    • Bhogaraju, S.1    Engel, B.D.2    Lorentzen, E.3
  • 14
    • 0031750484 scopus 로고    scopus 로고
    • Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons
    • Cole DG, Diener DR, Himelblau AL, Beech PL, Fuster JC, Rosenbaum JL. Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons. J Cell Biol 1998;141:993-1008.
    • (1998) J Cell Biol , vol.141 , pp. 993-1008
    • Cole, D.G.1    Diener, D.R.2    Himelblau, A.L.3    Beech, P.L.4    Fuster, J.C.5    Rosenbaum, J.L.6
  • 15
    • 0032517769 scopus 로고    scopus 로고
    • Distinct mutants of retrograde intraflagellar transport (IFT) share similar morphological and molecular defects
    • Piperno G, Siuda E, Henderson S, Segil M, Vaananen H, Sassaroli M. Distinct mutants of retrograde intraflagellar transport (IFT) share similar morphological and molecular defects. J Cell Biol 1998;143:1591-1601.
    • (1998) J Cell Biol , vol.143 , pp. 1591-1601
    • Piperno, G.1    Siuda, E.2    Henderson, S.3    Segil, M.4    Vaananen, H.5    Sassaroli, M.6
  • 16
    • 23044441462 scopus 로고    scopus 로고
    • Characterization of the intraflagellar transport complex B core: direct interaction of the IFT81 and IFT74/72 subunits
    • Lucker BF, Behal RH, Qin H, Siron LC, Taggart WD, Rosenbaum JL, Cole DG. Characterization of the intraflagellar transport complex B core: direct interaction of the IFT81 and IFT74/72 subunits. J Biol Chem 2005;280:27688-27696.
    • (2005) J Biol Chem , vol.280 , pp. 27688-27696
    • Lucker, B.F.1    Behal, R.H.2    Qin, H.3    Siron, L.C.4    Taggart, W.D.5    Rosenbaum, J.L.6    Cole, D.G.7
  • 17
    • 77954362705 scopus 로고    scopus 로고
    • Direct Interactions of Intraflagellar Transport Complex B Proteins IFT88, IFT52, and IFT46
    • Lucker BF, Miller MS, Dziedzic SA, Blackmarr PT, Cole DG. Direct Interactions of Intraflagellar Transport Complex B Proteins IFT88, IFT52, and IFT46. J Biol Chem 2010;285:21508-21518.
    • (2010) J Biol Chem , vol.285 , pp. 21508-21518
    • Lucker, B.F.1    Miller, M.S.2    Dziedzic, S.A.3    Blackmarr, P.T.4    Cole, D.G.5
  • 18
    • 79960674186 scopus 로고    scopus 로고
    • Biochemical mapping of interactions within the intraflagellar transport (IFT) B core complex: IFT52 binds directly to four other IFT-B subunits
    • Taschner M, Bhogaraju S, Vetter M, Morawetz M, Lorentzen E. Biochemical mapping of interactions within the intraflagellar transport (IFT) B core complex: IFT52 binds directly to four other IFT-B subunits. J Biol Chem 2011;286:26344-26352.
    • (2011) J Biol Chem , vol.286 , pp. 26344-26352
    • Taschner, M.1    Bhogaraju, S.2    Vetter, M.3    Morawetz, M.4    Lorentzen, E.5
  • 19
    • 33847413590 scopus 로고    scopus 로고
    • Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella
    • Hou Y, Qin H, Follit JA, Pazour GJ, Rosenbaum JL, Witman GB. Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella. J Cell Biol 2007;176:653-665.
    • (2007) J Cell Biol , vol.176 , pp. 653-665
    • Hou, Y.1    Qin, H.2    Follit, J.A.3    Pazour, G.J.4    Rosenbaum, J.L.5    Witman, G.B.6
  • 20
    • 55949094005 scopus 로고    scopus 로고
    • ODA16 aids axonemal outer row dynein assembly through an interaction with the intraflagellar transport machinery
    • Ahmed NT, Gao C, Lucker BF, Cole DG, Mitchell DR. ODA16 aids axonemal outer row dynein assembly through an interaction with the intraflagellar transport machinery. J Cell Biol 2008;183:313-322.
    • (2008) J Cell Biol , vol.183 , pp. 313-322
    • Ahmed, N.T.1    Gao, C.2    Lucker, B.F.3    Cole, D.G.4    Mitchell, D.R.5
  • 21
    • 84883111223 scopus 로고    scopus 로고
    • Molecular basis of tubulin transport within the cilium by IFT74 and IFT81
    • Bhogaraju S, et al. Molecular basis of tubulin transport within the cilium by IFT74 and IFT81. Science 2013;341:1009-1012.
    • (2013) Science , vol.341 , pp. 1009-1012
    • Bhogaraju, S.1
  • 22
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 2009;10:513-525.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 23
    • 34547590810 scopus 로고    scopus 로고
    • Functional dissection of Rab GTPases involved in primary cilium formation
    • Yoshimura S-I, Egerer J, Fuchs E, Haas AK, Barr FA. Functional dissection of Rab GTPases involved in primary cilium formation. J Cell Biol 2007;178:363-369.
    • (2007) J Cell Biol , vol.178 , pp. 363-369
    • Yoshimura, S.-I.1    Egerer, J.2    Fuchs, E.3    Haas, A.K.4    Barr, F.A.5
  • 24
    • 84890789300 scopus 로고    scopus 로고
    • Molecular complexes that direct rhodopsin transport to primary cilia
    • Wang J, Deretic D. Molecular complexes that direct rhodopsin transport to primary cilia. Prog Retin Eye Res 2013;38:1-19.
    • (2013) Prog Retin Eye Res , vol.38 , pp. 1-19
    • Wang, J.1    Deretic, D.2
  • 25
    • 33846605643 scopus 로고    scopus 로고
    • Intraflagellar transport protein 27 is a small G protein involved in cell-cycle control
    • Qin H, Wang Z, Diener D, Rosenbaum J. Intraflagellar transport protein 27 is a small G protein involved in cell-cycle control. Curr Biol 2007;17:193-202.
    • (2007) Curr Biol , vol.17 , pp. 193-202
    • Qin, H.1    Wang, Z.2    Diener, D.3    Rosenbaum, J.4
  • 26
    • 64049098228 scopus 로고    scopus 로고
    • A novel function for the atypical small G protein Rab-like 5 in the assembly of the trypanosome flagellum
    • Adhiambo C, Blisnick T, Toutirais G, Delannoy E, Bastin P. A novel function for the atypical small G protein Rab-like 5 in the assembly of the trypanosome flagellum. J Cell Sci 2009;122:834-841.
    • (2009) J Cell Sci , vol.122 , pp. 834-841
    • Adhiambo, C.1    Blisnick, T.2    Toutirais, G.3    Delannoy, E.4    Bastin, P.5
  • 27
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR, Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science 2001;294:1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 28
    • 33746356908 scopus 로고    scopus 로고
    • TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
    • Pan X, Eathiraj S, Munson M, Lambright DG. TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. Nature 2006;442:303-306.
    • (2006) Nature , vol.442 , pp. 303-306
    • Pan, X.1    Eathiraj, S.2    Munson, M.3    Lambright, D.G.4
  • 36
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenström P. Dali server: conservation mapping in 3D. Nucleic Acids Res 2010;38:W545-W549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenström, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.