메뉴 건너뛰기




Volumn 26, Issue , 2010, Pages 59-87

Trafficking to the ciliary membrane: How to get across the periciliary diffusion barrier?

Author keywords

cilia; flagella; signaling

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 4; MEMBRANE PROTEIN; RAB PROTEIN; RAB11 PROTEIN; RAB8 PROTEIN; UNCLASSIFIED DRUG;

EID: 77953895859     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.042308.113337     Document Type: Review
Times cited : (354)

References (146)
  • 1
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic- mutant Saccharomyces cerevisiae
    • Adams AE, Pringle JR. 1984. Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic- mutant Saccharomyces cerevisiae. J. Cell Biol. 98:934-45
    • (1984) J. Cell Biol. , vol.98 , pp. 934-45
    • Adams, A.E.1    Pringle, J.R.2
  • 3
    • 1342345291 scopus 로고    scopus 로고
    • Vertebrate primary cilia: A sensory part of centrosomal complex in tissue cells,but a "sleeping beauty" in cultured cells?
    • Alieva IB, Vorobjev IA. 2004. Vertebrate primary cilia: a sensory part of centrosomal complex in tissue cells,but a "sleeping beauty" in cultured cells? Cell Biol. Int. 28:139-50
    • (2004) Cell Biol. Int. , vol.28 , pp. 139-50
    • Alieva, I.B.1    Vorobjev, I.A.2
  • 4
    • 0015385636 scopus 로고
    • The three-dimensional structure of the basal body from the rhesus monkey oviduct
    • Anderson RG. 1972. The three-dimensional structure of the basal body from the rhesus monkey oviduct. J. Cell Biol. 54:246-65
    • (1972) J. Cell Biol. , vol.54 , pp. 246-65
    • Anderson, R.G.1
  • 5
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • Ang AL, Taguchi T, Francis S, Fölsch H, Murrells LJ, et al. 2004. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J. Cell Biol. 167:531-43
    • (2004) J. Cell Biol. , vol.167 , pp. 531-43
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Fölsch, H.4    Murrells, L.J.5
  • 6
    • 0020618356 scopus 로고
    • Molecular speciesofphosphatidylcholine, -ethanolamine, -serine, and -inositolin microsomal and photoreceptor membranes of bovine retina
    • Aveldaño MI, BazánNG. 1983. Molecular speciesofphosphatidylcholine, -ethanolamine, -serine, and -inositolin microsomal and photoreceptor membranes of bovine retina. J. Lipid Res. 24:620-27
    • (1983) J. Lipid Res. , vol.24 , pp. 620-27
    • Aveldaño, M.I.1    Bazán, N.G.2
  • 7
    • 2342657884 scopus 로고    scopus 로고
    • Decoding cilia function:defining specialized genes required for compartmentalized cilia biogenesis
    • Avidor-Reiss T, Maer AM, Koundakjian E, Polyanovsky A, Keil T, et al. 2004. Decoding cilia function:defining specialized genes required for compartmentalized cilia biogenesis. Cell 117:527-39
    • (2004) Cell , vol.117 , pp. 527-39
    • Avidor-Reiss, T.1    Maer, A.M.2    Koundakjian, E.3    Polyanovsky, A.4    Keil, T.5
  • 8
    • 75749090851 scopus 로고    scopus 로고
    • Intraflagellar transport: It's not just for cilia anymore
    • Baldari CT, Rosenbaum J. 2010. Intraflagellar transport: It's not just for cilia anymore. Curr. Opin. Cell Biol.22:75-80
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 75-80
    • Baldari, C.T.1    Rosenbaum, J.2
  • 9
    • 56149112941 scopus 로고    scopus 로고
    • The outer segment serves as a default destinationfor the trafficking of membrane proteins in photoreceptors
    • Baker SA, Haeri M, Yoo P, Gospe SM, Skiba NP, et al. 2008. The outer segment serves as a default destinationfor the trafficking of membrane proteins in photoreceptors. J. Cell Biol. 183:485-98
    • (2008) J. Cell Biol. , vol.183 , pp. 485-98
    • Baker, S.A.1    Haeri, M.2    Yoo, P.3    Gospe, S.M.4    Skiba, N.P.5
  • 10
    • 44449106038 scopus 로고    scopus 로고
    • Identification of ciliary localization sequenceswithin the third intracellular loop of G protein-coupled receptors
    • Berbari N, Johnson A, Lewis J, Askwith C, Mykytyn K. 2008a. Identification of ciliary localization sequenceswithin the third intracellular loop of G protein-coupled receptors. Mol. Biol. Cell 19:1540-47
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1540-47
    • Berbari, N.1    Johnson, A.2    Lewis, J.3    Askwith, C.4    Mykytyn, K.5
  • 11
    • 41949116864 scopus 로고    scopus 로고
    • Bardet-Biedl syndrome proteins are required forthe localization of G protein-coupled receptors to primary cilia
    • Berbari N, Lewis J, Bishop G, Askwith C, Mykytyn K. 2008b. Bardet-Biedl syndrome proteins are required forthe localization of G protein-coupled receptors to primary cilia. Proc. Natl. Acad. Sci. USA 105:4242-46
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4242-46
    • Berbari, N.1    Lewis, J.2    Bishop, G.3    Askwith, C.4    Mykytyn, K.5
  • 12
    • 0017664223 scopus 로고
    • Physics of chemoreception
    • Berg HC, Purcell EM. 1977. Physics of chemoreception. Biophys. J. 20:193-219
    • (1977) Biophys. J. , vol.20 , pp. 193-219
    • Berg, H.C.1    Purcell, E.M.2
  • 13
    • 0017693370 scopus 로고
    • Turnover of rod photoreceptor outer segments. II. Membraneaddition and loss in relationship to light
    • Besharse JC, Hollyfield JG, Rayborn ME. 1977. Turnover of rod photoreceptor outer segments. II. Membraneaddition and loss in relationship to light. J. Cell Biol. 75:507-27
    • (1977) J. Cell Biol. , vol.75 , pp. 507-27
    • Besharse, J.C.1    Hollyfield, J.G.2    Rayborn, M.E.3
  • 14
    • 69349094765 scopus 로고    scopus 로고
    • Mutations in INPP5E, encoding inos-itol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies
    • Bielas S, Silhavy J, Brancati F, Kisseleva M, Al-Gazali L, et al. 2009. Mutations in INPP5E, encoding inos-itol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies. Nat. Genet.41:1032-36
    • (2009) Nat. Genet. , vol.41 , pp. 1032-36
    • Bielas, S.1    Silhavy, J.2    Brancati, F.3    Kisseleva, M.4    Al-Gazali, L.5
  • 15
    • 0015102094 scopus 로고
    • The structure, origin, isolation, and composition of the tubular mastigonemes of theOchromonas flagellum
    • Bouck GB. 1971. The structure, origin, isolation, and composition of the tubular mastigonemes of theOchromonas flagellum. J. Cell Biol. 50:362-84
    • (1971) J. Cell Biol. , vol.50 , pp. 362-84
    • Bouck, G.B.1
  • 16
    • 77649143612 scopus 로고    scopus 로고
    • Diffusion of a soluble protein, photoactivatable GFP, through a sensory cilium
    • Calvert PD, Schiesser WE, Pugh EN. 2010. Diffusion of a soluble protein, photoactivatable GFP, through a sensory cilium. J. Gen. Physiol. 135:173-96
    • (2010) J. Gen. Physiol. , vol.135 , pp. 173-96
    • Calvert, P.D.1    Schiesser, W.E.2    Pugh, E.N.3
  • 18
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentalization of eukaryotic membranes
    • Caudron F, Barral Y. 2009. Septins and the lateral compartmentalization of eukaryotic membranes. Dev. Cell 16:493-506
    • (2009) Dev. Cell , vol.16 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 19
    • 0036208071 scopus 로고    scopus 로고
    • The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa
    • Cavalier-Smith T. 2002. The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa. Int. J. Syst. Evol. Microbiol. 52:297-354
    • (2002) Int. J. Syst. Evol. Microbiol. , vol.52 , pp. 297-354
    • Cavalier-Smith, T.1
  • 20
    • 0021921133 scopus 로고
    • Detection of plasma membrane cholesterol by filipin during microvil-logenesis and ciliogenesis in quail oviduct
    • Chailley B, Boisvieux-Ulrich E. 1985. Detection of plasma membrane cholesterol by filipin during microvil-logenesis and ciliogenesis in quail oviduct. J. Histochem. Cytochem. 33:1-10
    • (1985) J. Histochem. Cytochem. , vol.33 , pp. 1-10
    • Chailley, B.1    Boisvieux-Ulrich, E.2
  • 21
    • 69249245332 scopus 로고    scopus 로고
    • Cilium-independent regulation of Gli protein function by Sufu in Hedgehog signaling is evolutionarily conserved
    • Chen M-H, Wilson CW, Li Y-J, Law KKL, Lu C-S, et al. 2009. Cilium-independent regulation of Gli protein function by Sufu in Hedgehog signaling is evolutionarily conserved. Genes Dev. 23:1910-28
    • (2009) Genes Dev. , vol.23 , pp. 1910-28
    • Chen, M.-H.1    Wilson, C.W.2    Li, Y.-J.3    Law, K.K.L.4    Lu, C.-S.5
  • 22
    • 54249119254 scopus 로고    scopus 로고
    • Characterization of class i and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1
    • Chun J, Shapovalova Z, Dejgaard SY, Presley JF, Melançon P. 2008. Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1. Mol. Biol. Cell 19:3488-500
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3488-500
    • Chun, J.1    Shapovalova, Z.2    Dejgaard, S.Y.3    Presley, J.F.4    Melançon, P.5
  • 24
    • 0035899865 scopus 로고    scopus 로고
    • Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles
    • Deane JA, Cole DG, Seeley ES, Diener DR, Rosenbaum JL. 2001. Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles. Curr. Biol. 11:1586-90
    • (2001) Curr. Biol. , vol.11 , pp. 1586-90
    • Deane, J.A.1    Cole, D.G.2    Seeley, E.S.3    Diener, D.R.4    Rosenbaum, J.L.5
  • 25
    • 0028817222 scopus 로고
    • Rab8inretinal photoreceptors may participate in rhodopsin transport and in rod outer segment disk morphogenesis
    • DereticD,Huber LA, RansomN,ManciniM,SimonsK,Papermaster DS. 1995. rab8inretinal photoreceptors may participate in rhodopsin transport and in rod outer segment disk morphogenesis. J. Cell Sci. 108: Pt. 1, pp. 215-24
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 1 , pp. 215-24
    • Deretic, D.1    Huber, L.A.2    Ransom, N.3    Mancini, M.4    Simons, K.5    Papermaster, D.S.6
  • 26
    • 0030022944 scopus 로고    scopus 로고
    • Cytoplasmic domain of rhodopsin is essential for post-Golgi vesicle formation in a retinal cell-free system
    • Deretic D, Puleo-Scheppke B, Trippe C. 1996. Cytoplasmic domain of rhodopsin is essential for post-Golgi vesicle formation in a retinal cell-free system. J. Biol. Chem. 271:2279-86
    • (1996) J. Biol. Chem. , vol.271 , pp. 2279-86
    • Deretic, D.1    Puleo-Scheppke, B.2    Trippe, C.3
  • 27
    • 0032168064 scopus 로고    scopus 로고
    • Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA
    • Deretic D, Schmerl S, Hargrave PA, Arendt A, McDowell JH. 1998. Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA. Proc. Natl. Acad. Sci. USA 95:10620-25
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10620-25
    • Deretic, D.1    Schmerl, S.2    Hargrave, P.A.3    Arendt, A.4    McDowell, J.H.5
  • 28
    • 14744272294 scopus 로고    scopus 로고
    • Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4)
    • Deretic D, Williams AH, Ransom N, Morel V, Hargrave PA, et al. 2005. Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4). Proc. Natl. Acad. Sci. USA 102:3301-6
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3301-6
    • Deretic, D.1    Williams, A.H.2    Ransom, N.3    Morel, V.4    Hargrave, P.A.5
  • 29
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G, De Camilli P. 2006. Phosphoinositides in cell regulation and membrane dynamics. Nature 443:651-57
    • (2006) Nature , vol.443 , pp. 651-57
    • Di Paolo, G.1    De Camilli, P.2
  • 30
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin DG, Nelson WJ. 1996. Origins of cell polarity. Cell 84:335-44
    • (1996) Cell , vol.84 , pp. 335-44
    • Drubin, D.G.1    Nelson, W.J.2
  • 31
    • 0035797511 scopus 로고    scopus 로고
    • Polarized dendritic transport and theAP-1 mu1 clathrin adaptor UNC-101 localize odorant receptors to olfactory cilia
    • Dwyer ND, Adler CE, Crump JG, L'Etoile ND, Bargmann CI. 2001. Polarized dendritic transport and theAP-1 mu1 clathrin adaptor UNC-101 localize odorant receptors to olfactory cilia. Neuron 31:277-87
    • (2001) Neuron , vol.31 , pp. 277-87
    • Dwyer, N.D.1    Adler, C.E.2    Crump, J.G.3    L'Etoile, N.D.4    Bargmann, C.I.5
  • 32
    • 66949128729 scopus 로고    scopus 로고
    • Identification of a palmitoylacyl transferase required for protein sorting to the flagellar membrane
    • Emmer BT, Souther C, Toriello KM, Olson CL, Epting CL, Engman DM. 2009. Identification of a palmitoylacyl transferase required for protein sorting to the flagellar membrane. J. Cell Sci. 122:867-74
    • (2009) J. Cell Sci. , vol.122 , pp. 867-74
    • Emmer, B.T.1    Souther, C.2    Toriello, K.M.3    Olson, C.L.4    Epting, C.L.5    Engman, D.M.6
  • 33
    • 70449517408 scopus 로고    scopus 로고
    • Intraflagellar transport is required for polarized recycling of the TCR/CD3 complex to the immune synapse
    • Finetti F, Paccani SR, Riparbelli MG, Giacomello E, Perinetti G, et al. 2009. Intraflagellar transport is required for polarized recycling of the TCR/CD3 complex to the immune synapse. Nat. Cell Biol. 11:1-10
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1-10
    • Finetti, F.1    Paccani, S.R.2    Riparbelli, M.G.3    Giacomello, E.4    Perinetti, G.5
  • 35
    • 75749089291 scopus 로고    scopus 로고
    • The cytoplasmic tail of fibrocystin contains a ciliary target in gsequence
    • Follit JA, Li L, Vucica Y, Pazour GJ. 2010. The cytoplasmic tail of fibrocystin contains a ciliary target in gsequence. J. Cell Biol. 188:21-28
    • (2010) J. Cell Biol. , vol.188 , pp. 21-28
    • Follit, J.A.1    Li, L.2    Vucica, Y.3    Pazour, G.J.4
  • 37
    • 33748327050 scopus 로고    scopus 로고
    • The intraflagellar transport protein IFT20 is associatedwith the Golgi complex and is required for cilia assembly
    • Follit JA, Tuft RA, Fogarty KE, Pazour GJ. 2006. The intraflagellar transport protein IFT20 is associatedwith the Golgi complex and is required for cilia assembly. Mol. Biol. Cell 17:3781-92
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3781-92
    • Follit, J.A.1    Tuft, R.A.2    Fogarty, K.E.3    Pazour, G.J.4
  • 38
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclearpore complexes
    • Frey S, Görlich D. 2007. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclearpore complexes. Cell 130:512-23
    • (2007) Cell , vol.130 , pp. 512-23
    • Frey, S.1    Görlich, D.2
  • 40
    • 33646764178 scopus 로고    scopus 로고
    • Polycystin-2 traffics tocilia independently ofpolycystin-1by using an N-terminal RVxP motif
    • GengL,OkuharaD,Yu Z, TianX,CaiY,etal. 2006. Polycystin-2 traffics tocilia independently ofpolycystin-1by using an N-terminal RVxP motif. J. Cell Sci. 119:1383-95
    • (2006) J. Cell Sci. , vol.119 , pp. 1383-95
    • Geng, L.1    Okuhara, D.2    Yu, Z.3    Tian, X.4    Cai, Y.5
  • 41
    • 0033560770 scopus 로고    scopus 로고
    • Flagellar protein localization mediated by a calcium-myristoyl/ palmitoylswitch mechanism
    • Godsel LM, Engman DM. 1999. Flagellar protein localization mediated by a calcium-myristoyl/palmitoylswitch mechanism. EMBO J. 18:2057-65
    • (1999) EMBO J. , vol.18 , pp. 2057-65
    • Godsel, L.M.1    Engman, D.M.2
  • 42
    • 0024276923 scopus 로고
    • A GTP-binding protein required for secretion rapidlyassociates with secretory vesicles and the plasma membrane in yeast
    • Goud B, Salminen A, Walworth NC, Novick PJ. 1988. A GTP-binding protein required for secretion rapidlyassociates with secretory vesicles and the plasma membrane in yeast. Cell 53:753-68
    • (1988) Cell , vol.53 , pp. 753-68
    • Goud, B.1    Salminen, A.2    Walworth, N.C.3    Novick, P.J.4
  • 43
    • 35548974826 scopus 로고    scopus 로고
    • Cep164, a novel centriole appendageprotein required for primary cilium formation
    • Graser S, Stierhof Y-D, Lavoie SB, Gassner OS, Lamla S, et al. 2007. Cep164, a novel centriole appendageprotein required for primary cilium formation. J. Cell Biol. 179:321-30
    • (2007) J. Cell Biol. , vol.179 , pp. 321-30
    • Graser, S.1    Stierhof, Y.-D.2    Lavoie, S.B.3    Gassner, O.S.4    Lamla, S.5
  • 44
    • 70349651962 scopus 로고    scopus 로고
    • The planar cell polarity effector Fuz is essential for targeted membrane trafficking, ciliogenesis and mouse embryonic development
    • Gray R, Abitua P, Wlodarczyk B, Szabo-Rogers H, Blanchard O, et al. 2009. The planar cell polarity effector Fuz is essential for targeted membrane trafficking, ciliogenesis and mouse embryonic development. Nat. Cell Biol. 11:1225-32
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1225-32
    • Gray, R.1    Abitua, P.2    Wlodarczyk, B.3    Szabo-Rogers, H.4    Blanchard, O.5
  • 45
    • 0036732902 scopus 로고    scopus 로고
    • A Rab8-specific GDP/GTP exchange factor is involvedin actin remodeling and polarized membrane transport
    • Hattula K, Furuhjelm J, Arffman A, Peränen J. 2002. A Rab8-specific GDP/GTP exchange factor is involvedin actin remodeling and polarized membrane transport. Mol. Biol. Cell 13:3268-80
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3268-80
    • Hattula, K.1    Furuhjelm, J.2    Arffman, A.3    Peränen, J.4
  • 47
    • 40749144679 scopus 로고    scopus 로고
    • Gli2 and Gli3 localize to cilia andrequire the intraflagellar transport protein polaris for processing and function
    • Haycraft CJ, Banizs B, Aydin-Son Y, Zhang Q, Michaud EJ, et al. 2005. Gli2 and Gli3 localize to cilia andrequire the intraflagellar transport protein polaris for processing and function. PLoS Genet. 1:e53
    • (2005) PLoS Genet. , vol.1
    • Haycraft, C.J.1    Banizs, B.2    Aydin-Son, Y.3    Zhang, Q.4    Michaud, E.J.5
  • 48
    • 0018827560 scopus 로고
    • Three-dimensional visualization of coated vesicle formation in fibroblasts
    • Heuser J. 1980. Three-dimensional visualization of coated vesicle formation in fibroblasts. J. Cell Biol. 84:560-83
    • (1980) J. Cell Biol. , vol.84 , pp. 560-83
    • Heuser, J.1
  • 49
    • 70949085969 scopus 로고    scopus 로고
    • Planar cell polarity effector gene Fuzzy regulates cilia formation andHedgehog signal transduction in mouse
    • Heydeck W, Zeng H, Liu A. 2009. Planar cell polarity effector gene Fuzzy regulates cilia formation andHedgehog signal transduction in mouse. Dev. Dyn. 238:3035-42
    • (2009) Dev. Dyn. , vol.238 , pp. 3035-42
    • Heydeck, W.1    Zeng, H.2    Liu, A.3
  • 50
    • 33847413590 scopus 로고    scopus 로고
    • Functional analysis of an individual IFTprotein: IFT46 is required for transport of outer dynein arms into flagella
    • Hou Y, Qin H, Follit JA, Pazour GJ, Rosenbaum JL, et al. 2007. Functional analysis of an individual IFTprotein: IFT46 is required for transport of outer dynein arms into flagella. J. Cell Biol. 176:653-65
    • (2007) J. Cell Biol. , vol.176 , pp. 653-65
    • Hou, Y.1    Qin, H.2    Follit, J.A.3    Pazour, G.J.4    Rosenbaum, J.L.5
  • 51
    • 34548515061 scopus 로고    scopus 로고
    • STAM and Hrs down-regulate ciliary TRP receptors
    • Hu J, Wittekind SG, Barr MM. 2007. STAM and Hrs down-regulate ciliary TRP receptors. Mol. Biol. Cell18:3277-89
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3277-89
    • Hu, J.1    Wittekind, S.G.2    Barr, M.M.3
  • 52
    • 69449094091 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is involved in the disassemblyof cilia and flagella
    • Huang K, Diener DR, Rosenbaum JL. 2009. The ubiquitin conjugation system is involved in the disassemblyof cilia and flagella. J. Cell Biol. 186:601-13
    • (2009) J. Cell Biol. , vol.186 , pp. 601-13
    • Huang, K.1    Diener, D.R.2    Rosenbaum, J.L.3
  • 53
    • 0242581681 scopus 로고    scopus 로고
    • Hedgehog signalling in the mouserequires intraflagellar transport proteins
    • Huangfu D, Liu A, Rakeman AS, Murcia NS, Niswander L, et al. 2003. Hedgehog signalling in the mouserequires intraflagellar transport proteins. Nature 426:83-87
    • (2003) Nature , vol.426 , pp. 83-87
    • Huangfu, D.1    Liu, A.2    Rakeman, A.S.3    Murcia, N.S.4    Niswander, L.5
  • 54
    • 0027517448 scopus 로고
    • Rab8, a small GTPase involved in vesiculartraffic between the TGN and the basolateral plasma membrane
    • Huber LA, Pimplikar S, Parton RG, Virta H, Zerial M, et al. 1993. Rab8, a small GTPase involved in vesiculartraffic between the TGN and the basolateral plasma membrane. J. Cell Biol. 123:35-45
    • (1993) J. Cell Biol. , vol.123 , pp. 35-45
    • Huber, L.A.1    Pimplikar, S.2    Parton, R.G.3    Virta, H.4    Zerial, M.5
  • 55
    • 0025013079 scopus 로고
    • Cell body and flagellar agglutinins in Chlamydomonas reinhardtii: The cell body plasma membrane is a reservoir for agglutinins whose migration to the flagella is regulated by a functional barrier
    • Hunnicutt GR, Kosfiszer MG, Snell WJ. 1990. Cell body and flagellar agglutinins in Chlamydomonas reinhardtii: the cell body plasma membrane is a reservoir for agglutinins whose migration to the flagella is regulated by a functional barrier. J. Cell Biol. 111:1605-16
    • (1990) J. Cell Biol. , vol.111 , pp. 1605-16
    • Hunnicutt, G.R.1    Kosfiszer, M.G.2    Snell, W.J.3
  • 56
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane- traffickingnetwork
    • Hurley JH, Emr SD. 2006. The ESCRT complexes: structure and mechanism of a membrane-traffickingnetwork. Annu. Rev. Biophys. Biomol. Struct. 35:277-98
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-98
    • Hurley, J.H.1    Emr, S.D.2
  • 57
    • 57349094868 scopus 로고    scopus 로고
    • Arf GTPase-activating protein ASAP1 interacts withRab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recyclingendosome
    • Inoue H, Ha VL, Prekeris R, Randazzo PA. 2008. Arf GTPase-activating protein ASAP1 interacts withRab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recyclingendosome. Mol. Biol. Cell. 19:4224-37
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 4224-37
    • Inoue, H.1    Ha, V.L.2    Prekeris, R.3    Randazzo, P.A.4
  • 58
    • 0021004872 scopus 로고
    • Lateral diffusion in membranes
    • Jacobson K. 1983. Lateral diffusion in membranes. Cell Motil. 3:367-73
    • (1983) Cell Motil. , vol.3 , pp. 367-73
    • Jacobson, K.1
  • 59
    • 69349095810 scopus 로고    scopus 로고
    • INPP5E mutations cause primary ciliumsignaling defects, ciliary instability and ciliopathies in human and mouse
    • Jacoby M, Cox J, Gayral S, Hampshire D, Ayub M, et al. 2009. INPP5E mutations cause primary ciliumsignaling defects, ciliary instability and ciliopathies in human and mouse. Nat. Genet. 41:1027-31
    • (2009) Nat. Genet. , vol.41 , pp. 1027-31
    • Jacoby, M.1    Cox, J.2    Gayral, S.3    Hampshire, D.4    Ayub, M.5
  • 61
    • 34247385150 scopus 로고    scopus 로고
    • GM1 and GM3 gangliosides highlight distinct lipid microdomains within the apicaldomain of epithelial cells
    • Janich P, Corbeil D. 2007. GM1 and GM3 gangliosides highlight distinct lipid microdomains within the apicaldomain of epithelial cells. FEBS Lett. 581:1783-87
    • (2007) FEBS Lett. , vol.581 , pp. 1783-87
    • Janich, P.1    Corbeil, D.2
  • 62
    • 33744991746 scopus 로고    scopus 로고
    • Ciliary targeting of olfactory CNGchannels requires the CNGB1b subunit and the kinesin-2 motor protein, KIF17
    • Jenkins PM, Hurd TW, Zhang L, McEwen DP, Brown RL, et al. 2006. Ciliary targeting of olfactory CNGchannels requires the CNGB1b subunit and the kinesin-2 motor protein, KIF17. Curr. Biol. 16:1211-16
    • (2006) Curr. Biol. , vol.16 , pp. 1211-16
    • Jenkins, P.M.1    Hurd, T.W.2    Zhang, L.3    McEwen, D.P.4    Brown, R.L.5
  • 63
    • 33644533515 scopus 로고    scopus 로고
    • Evolution of intraflagellar transport from coated vesicles and autogenous origin ofthe eukaryotic cilium
    • Jékely G, Arendt D. 2006. Evolution of intraflagellar transport from coated vesicles and autogenous origin ofthe eukaryotic cilium. BioEssays 28:191-98
    • (2006) BioEssays , vol.28 , pp. 191-98
    • Jékely, G.1    Arendt, D.2
  • 64
    • 77953879123 scopus 로고    scopus 로고
    • The conserved Bardet-Biedl Syndrome proteinsassemble a coat that traffics membrane proteins to cilia
    • Jin H, White SR, Shida T, Schulz S, Aguiar M, et al. 2010. The conserved Bardet-Biedl Syndrome proteinsassemble a coat that traffics membrane proteins to cilia. Cell 141:1208-19
    • (2010) Cell , vol.141 , pp. 1208-19
    • Jin, H.1    White, S.R.2    Shida, T.3    Schulz, S.4    Aguiar, M.5
  • 65
    • 0023446073 scopus 로고
    • Lipids of Paramecium
    • Kaneshiro ES. 1987. Lipids of Paramecium. J. Lipid Res. 28:1241-58
    • (1987) J. Lipid Res. , vol.28 , pp. 1241-58
    • Kaneshiro, E.S.1
  • 67
    • 0021369651 scopus 로고
    • Structural rearrangements of tubulin and actin during the cell cycle of theyeast Saccharomyces
    • Kilmartin JV, Adams AE. 1984. Structural rearrangements of tubulin and actin during the cell cycle of theyeast Saccharomyces. J. Cell Biol. 98:922-33
    • (1984) J. Cell Biol. , vol.98 , pp. 922-33
    • Kilmartin, J.V.1    Adams, A.E.2
  • 68
    • 76049114315 scopus 로고    scopus 로고
    • Gli2 trafficking links Hedgehog-dependent activation of Smoothened inthe primary cilium to transcriptional activation in the nucleus
    • Kim J, Kato M, Beachy PA. 2009. Gli2 trafficking links Hedgehog-dependent activation of Smoothened inthe primary cilium to transcriptional activation in the nucleus. Proc. Natl. Acad. Sci. USA 106:21666-71
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 21666-71
    • Kim, J.1    Kato, M.2    Beachy, P.A.3
  • 69
    • 56049117628 scopus 로고    scopus 로고
    • CEP290 interacts with the centriolar satellite component PCM-1and is required for Rab8 localization to the primary cilium
    • Kim J, Krishnaswami S, Gleeson J. 2008. CEP290 interacts with the centriolar satellite component PCM-1and is required for Rab8 localization to the primary cilium. Hum. Mol. Genet. 17:3796-805
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3796-805
    • Kim, J.1    Krishnaswami, S.2    Gleeson, J.3
  • 70
    • 77951128108 scopus 로고    scopus 로고
    • Functional genomic screen for modulators ofciliogenesis and cilium length
    • Kim J, Lee JE, Heynen S, Suyama E, Ono K, et al. 2010. Functional genomic screen for modulators ofciliogenesis and cilium length. Nature 464:1048-51
    • (2010) Nature , vol.464 , pp. 1048-51
    • Kim, J.1    Lee, J.E.2    Heynen, S.3    Suyama, E.4    Ono, K.5
  • 71
    • 62849099990 scopus 로고    scopus 로고
    • Ankyrin-G promotes cyclic nucleotide-gated channeltransport to rod photoreceptor sensory cilia
    • Kizhatil K, Baker SA, Arshavsky VY, Bennett V. 2009. Ankyrin-G promotes cyclic nucleotide-gated channeltransport to rod photoreceptor sensory cilia. Science 323:1614-17
    • (2009) Science , vol.323 , pp. 1614-17
    • Kizhatil, K.1    Bakeri, S.A.2    Arshavsky, V.Y.3    Bennett, V.4
  • 73
    • 0023266351 scopus 로고
    • The specific direct interaction of helper T cells and antigen-presentingB cells. II. Reorientation of the microtubule organizing center and reorganization of the membrane-associated cytoskeleton inside the bound helper T cells
    • Kupfer A, Swain SL, Singer SJ. 1987. The specific direct interaction of helper T cells and antigen-presentingB cells. II. Reorientation of the microtubule organizing center and reorganization of the membrane-associated cytoskeleton inside the bound helper T cells. J. Exp. Med. 165:1565-80
    • (1987) J. Exp. Med. , vol.165 , pp. 1565-80
    • Kupfer, A.1    Swain, S.L.2    Singer, S.J.3
  • 74
    • 76149101303 scopus 로고    scopus 로고
    • The Chlamy domonas reinhardtii BBS omeis an IFT cargo required for export of specific signaling proteins from flagella
    • Lechtreck KF, Johnson EC, Sakai T, Cochran D, Ballif BA, et al. 2009. The Chlamy domonas reinhardtii BBS omeis an IFT cargo required for export of specific signaling proteins from flagella. J. Cell Biol. 187:1117-32
    • (2009) J. Cell Biol. , vol.187 , pp. 1117-32
    • Lechtreck, K.F.1    Johnson, E.C.2    Sakai, T.3    Cochran, D.4    Ballif, B.A.5
  • 75
    • 0027392157 scopus 로고
    • Unconfined lateral diffusion and an estimateof pericellular matrix viscosity revealed by measuring the mobility of gold-tagged lipids
    • Lee GM, Zhang F, Ishihara A, McNeil CL, Jacobson KA. 1993. Unconfined lateral diffusion and an estimateof pericellular matrix viscosity revealed by measuring the mobility of gold-tagged lipids. J. Cell Biol.120:25-35
    • (1993) J. Cell Biol. , vol.120 , pp. 25-35
    • Lee, G.M.1    Zhang, F.2    Ishihara, A.3    McNeil, C.L.4    Jacobson, K.A.5
  • 76
    • 0030475229 scopus 로고    scopus 로고
    • Transgenic mice carrying the dominant rhodopsin mutationP347S: Evidence for defective vectorial transport of rhodopsin to the outer segments
    • Li T, Snyder WK, Olsson JE, Dryja TP. 1996. Transgenic mice carrying the dominant rhodopsin mutationP347S: evidence for defective vectorial transport of rhodopsin to the outer segments. Proc. Natl. Acad. Sci. USA 93:14176-81
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14176-81
    • Li, T.1    Snyder, W.K.2    Olsson, J.E.3    Dryja, T.P.4
  • 77
    • 0031041168 scopus 로고    scopus 로고
    • Comparative activity of ADP-ribosylation factor family members in the earlysteps of coated vesicle formation on rat liver Golgi membranes
    • Liang JO, Kornfeld S. 1997. Comparative activity of ADP-ribosylation factor family members in the earlysteps of coated vesicle formation on rat liver Golgi membranes. J. Biol. Chem. 272:4141-48
    • (1997) J. Biol. Chem. , vol.272 , pp. 4141-48
    • Liang, J.O.1    Kornfeld, S.2
  • 78
    • 57049171416 scopus 로고    scopus 로고
    • A BBSome subunit links ciliogenesis,microtubule stability, and acetylation
    • Loktev AV, Zhang Q, Beck JS, Searby CC, Scheetz TE, et al. 2008. A BBSome subunit links ciliogenesis,microtubule stability, and acetylation. Dev. Cell 15:854-65
    • (2008) Dev. Cell , vol.15 , pp. 854-65
    • Loktev, A.V.1    Zhang, Q.2    Beck, J.S.3    Searby, C.C.4    Scheetz, T.E.5
  • 79
    • 37549042393 scopus 로고    scopus 로고
    • A novel Usher protein network at thepericiliary reloading point between molecular transport machineries in vertebrate photoreceptor cells
    • Maerker T, van Wijk E, Overlack N, Kersten FF, McGee J, et al. 2008. A novel Usher protein network at thepericiliary reloading point between molecular transport machineries in vertebrate photoreceptor cells. Hum. Mol. Genet. 17:71-86
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 71-86
    • Maerker, T.1    Van Wijk, E.2    Overlack, N.3    Kersten, F.F.4    McGee, J.5
  • 81
    • 39749086896 scopus 로고    scopus 로고
    • Proteomic analysis of a membrane preparation from rat olfactory sensory cilia
    • Mayer U, Ungerer N, Klimmeck D, Warnken U, Schnölzer M, et al. 2008. Proteomic analysis of a membrane preparation from rat olfactory sensory cilia. Chem. Senses 33:145-62
    • (2008) Chem. Senses , vol.33 , pp. 145-62
    • Mayer, U.1    Ungerer, N.2    Klimmeck, D.3    Warnken, U.4    Schnölzer, M.5
  • 82
    • 59649128407 scopus 로고    scopus 로고
    • Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4
    • Mazelova J, Astuto-Gribble L, Inoue H, Tam BM, Schonteich E, et al. 2009a. Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4. EMBO J. 28:183-92
    • (2009) EMBO J. , vol.28 , pp. 183-92
    • Mazelova, J.1    Astuto-Gribble, L.2    Inoue, H.3    Tam, B.M.4    Schonteich, E.5
  • 83
    • 68949189407 scopus 로고    scopus 로고
    • Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments
    • Mazelova J, Ransom N, Astuto-Gribble L, Wilson M, Deretic D. 2009b. Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments. J. Cell Sci. 122:2003-13
    • (2009) J. Cell Sci. , vol.122 , pp. 2003-13
    • Mazelova, J.1    Ransom, N.2    Astuto-Gribble, L.3    Wilson, M.4    Deretic, D.5
  • 84
    • 75549090700 scopus 로고    scopus 로고
    • Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium
    • Milenkovic L, Scott MP, Rohatgi R. 2009. Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium. J. Cell Biol. 187:365-74
    • (2009) J. Cell Biol. , vol.187 , pp. 365-74
    • Milenkovic, L.1    Scott, M.P.2    Rohatgi, R.3
  • 85
    • 0018593969 scopus 로고
    • Inhomogeneous distribution of filipin-sterol complexes in the ciliary membrane of rat tracheal epithelium
    • Montesano R. 1979. Inhomogeneous distribution of filipin-sterol complexes in the ciliary membrane of rat tracheal epithelium. Am. J. Anat. 156:139-45
    • (1979) Am. J. Anat. , vol.156 , pp. 139-45
    • Montesano, R.1
  • 86
    • 0035166819 scopus 로고    scopus 로고
    • Mutant rab8 impairs docking and fusion of rhodopsin-bearing post-Golgi membranes and causes cell death of transgenic Xenopus rods
    • Moritz OL, Tam BM, Hurd LL, Peränen J, Deretic D, et al. 2001. Mutant rab8 impairs docking and fusion of rhodopsin-bearing post-Golgi membranes and causes cell death of transgenic Xenopus rods. Mol. Biol. Cell 12:2341-51
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2341-51
    • Moritz, O.L.1    Tam, B.M.2    Hurd, L.L.3    Peränen, J.4    Deretic, D.5
  • 87
    • 33748579946 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of themembrane skeleton at the plasma membrane interface by electron tomography
    • Morone N, Fujiwara T, Murase K, Kasai RS, Ike H, et al. 2006. Three-dimensional reconstruction of themembrane skeleton at the plasma membrane interface by electron tomography. J. Cell Biol. 174:851-62
    • (2006) J. Cell Biol. , vol.174 , pp. 851-62
    • Morone, N.1    Fujiwara, T.2    Murase, K.3    Kasai, R.S.4    Ike, H.5
  • 88
    • 0028322016 scopus 로고
    • Candidate gene associated with amutation causing recessive polycystic kidney disease in mice
    • Moyer JH, Lee-Tischler MJ, Kwon HY, Schrick JJ, Avner ED, et al. 1994. Candidate gene associated with amutation causing recessive polycystic kidney disease in mice. Science 264:1329-33
    • (1994) Science , vol.264 , pp. 1329-33
    • Moyer, J.H.1    Lee-Tischler, M.J.2    Kwon, H.Y.3    Schrick, J.J.4    Avner, E.D.5
  • 89
    • 0000060880 scopus 로고
    • Evidence for a functional membrane barrierin the transition zone between the flagellum and cell body of Chlamydomonas eugametos gametes
    • Musgrave A, Wildt P, Etten I, Pijst H, Scholma C, et al. 1986. Evidence for a functional membrane barrierin the transition zone between the flagellum and cell body of Chlamydomonas eugametos gametes. Planta167:544-53
    • (1986) Planta , vol.167 , pp. 544-53
    • Musgrave, A.1    Wildt, P.2    Etten, I.3    Pijst, H.4    Scholma, C.5
  • 90
    • 34250012834 scopus 로고    scopus 로고
    • A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis
    • Nachury MV, Loktev AV, Zhang Q, Westlake CJ, Peränen J, et al. 2007. A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis. Cell 129:1201-13
    • (2007) Cell , vol.129 , pp. 1201-13
    • Nachury, M.V.1    Loktev, A.V.2    Zhang, Q.3    Westlake, C.J.4    Peränen, J.5
  • 91
    • 20444383209 scopus 로고    scopus 로고
    • Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions
    • Nair KS, Hanson SM, Mendez A, Gurevich EV, Kennedy MJ, et al. 2005. Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron 46:555-67
    • (2005) Neuron , vol.46 , pp. 555-67
    • Nair, K.S.1    Hanson, S.M.2    Mendez, A.3    Gurevich, E.V.4    Kennedy, M.J.5
  • 92
    • 0038726090 scopus 로고    scopus 로고
    • Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization
    • Nakada C, Ritchie K, Oba Y, Nakamura M, Hotta Y, et al. 2003. Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization. Nat. Cell Biol. 5:626-32
    • (2003) Nat. Cell Biol. , vol.5 , pp. 626-32
    • Nakada, C.1    Ritchie, K.2    Oba, Y.3    Nakamura, M.4    Hotta, Y.5
  • 93
    • 1842813568 scopus 로고    scopus 로고
    • Sequences required for the flagellar targeting of an integral membrane protein
    • Nasser MIA, Landfear SM. 2004. Sequences required for the flagellar targeting of an integral membrane protein. Mol. Biochem. Parasitol. 135:89-100
    • (2004) Mol. Biochem. Parasitol. , vol.135 , pp. 89-100
    • Nasser, M.I.A.1    Landfear, S.M.2
  • 94
    • 0037317302 scopus 로고    scopus 로고
    • Polycystins 1 and 2 mediate mechanosen-sation in the primary cilium of kidney cells
    • Nauli SM, Alenghat FJ, Luo Y, Williams E, Vassilev P, et al. 2003. Polycystins 1 and 2 mediate mechanosen-sation in the primary cilium of kidney cells. Nat. Genet. 33:129-37
    • (2003) Nat. Genet. , vol.33 , pp. 129-37
    • Nauli, S.M.1    Alenghat, F.J.2    Luo, Y.3    Williams, E.4    Vassilev, P.5
  • 95
    • 3843115666 scopus 로고    scopus 로고
    • ReducedGprotein-coupled signaling efficiency in retinal rod outer segments in response to n-3 fatty acid deficiency
    • Niu SL,MitchellDC, Lim SY, Wen ZM, Kim HY,etal. 2004. ReducedGprotein-coupled signaling efficiency in retinal rod outer segments in response to n-3 fatty acid deficiency. J. Biol. Chem. 279:31098-104
    • (2004) J. Biol. Chem. , vol.279 , pp. 31098-104
    • Niu, S.L.1    Mitchell, D.C.2    Lim, S.Y.3    Wen, Z.M.4    Kim, H.Y.5
  • 96
    • 49449086772 scopus 로고    scopus 로고
    • Intraflagellar transport, cilia, and mammalian Hedgehog signaling: Analysis in mouse embryonic fibroblasts
    • Ocbina PJR, Anderson KV. 2008. Intraflagellar transport, cilia, and mammalian Hedgehog signaling: analysis in mouse embryonic fibroblasts. Dev. Dyn. 237:2030-38
    • (2008) Dev. Dyn. , vol.237 , pp. 2030-38
    • Ocbina, P.J.R.1    Anderson, K.V.2
  • 97
    • 43149102968 scopus 로고    scopus 로고
    • Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8
    • Omori Y, Zhao C, Saras A, Mukhopadhyay S, Kim W, et al. 2008. elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8. Nat. Cell Biol. 10:437-44
    • (2008) Nat. Cell Biol. , vol.10 , pp. 437-44
    • Omori, Y.1    Zhao, C.2    Saras, A.3    Mukhopadhyay, S.4    Kim, W.5
  • 98
    • 0021926706 scopus 로고
    • Vesicular transport of newly synthesized opsin from the Golgi apparatus toward the rod outer segment. Ultrastructural immunocytochemical and autoradiographic evidence in Xenopus retinas
    • Papermaster DS, Schneider BG, Besharse JC. 1985. Vesicular transport of newly synthesized opsin from the Golgi apparatus toward the rod outer segment. Ultrastructural immunocytochemical and autoradiographic evidence in Xenopus retinas. Investig. Ophthalmol. Vis. Sci. 26:1386-404
    • (1985) Investig. Ophthalmol. Vis. Sci. , vol.26 , pp. 1386-404
    • Papermaster, D.S.1    Schneider, B.G.2    Besharse, J.C.3
  • 99
    • 46249125254 scopus 로고    scopus 로고
    • Dishevelled controls apical docking and planarpolarization of basal bodies in ciliated epithelial cells
    • Park T, Mitchell B, Abitua P, Kintner C, Wallingford J. 2008. Dishevelled controls apical docking and planarpolarization of basal bodies in ciliated epithelial cells. Nat. Genet. 40:871-79
    • (2008) Nat. Genet. , vol.40 , pp. 871-79
    • Park, T.1    Mitchell, B.2    Abitua, P.3    Kintner, C.4    Wallingford, J.5
  • 100
    • 33644624937 scopus 로고    scopus 로고
    • Ciliogenesis defects in embryos lacking inturned or fuzzy functionare associated with failure of planar cell polarity and Hedgehog signaling
    • Park TJ, Haigo SL, Wallingford JB. 2006. Ciliogenesis defects in embryos lacking inturned or fuzzy functionare associated with failure of planar cell polarity and Hedgehog signaling. Nat. Genet. 38:303-11
    • (2006) Nat. Genet. , vol.38 , pp. 303-11
    • Park, T.J.1    Haigo, S.L.2    Wallingford, J.B.3
  • 101
  • 102
    • 0034735526 scopus 로고    scopus 로고
    • Chlamydomonas IFT88 and its mousehomologue, polycystic kidney disease gene Tg737, are required for assembly of cilia and flagella
    • Pazour GJ, Dickert BL, Vucica Y, Seeley ES, Rosenbaum JL, et al. 2000. Chlamydomonas IFT88 and its mousehomologue, polycystic kidney disease gene Tg737, are required for assembly of cilia and flagella. J. CellBiol. 151:709-18
    • (2000) J. Cell Biol. , vol.151 , pp. 709-18
    • Pazour, G.J.1    Dickert, B.L.2    Vucica, Y.3    Seeley, E.S.4    Rosenbaum, J.L.5
  • 103
    • 0037019017 scopus 로고    scopus 로고
    • Polycystin-2 localizes to kidney ciliaand the ciliary level is elevated in orpk mice with polycystic kidney disease
    • Pazour GJ, San Agustin JT, Follit JA, Rosenbaum JL, Witman GB. 2002. Polycystin-2 localizes to kidney ciliaand the ciliary level is elevated in orpk mice with polycystic kidney disease. Curr. Biol. 12:R378-80
    • (2002) Curr. Biol. , vol.12
    • Pazour, G.J.1    San Agustin, J.T.2    Follit, J.A.3    Rosenbaum, J.L.4    Witman, G.B.5
  • 104
    • 0020678847 scopus 로고
    • Fine structure of a periciliary ridge complex of frog retinal rod cells revealed by ultrahigh resolution scanning electron microscopy
    • Peters KR, Palade GE, Schneider BG, Papermaster DS. 1983. Fine structure of a periciliary ridge complex of frog retinal rod cells revealed by ultrahigh resolution scanning electron microscopy. J. Cell Biol. 96:265-76
    • (1983) J. Cell Biol. , vol.96 , pp. 265-76
    • Peters, K.R.1    Palade, G.E.2    Schneider, B.G.3    Papermaster, D.S.4
  • 105
    • 0016146318 scopus 로고
    • Lateral diffusion of rhodopsin in the photoreceptor membrane
    • Poo M, Cone RA. 1974. Lateral diffusion of rhodopsin in the photoreceptor membrane. Nature 247:438-41
    • (1974) Nature , vol.247 , pp. 438-41
    • Poo, M.1    Cone, R.A.2
  • 106
    • 0021795601 scopus 로고
    • Analysis of the morphology and function of primary cilia inconnective tissues: A cellular cybernetic probe?
    • Poole CA, Flint MH, Beaumont BW. 1985. Analysis of the morphology and function of primary cilia inconnective tissues: a cellular cybernetic probe? Cell Motil. 5:175-93
    • (1985) Cell Motil. , vol.5 , pp. 175-93
    • Poole, C.A.1    Flint, M.H.2    Beaumont, B.W.3
  • 107
    • 24944555725 scopus 로고    scopus 로고
    • Intraflagellar transport is required for thevectorial movement of TRPV channels in the ciliary membrane
    • Qin H, Burnette DT, Bae Y-K, Forscher P, Barr MM, et al. 2005. Intraflagellar transport is required for thevectorial movement of TRPV channels in the ciliary membrane. Curr. Biol. 15:1695-99
    • (2005) Curr. Biol. , vol.15 , pp. 1695-99
    • Qin, H.1    Burnette, D.T.2    Bae, Y.-K.3    Forscher, P.4    Barr, M.M.5
  • 108
    • 1642382220 scopus 로고    scopus 로고
    • Intraflagellar transport (IFT) cargo: IFTtransports flagellar precursors to the tip and turnover products to the cell body
    • Qin H, Diener DR, Geimer S, Cole DG, Rosenbaum JL. 2004. Intraflagellar transport (IFT) cargo: IFTtransports flagellar precursors to the tip and turnover products to the cell body. J. Cell Biol. 164:255-66
    • (2004) J. Cell Biol. , vol.164 , pp. 255-66
    • Qin, H.1    Diener, D.R.2    Geimer, S.3    Cole, D.G.4    Rosenbaum, J.L.5
  • 109
    • 41849134729 scopus 로고    scopus 로고
    • Leptin resistance contributes to obesityand hypertension in mouse models of Bardet-Biedl syndrome
    • Rahmouni K, Fath MA, Seo S, Thedens DR, Berry CJ, et al. 2008. Leptin resistance contributes to obesityand hypertension in mouse models of Bardet-Biedl syndrome. J. Clin. Investig. 118:1458-67
    • (2008) J. Clin. Investig. , vol.118 , pp. 1458-67
    • Rahmouni, K.1    Fath, M.A.2    Seo, S.3    Thedens, D.R.4    Berry, C.J.5
  • 110
    • 0001199903 scopus 로고
    • Olfactory cilia in the frog
    • Reese T. 1965. Olfactory cilia in the frog. J. Cell Biol. 25:209-30
    • (1965) J. Cell Biol. , vol.25 , pp. 209-30
    • Reese, T.1
  • 111
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck K, Görlich D. 2001. Kinetic analysis of translocation through nuclear pore complexes. EMBO J.20:1320-30
    • (2001) EMBO J. , vol.20 , pp. 1320-30
    • Ribbeck, K.1    Görlich, D.2
  • 112
    • 0032368252 scopus 로고    scopus 로고
    • Single-photon detection by rod cells of the retina
    • Rieke F, Baylor DA. 1998. Single-photon detection by rod cells of the retina. Rev. Mod. Phys. 70:1027-36
    • (1998) Rev. Mod. Phys. , vol.70 , pp. 1027-36
    • Rieke, F.1    Baylor, D.A.2
  • 113
    • 71549119821 scopus 로고    scopus 로고
    • Planarian Hh signaling regulates regenerationpolarity and links Hh pathway evolution to cilia
    • Rink JC, Gurley KA, Elliott SA, Sánchez Alvarado A. 2009. Planarian Hh signaling regulates regenerationpolarity and links Hh pathway evolution to cilia. Science 326:1406-10
    • (2009) Science , vol.326 , pp. 1406-10
    • Rink, J.C.1    Gurley, K.A.2    Elliott, S.A.3    Sánchez Alvarado, A.4
  • 114
    • 33947322678 scopus 로고    scopus 로고
    • The intraflagellar transportcomponent IFT88/polaris is a centrosomal protein regulating G1-S transition in non-ciliated cells
    • Robert A, Margall-Ducos G, Guidotti J-E, Brégerie O, Celati C, et al. 2007. The intraflagellar transportcomponent IFT88/polaris is a centrosomal protein regulating G1-S transition in non-ciliated cells. J.Cell Sci. 120:628-37
    • (2007) J.Cell Sci. , vol.120 , pp. 628-37
    • Robert, A.1    Margall-Ducos, G.2    Guidotti, J.-E.3    Brégerie, O.4    Celati, C.5
  • 116
    • 34547110771 scopus 로고    scopus 로고
    • Patched1 regulates hedgehog signaling at the primary cilium
    • Rohatgi R, Milenkovic L, Scott MP. 2007. Patched1 regulates hedgehog signaling at the primary cilium. Science 317:372-76
    • (2007) Science , vol.317 , pp. 372-76
    • Rohatgi, R.1    Milenkovic, L.2    Scott, M.P.3
  • 118
    • 33947384151 scopus 로고    scopus 로고
    • Overview of structure and function of mammalian cilia
    • Satir P, Christensen ST. 2007. Overview of structure and function of mammalian cilia. Annu. Rev. Physiol.69:377-400
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 377-400
    • Satir, P.1    Christensen, S.T.2
  • 120
    • 77950589400 scopus 로고    scopus 로고
    • Intraflagellar transport molecules in ciliary and nonciliary cells of the retina
    • Sedmak T, Wolfrum U. 2010. Intraflagellar transport molecules in ciliary and nonciliary cells of the retina. J. Cell Biol. 189:171-86
    • (2010) J. Cell Biol. , vol.189 , pp. 171-86
    • Sedmak, T.1    Wolfrum, U.2
  • 121
    • 63149175815 scopus 로고    scopus 로고
    • Requirement of Bardet-Biedl syndromeproteins for leptin receptor signaling
    • Seo S, Guo D-F, Bugge K, Morgan DA, Rahmouni K, et al. 2009. Requirement of Bardet-Biedl syndromeproteins for leptin receptor signaling. Hum. Mol. Genet. 18:1323-31
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1323-31
    • Seo, S.1    Guo, D.-F.2    Bugge, K.3    Morgan, D.A.4    Rahmouni, K.5
  • 124
    • 33746891890 scopus 로고    scopus 로고
    • The primary cilium as the cell's antenna: Signaling at a sensory organelle
    • Singla V, Reiter JF. 2006. The primary cilium as the cell's antenna: signaling at a sensory organelle. Science313:629-33
    • (2006) Science , vol.313 , pp. 629-33
    • Singla, V.1    Reiter, J.F.2
  • 125
    • 0001577217 scopus 로고
    • Centrioles and the formation of rudimentary cilia by fibroblasts and smooth muscle cells
    • Sorokin S. 1962. Centrioles and the formation of rudimentary cilia by fibroblasts and smooth muscle cells. J.Cell Biol. 15:363-77
    • (1962) J.Cell Biol. , vol.15 , pp. 363-77
    • Sorokin, S.1
  • 126
    • 0020658553 scopus 로고
    • Freeze-fracture localization of filipin-cholesterol complexes in the plasmamembrane of Trypanosoma cruzi
    • Souto-Padrón T, De Souza W. 1983. Freeze-fracture localization of filipin-cholesterol complexes in the plasmamembrane of Trypanosoma cruzi. J. Parasitol. 69:129-37
    • (1983) J. Parasitol. , vol.69 , pp. 129-37
    • Souto-Padrón, T.1    De Souza, W.2
  • 127
    • 0033574678 scopus 로고    scopus 로고
    • A primer on vesicle budding
    • Springer S, Spang A, Schekman R. 1999. A primer on vesicle budding. Cell 97:145-48
    • (1999) Cell , vol.97 , pp. 145-48
    • Springer, S.1    Spang, A.2    Schekman, R.3
  • 128
    • 0027935666 scopus 로고
    • A rhodopsin gene mutation responsible for autosomaldominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptorouter segment
    • Sung CH, Makino C, Baylor D, Nathans J. 1994. A rhodopsin gene mutation responsible for autosomaldominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptorouter segment. J. Neurosci. 14:5818-33
    • (1994) J. Neurosci. , vol.14 , pp. 5818-33
    • Sung, C.H.1    Makino, C.2    Baylor, D.3    Nathans, J.4
  • 129
    • 0034644626 scopus 로고    scopus 로고
    • Plasma membrane compartmentalization in yeast bymessenger RNA transport and a septin diffusion barrier
    • Takizawa PA, DeRisi JL, Wilhelm JE, Vale RD. 2000. Plasma membrane compartmentalization in yeast bymessenger RNA transport and a septin diffusion barrier. Science 290:341-44
    • (2000) Science , vol.290 , pp. 341-44
    • Takizawa, P.A.1    Derisi, J.L.2    Wilhelm, J.E.3    Vale, R.D.4
  • 130
    • 0034739845 scopus 로고    scopus 로고
    • Identification of an outer segment targeting signalin the COOH terminus of rhodopsin using transgenic Xenopus laevis
    • Tam BM, Moritz OL, Hurd LB, Papermaster DS. 2000. Identification of an outer segment targeting signalin the COOH terminus of rhodopsin using transgenic Xenopus laevis. J. Cell Biol. 151:1369-80
    • (2000) J. Cell Biol. , vol.151 , pp. 1369-80
    • Tam, B.M.1    Moritz, O.L.2    Hurd, L.B.3    Papermaster, D.S.4
  • 131
    • 44449127738 scopus 로고    scopus 로고
    • Endosomal sorting complex required for transport proteins incancer pathogenesis, vesicular transport, and non-endosomal functions
    • Tanaka N, Kyuuma M, Sugamura K. 2008. Endosomal sorting complex required for transport proteins incancer pathogenesis, vesicular transport, and non-endosomal functions. Cancer Sci. 99:1293-303
    • (2008) Cancer Sci. , vol.99 , pp. 1293-303
    • Tanaka, N.1    Kyuuma, M.2    Sugamura, K.3
  • 132
    • 72049130317 scopus 로고    scopus 로고
    • Cystin localizes to primary cilia via membranemicrodomains and a targeting motif
    • Tao B, Bu S, Yang Z, Siroky B, Kappes JC, et al. 2009. Cystin localizes to primary cilia via membranemicrodomains and a targeting motif. J. Am. Soc. Nephrol. 20:2570-80
    • (2009) J. Am. Soc. Nephrol. , vol.20 , pp. 2570-80
    • Tao, B.1    Bu, S.2    Yang, Z.3    Siroky, B.4    Kappes, J.C.5
  • 133
    • 69549085116 scopus 로고    scopus 로고
    • The nonmotile ciliopathies
    • Tobin JL, Beales PL. 2009. The nonmotile ciliopathies. Genet. Med. 11:386-402
    • (2009) Genet. Med. , vol.11 , pp. 386-402
    • Tobin, J.L.1    Beales, P.L.2
  • 134
    • 70349780604 scopus 로고    scopus 로고
    • Clathrin couture: Fashioning distinctive membrane coats at the cell surface
    • Traub LM. 2009. Clathrin couture: fashioning distinctive membrane coats at the cell surface. PLoS Biol.7:e1000192
    • (2009) PLoS Biol. , vol.7
    • Traub, L.M.1
  • 135
    • 48549102438 scopus 로고    scopus 로고
    • CP110 suppresses primary cilia for mation through its interaction with CEP290, a protein deficient in human ciliary disease
    • Tsang WY, Bossard C, Khanna H, Peränen J, Swaroop A, et al. 2008. CP110 suppresses primary cilia for mation through its interaction with CEP290, a protein deficient in human ciliary disease. Dev. Cell 15:187-97
    • (2008) Dev. Cell , vol.15 , pp. 187-97
    • Tsang, W.Y.1    Bossard, C.2    Khanna, H.3    Peränen, J.4    Swaroop, A.5
  • 137
    • 0022516245 scopus 로고
    • The tight junction does not allow lipid molecules to diffuse fromone epithelial cell to the next
    • van Meer G, Gumbiner B, Simons K. 1986. The tight junction does not allow lipid molecules to diffuse fromone epithelial cell to the next. Nature 322:639-41
    • (1986) Nature , vol.322 , pp. 639-41
    • Van Meer, G.1    Gumbiner, B.2    Simons, K.3
  • 138
    • 33845487091 scopus 로고    scopus 로고
    • FAPP2, cilium formation, and compart-mentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells
    • Vieira OV, Gaus K, Verkade P, Fullekrug J, Vaz WLC, et al. 2006. FAPP2, cilium formation, and compart-mentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells. Proc. Natl. Acad. Sci. USA 103:18556-61
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18556-61
    • Vieira, O.V.1    Gaus, K.2    Verkade, P.3    Fullekrug, J.4    Vaz, W.L.C.5
  • 139
    • 26244448510 scopus 로고    scopus 로고
    • Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic
    • Volpicelli-Daley LA, Li Y, Zhang C-J, Kahn RA. 2005. Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic. Mol. Biol. Cell 16:4495-508
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4495-508
    • Volpicelli-Daley, L.A.1    Li, Y.2    Zhang, C.-J.3    Kahn, R.A.4
  • 140
    • 0030930514 scopus 로고    scopus 로고
    • Sec2p mediates nucleotide exchange on Sec4p and isinvolved in polarized delivery of post-Golgi vesicles
    • Walch-Solimena C, Collins RN, Novick PJ. 1997. Sec2p mediates nucleotide exchange on Sec4p and isinvolved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137:1495-509
    • (1997) J. Cell Biol. , vol.137 , pp. 1495-509
    • Walch-Solimena, C.1    Collins, R.N.2    Novick, P.J.3
  • 141
    • 62449174504 scopus 로고    scopus 로고
    • Selective translocation of intracellular Smoothened to theprimary cilium in response to Hedgehog pathway modulation
    • Wang Y, Zhou Z, Walsh C, McMahon A. 2009. Selective translocation of intracellular Smoothened to theprimary cilium in response to Hedgehog pathway modulation. Proc. Natl. Acad. Sci. USA 106:2623-28
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2623-28
    • Wang, Y.1    Zhou, Z.2    Walsh, C.3    McMahon, A.4
  • 142
    • 78149439494 scopus 로고    scopus 로고
    • Building the primary cilium membrane:regulation of GEF trafficking and activity and a Rab11-Rab8 cascade
    • Presented at San Diego. Abstr.
    • Westlake CJ, Wright KJ, Nachury MV, Baye LM, Rahajeng J, et al. 2009. Building the primary cilium membrane:regulation of GEF trafficking and activity and a Rab11-Rab8 cascade. Presented at Am. Soc. Cell Biol. Annu. Meet. 49th, San Diego. Abstr. 34
    • (2009) Am. Soc. Cell Biol. Annu. Meet. 49th , pp. 34
    • Westlake, C.J.1    Wright, K.J.2    Nachury, M.V.3    Baye, L.M.4    Rahajeng, J.5
  • 143
    • 65549170297 scopus 로고    scopus 로고
    • Fused has evolved divergent roles in vertebrate Hedgehog signalling and motile ciliogenesis
    • Wilson C, Nguyen C, Chen M, Yang J, Gacayan R, et al. 2009. Fused has evolved divergent roles in vertebrate Hedgehog signalling and motile ciliogenesis. Nature 459:98-102
    • (2009) Nature , vol.459 , pp. 98-102
    • Wilson, C.1    Nguyen, C.2    Chen, M.3    Yang, J.4    Gacayan, R.5
  • 144
    • 0036785149 scopus 로고    scopus 로고
    • The polycystic kidney disease proteins, polycystin-1,polycystin-2, polaris, and cystin, are co-localized in renal cilia
    • Yoder BK, Hou X, Guay-Woodford LM. 2002. The polycystic kidney disease proteins, polycystin-1,polycystin-2, polaris, and cystin, are co-localized in renal cilia. J. Am. Soc. Nephrol. 13:2508-16
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2508-16
    • Yoder, B.K.1    Hou, X.2    Guay-Woodford, L.M.3
  • 145
    • 34547590810 scopus 로고    scopus 로고
    • Functional dissection of Rab GTPases involvedin primary cilium formation
    • Yoshimura S-I, Egerer J, Fuchs E, Haas AK, Barr FA. 2007. Functional dissection of Rab GTPases involvedin primary cilium formation. J. Cell Biol. 178:363-69
    • (2007) J. Cell Biol. , vol.178 , pp. 363-69
    • Yoshimura, S.-I.1    Egerer, J.2    Fuchs, E.3    Haas, A.K.4    Barr, F.A.5
  • 146
    • 66249115336 scopus 로고    scopus 로고
    • The exocyst protein Sec10 is necessary for primary ciliogenesis andcystogenesis in vitro
    • Zuo X, Guo W, Lipschutz JH. 2009. The exocyst protein Sec10 is necessary for primary ciliogenesis andcystogenesis in vitro. Mol. Biol. Cell 20:2522-29
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2522-29
    • Zuo, X.1    Guo, W.2    Lipschutz, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.