메뉴 건너뛰기




Volumn 25, Issue 12, 2015, Pages 1583-1593

Assembly of IFT Trains at the Ciliary Base Depends on IFT74

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDOMONAS REINHARDTII;

EID: 84931562521     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2015.04.060     Document Type: Article
Times cited : (59)

References (41)
  • 1
    • 33847413590 scopus 로고    scopus 로고
    • Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella
    • Y. Hou, H. Qin, J.A. Follit, G.J. Pazour, J.L. Rosenbaum, and G.B. Witman Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella J. Cell Biol. 176 2007 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
  • 3
    • 84921822477 scopus 로고    scopus 로고
    • Tubulin transport by IFT is upregulated during ciliary growth by a cilium-autonomous mechanism
    • J.M. Craft, J.A. Harris, S. Hyman, P. Kner, and K.F. Lechtreck Tubulin transport by IFT is upregulated during ciliary growth by a cilium-autonomous mechanism J. Cell Biol. 208 2015 223 237 10.1083/jcb.201409036
    • (2015) J. Cell Biol. , vol.208 , pp. 223-237
    • Craft, J.M.1    Harris, J.A.2    Hyman, S.3    Kner, P.4    Lechtreck, K.F.5
  • 4
    • 1642382220 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT) cargo: IFT transports flagellar precursors to the tip and turnover products to the cell body
    • H. Qin, D.R. Diener, S. Geimer, D.G. Cole, and J.L. Rosenbaum Intraflagellar transport (IFT) cargo: IFT transports flagellar precursors to the tip and turnover products to the cell body J. Cell Biol. 164 2004 255 266
    • (2004) J. Cell Biol. , vol.164 , pp. 255-266
    • Qin, H.1    Diener, D.R.2    Geimer, S.3    Cole, D.G.4    Rosenbaum, J.L.5
  • 6
    • 23844485210 scopus 로고    scopus 로고
    • Cilia and Hedgehog responsiveness in the mouse
    • D. Huangfu, and K.V. Anderson Cilia and Hedgehog responsiveness in the mouse Proc. Natl. Acad. Sci. USA 102 2005 11325 11330
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11325-11330
    • Huangfu, D.1    Anderson, K.V.2
  • 7
    • 27744484694 scopus 로고    scopus 로고
    • Loss of the retrograde motor for IFT disrupts localization of Smo to cilia and prevents the expression of both activator and repressor functions of Gli
    • S.R. May, A.M. Ashique, M. Karlen, B. Wang, Y. Shen, K. Zarbalis, J. Reiter, J. Ericson, and A.S. Peterson Loss of the retrograde motor for IFT disrupts localization of Smo to cilia and prevents the expression of both activator and repressor functions of Gli Dev. Biol. 287 2005 378 389
    • (2005) Dev. Biol. , vol.287 , pp. 378-389
    • May, S.R.1    Ashique, A.M.2    Karlen, M.3    Wang, B.4    Shen, Y.5    Zarbalis, K.6    Reiter, J.7    Ericson, J.8    Peterson, A.S.9
  • 8
    • 84856343802 scopus 로고    scopus 로고
    • Architecture and function of IFT complex proteins in ciliogenesis
    • M. Taschner, S. Bhogaraju, and E. Lorentzen Architecture and function of IFT complex proteins in ciliogenesis Differentiation 83 2012 S12 S22
    • (2012) Differentiation , vol.83 , pp. S12-S22
    • Taschner, M.1    Bhogaraju, S.2    Lorentzen, E.3
  • 12
    • 84889019584 scopus 로고    scopus 로고
    • Intraflagellar transport complex structure and cargo interactions
    • S. Bhogaraju, B.D. Engel, and E. Lorentzen Intraflagellar transport complex structure and cargo interactions Cilia 2 2013 10
    • (2013) Cilia , vol.2 , pp. 10
    • Bhogaraju, S.1    Engel, B.D.2    Lorentzen, E.3
  • 13
    • 23044441462 scopus 로고    scopus 로고
    • Characterization of the intraflagellar transport complex B core: direct interaction of the IFT81 and IFT74/72 subunits
    • B.F. Lucker, R.H. Behal, H. Qin, L.C. Siron, W.D. Taggart, J.L. Rosenbaum, and D.G. Cole Characterization of the intraflagellar transport complex B core: direct interaction of the IFT81 and IFT74/72 subunits J. Biol. Chem. 280 2005 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
  • 14
    • 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
    • M. Taschner, S. Bhogaraju, M. Vetter, M. Morawetz, and E. Lorentzen Biochemical mapping of interactions within the intraflagellar transport (IFT) B core complex: IFT52 binds directly to four other IFT-B subunits J. Biol. Chem. 286 2011 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
  • 16
    • 65549169874 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT) protein IFT25 is a phosphoprotein component of IFT complex B and physically interacts with IFT27 in Chlamydomonas
    • Z. Wang, Z.C. Fan, S.M. Williamson, and H. Qin Intraflagellar transport (IFT) protein IFT25 is a phosphoprotein component of IFT complex B and physically interacts with IFT27 in Chlamydomonas PLoS ONE 4 2009 e5384
    • (2009) PLoS ONE , vol.4
    • Wang, Z.1    Fan, Z.C.2    Williamson, S.M.3    Qin, H.4
  • 17
    • 0042971367 scopus 로고    scopus 로고
    • Hypoxia regulates assembly of cilia in suppressors of Tetrahymena lacking an intraflagellar transport subunit gene
    • J.M. Brown, N.A. Fine, G. Pandiyan, R. Thazhath, and J. Gaertig Hypoxia regulates assembly of cilia in suppressors of Tetrahymena lacking an intraflagellar transport subunit gene Mol. Biol. Cell 14 2003 3192 3207
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3192-3207
    • Brown, J.M.1    Fine, N.A.2    Pandiyan, G.3    Thazhath, R.4    Gaertig, J.5
  • 19
    • 0014518546 scopus 로고
    • Flagellar elongation and shortening in Chlamydomonas. The use of cycloheximide and colchicine to study the synthesis and assembly of flagellar proteins
    • J.L. Rosenbaum, J.E. Moulder, and D.L. Ringo Flagellar elongation and shortening in Chlamydomonas. The use of cycloheximide and colchicine to study the synthesis and assembly of flagellar proteins J. Cell Biol. 41 1969 600 619
    • (1969) J. Cell Biol. , vol.41 , pp. 600-619
    • Rosenbaum, J.L.1    Moulder, J.E.2    Ringo, D.L.3
  • 20
    • 0033535044 scopus 로고    scopus 로고
    • The DHC1b (DHC2) isoform of cytoplasmic dynein is required for flagellar assembly
    • G.J. Pazour, B.L. Dickert, and G.B. Witman The DHC1b (DHC2) isoform of cytoplasmic dynein is required for flagellar assembly J. Cell Biol. 144 1999 473 481
    • (1999) J. Cell Biol. , vol.144 , pp. 473-481
    • Pazour, G.J.1    Dickert, B.L.2    Witman, G.B.3
  • 21
    • 0031777851 scopus 로고    scopus 로고
    • A dynein light chain is essential for the retrograde particle movement of intraflagellar transport (IFT)
    • G.J. Pazour, C.G. Wilkerson, and G.B. Witman A dynein light chain is essential for the retrograde particle movement of intraflagellar transport (IFT) J. Cell Biol. 141 1998 979 992
    • (1998) J. Cell Biol. , vol.141 , pp. 979-992
    • Pazour, G.J.1    Wilkerson, C.G.2    Witman, G.B.3
  • 22
    • 77954362705 scopus 로고    scopus 로고
    • Direct interactions of intraflagellar transport complex B proteins IFT88, IFT52, and IFT46
    • B.F. Lucker, M.S. Miller, S.A. Dziedzic, P.T. Blackmarr, and D.G. Cole Direct interactions of intraflagellar transport complex B proteins IFT88, IFT52, and IFT46 J. Biol. Chem. 285 2010 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
  • 23
    • 0035899865 scopus 로고    scopus 로고
    • Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles
    • J.A. Deane, D.G. Cole, E.S. Seeley, D.R. Diener, and J.L. Rosenbaum Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles Curr. Biol. 11 2001 1586 1590
    • (2001) Curr. Biol. , vol.11 , pp. 1586-1590
    • Deane, J.A.1    Cole, D.G.2    Seeley, E.S.3    Diener, D.R.4    Rosenbaum, J.L.5
  • 24
    • 84864972532 scopus 로고    scopus 로고
    • Dissecting the sequential assembly and localization of intraflagellar transport particle complex B in Chlamydomonas
    • E.A. Richey, and H. Qin Dissecting the sequential assembly and localization of intraflagellar transport particle complex B in Chlamydomonas PLoS ONE 7 2012 e43118
    • (2012) PLoS ONE , vol.7
    • Richey, E.A.1    Qin, H.2
  • 25
    • 77956388187 scopus 로고    scopus 로고
    • CEP290 tethers flagellar transition zone microtubules to the membrane and regulates flagellar protein content
    • B. Craige, C.C. Tsao, D.R. Diener, Y. Hou, K.F. Lechtreck, J.L. Rosenbaum, and G.B. Witman CEP290 tethers flagellar transition zone microtubules to the membrane and regulates flagellar protein content J. Cell Biol. 190 2010 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
  • 27
    • 79959653860 scopus 로고    scopus 로고
    • A role for the primary cilium in Notch signaling and epidermal differentiation during skin development
    • E.J. Ezratty, N. Stokes, S. Chai, A.S. Shah, S.E. Williams, and E. Fuchs A role for the primary cilium in Notch signaling and epidermal differentiation during skin development Cell 145 2011 1129 1141
    • (2011) Cell , vol.145 , pp. 1129-1141
    • Ezratty, E.J.1    Stokes, N.2    Chai, S.3    Shah, A.S.4    Williams, S.E.5    Fuchs, E.6
  • 28
    • 34249653927 scopus 로고    scopus 로고
    • IFT-81 and IFT-74 are required for intraflagellar transport in C. elegans
    • T. Kobayashi, K. Gengyo-Ando, T. Ishihara, I. Katsura, and S. Mitani IFT-81 and IFT-74 are required for intraflagellar transport in C. elegans Genes Cells 12 2007 593 602
    • (2007) Genes Cells , vol.12 , pp. 593-602
    • Kobayashi, T.1    Gengyo-Ando, K.2    Ishihara, T.3    Katsura, I.4    Mitani, S.5
  • 29
    • 13444250115 scopus 로고    scopus 로고
    • Chlamydomonas IFT172 is encoded by FLA11, interacts with CrEB1, and regulates IFT at the flagellar tip
    • L.B. Pedersen, M.S. Miller, S. Geimer, J.M. Leitch, J.L. Rosenbaum, and D.G. Cole Chlamydomonas IFT172 is encoded by FLA11, interacts with CrEB1, and regulates IFT at the flagellar tip Curr. Biol. 15 2005 262 266
    • (2005) Curr. Biol. , vol.15 , pp. 262-266
    • Pedersen, L.B.1    Miller, M.S.2    Geimer, S.3    Leitch, J.M.4    Rosenbaum, J.L.5    Cole, D.G.6
  • 30
    • 72449151681 scopus 로고    scopus 로고
    • Retrograde intraflagellar transport mutants identify complex A proteins with multiple genetic interactions in Chlamydomonas reinhardtii
    • C. Iomini, L. Li, J.M. Esparza, and S.K. Dutcher Retrograde intraflagellar transport mutants identify complex A proteins with multiple genetic interactions in Chlamydomonas reinhardtii Genetics 183 2009 885 896
    • (2009) Genetics , vol.183 , pp. 885-896
    • Iomini, C.1    Li, L.2    Esparza, J.M.3    Dutcher, S.K.4
  • 31
    • 84881532489 scopus 로고    scopus 로고
    • An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier
    • D.K. Breslow, E.F. Koslover, F. Seydel, A.J. Spakowitz, and M.V. Nachury An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier J. Cell Biol. 203 2013 129 147
    • (2013) J. Cell Biol. , vol.203 , pp. 129-147
    • Breslow, D.K.1    Koslover, E.F.2    Seydel, F.3    Spakowitz, A.J.4    Nachury, M.V.5
  • 32
    • 84897958996 scopus 로고    scopus 로고
    • Getting tubulin to the tip of the cilium: one IFT train, many different tubulin cargo-binding sites?
    • S. Bhogaraju, K. Weber, B.D. Engel, K.F. Lechtreck, and E. Lorentzen Getting tubulin to the tip of the cilium: one IFT train, many different tubulin cargo-binding sites? BioEssays 36 2014 463 467
    • (2014) BioEssays , vol.36 , pp. 463-467
    • Bhogaraju, S.1    Weber, K.2    Engel, B.D.3    Lechtreck, K.F.4    Lorentzen, E.5
  • 33
    • 84859498001 scopus 로고    scopus 로고
    • Subunit interactions and organization of the Chlamydomonas reinhardtii intraflagellar transport complex A proteins
    • R.H. Behal, M.S. Miller, H. Qin, B.F. Lucker, A. Jones, and D.G. Cole Subunit interactions and organization of the Chlamydomonas reinhardtii intraflagellar transport complex A proteins J. Biol. Chem. 287 2012 11689 11703
    • (2012) J. Biol. Chem. , vol.287 , pp. 11689-11703
    • Behal, R.H.1    Miller, M.S.2    Qin, H.3    Lucker, B.F.4    Jones, A.5    Cole, D.G.6
  • 34
    • 84859863721 scopus 로고    scopus 로고
    • Disruption of IFT complex A causes cystic kidneys without mitotic spindle misorientation
    • J.A. Jonassen, J. SanAgustin, S.P. Baker, and G.J. Pazour Disruption of IFT complex A causes cystic kidneys without mitotic spindle misorientation J. Am. Soc. Nephrol. 23 2012 641 651
    • (2012) J. Am. Soc. Nephrol. , vol.23 , pp. 641-651
    • Jonassen, J.A.1    SanAgustin, J.2    Baker, S.P.3    Pazour, G.J.4
  • 35
    • 4644274566 scopus 로고    scopus 로고
    • A dynein light intermediate chain, D1bLIC, is required for retrograde intraflagellar transport
    • Y. Hou, G.J. Pazour, and G.B. Witman A dynein light intermediate chain, D1bLIC, is required for retrograde intraflagellar transport Mol. Biol. Cell 15 2004 4382 4394
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4382-4394
    • Hou, Y.1    Pazour, G.J.2    Witman, G.B.3
  • 36
    • 84913052469 scopus 로고
    • Nutritional studies with Chlamydomonas reinhardi
    • R. Sager, and S. Granick Nutritional studies with Chlamydomonas reinhardi Ann. N Y Acad. Sci. 56 1953 831 838
    • (1953) Ann. N Y Acad. Sci. , vol.56 , pp. 831-838
    • Sager, R.1    Granick, S.2
  • 37
    • 84869145990 scopus 로고    scopus 로고
    • A FAP46 mutant provides new insights into the function and assembly of the C1d complex of the ciliary central apparatus
    • J.M. Brown, C.G. Dipetrillo, E.F. Smith, and G.B. Witman A FAP46 mutant provides new insights into the function and assembly of the C1d complex of the ciliary central apparatus J. Cell Sci. 125 2012 3904 3913
    • (2012) J. Cell Sci. , vol.125 , pp. 3904-3913
    • Brown, J.M.1    Dipetrillo, C.G.2    Smith, E.F.3    Witman, G.B.4
  • 38
    • 0036967786 scopus 로고    scopus 로고
    • An engineered Streptomyces hygroscopicus aph 7" gene mediates dominant resistance against hygromycin B in Chlamydomonas reinhardtii
    • P. Berthold, R. Schmitt, and W. Mages An engineered Streptomyces hygroscopicus aph 7" gene mediates dominant resistance against hygromycin B in Chlamydomonas reinhardtii Protist 153 2002 401 412
    • (2002) Protist , vol.153 , pp. 401-412
    • Berthold, P.1    Schmitt, R.2    Mages, W.3
  • 39
    • 17444404204 scopus 로고    scopus 로고
    • Restriction enzyme site-directed amplification PCR: a tool to identify regions flanking a marker DNA
    • D. González-Ballester, A. de Montaigu, A. Galván, and E. Fernández Restriction enzyme site-directed amplification PCR: a tool to identify regions flanking a marker DNA Anal. Biochem. 340 2005 330 335
    • (2005) Anal. Biochem. , vol.340 , pp. 330-335
    • González-Ballester, D.1    De Montaigu, A.2    Galván, A.3    Fernández, E.4
  • 41
    • 0004183642 scopus 로고    scopus 로고
    • Second Edition Academic Press Burlington
    • E.H. Harris Second Edition The Chlamydomonas Sourcebook Volume 1 and 3 2009 Academic Press Burlington
    • (2009) The Chlamydomonas Sourcebook , vol.1-3
    • Harris, E.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.