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Volumn 12, Issue 7, 2010, Pages 703-710

Ciliary entry of the kinesin-2 motor KIF17 is regulated by importin-Β2 and RanGTP

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; KARYOPHERIN BETA; KARYOPHERIN BETA2; KINESIN 2; PROTEIN KIF17; PROTEIN RANGTP; UNCLASSIFIED DRUG;

EID: 77954244487     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb2073     Document Type: Article
Times cited : (235)

References (44)
  • 1
    • 67649635952 scopus 로고    scopus 로고
    • Intraflagellar transport and the generation of dynamic, structurally and functionally diverse cilia
    • Silverman, M. A. & Leroux, M. R. Intraflagellar transport and the generation of dynamic, structurally and functionally diverse cilia. Trends Cell Biol. 19, 306-316 (2009).
    • (2009) Trends Cell Biol. , vol.19 , pp. 306-316
    • Silverman, M.A.1    Leroux, M.R.2
  • 2
    • 38349000827 scopus 로고    scopus 로고
    • Intraflagellar transport motors in cilia: Moving along the cell's antenna
    • Scholey, J. M. Intraflagellar transport motors in cilia: moving along the cell's antenna. J. Cell Biol. 180, 23-29 (2008).
    • (2008) J. Cell Biol. , vol.180 , pp. 23-29
    • Scholey, J.M.1
  • 4
    • 63049116544 scopus 로고    scopus 로고
    • The vertebrate primary cilium in development, homeostasis, and disease
    • Gerdes, J. M., Davis, E. E. & Katsanis, N. The vertebrate primary cilium in development, homeostasis, and disease. Cell 137, 32-45 (2009).
    • (2009) Cell , vol.137 , pp. 32-45
    • Gerdes, J.M.1    Davis, E.E.2    Katsanis, N.3
  • 5
    • 33947384151 scopus 로고    scopus 로고
    • Overview of structure and function of mammalian cilia
    • Satir, P. & Christensen, S. T. Overview of structure and function of mammalian cilia. Annu. Rev. Physiol. 69, 377-400 (2007).
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 377-400
    • Satir, P.1    Christensen, S.T.2
  • 6
    • 33646164168 scopus 로고    scopus 로고
    • Intraflagellar transport and cilium-based signaling
    • Scholey, J. M. & Anderson, K. V. Intraflagellar transport and cilium-based signaling. Cell 125, 439-442 (2006).
    • (2006) Cell , vol.125 , pp. 439-442
    • Scholey, J.M.1    Anderson, K.V.2
  • 7
    • 69549085116 scopus 로고    scopus 로고
    • The nonmotile ciliopathies
    • Tobin, J. L. & Beales, P. L. The nonmotile ciliopathies. Genet. Med. 11, 386-402 (2009).
    • (2009) Genet. Med. , vol.11 , pp. 386-402
    • Tobin, J.L.1    Beales, P.L.2
  • 8
    • 35448961665 scopus 로고    scopus 로고
    • Mechanisms of disease-when cilia go bad: Cilia defects and ciliopathies
    • Fliegauf, M., Benzing, T. & Omran, H. Mechanisms of disease-when cilia go bad: cilia defects and ciliopathies. Nat. Rev. Mol. Cell Biol. 8, 880-893 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 880-893
    • Fliegauf, M.1    Benzing, T.2    Omran, H.3
  • 10
    • 23144445446 scopus 로고    scopus 로고
    • Functional coordination of intraflagellar transport motors
    • Ou, G. S., Blacque, O. E., Snow, J. J., Leroux, M. R. & Scholey, J. M. Functional coordination of intraflagellar transport motors. Nature 436, 583-587 (2005).
    • (2005) Nature , vol.436 , pp. 583-587
    • Ou, G.S.1    Blacque, O.E.2    Snow, J.J.3    Leroux, M.R.4    Scholey, J.M.5
  • 11
    • 7944222301 scopus 로고    scopus 로고
    • Two anterograde intraflagellar transport motors cooperate to build sensory cilia on C. elegans neurons
    • Snow, J. J. et al. Two anterograde intraflagellar transport motors cooperate to build sensory cilia on C. elegans neurons. Nat. Cell Biol. 6, 1109-1123 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1109-1123
    • Snow, J.J.1
  • 12
    • 40949162296 scopus 로고    scopus 로고
    • The homodimeric kinesin, Kif17, is essential for vertebrate photoreceptor sensory outer segment development
    • Insinna, C., Pathak, N., Perkins, B., Drummond, I. & Besharse, J. C. The homodimeric kinesin, Kif17, is essential for vertebrate photoreceptor sensory outer segment development. Dev. Biol. 316, 160-170 (2008).
    • (2008) Dev. Biol. , vol.316 , pp. 160-170
    • Insinna, C.1    Pathak, N.2    Perkins, B.3    Drummond, I.4    Besharse, J.C.5
  • 13
    • 33744991746 scopus 로고    scopus 로고
    • Ciliary targeting of olfactory CNG channels requires the CNGB1b subunit and the kinesin-2 motor protein KIF17
    • Jenkins, P. M. et al. Ciliary targeting of olfactory CNG channels requires the CNGB1b subunit and the kinesin-2 motor protein, KIF17. Curr. Biol. 16, 1211-1216 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 1211-1216
    • Jenkins, P.M.1
  • 14
    • 70349097740 scopus 로고    scopus 로고
    • Different roles for KIF17 and kinesin II in photoreceptor development and maintenance
    • Insinna, C., Humby, M., Sedmak, T., Wolfrum, U. & Besharse, J. C. Different roles for KIF17 and kinesin II in photoreceptor development and maintenance. Dev. Dynam. 238, 2211-2222 (2009).
    • (2009) Dev. Dynam. , vol.238 , pp. 2211-2222
    • Insinna, C.1    Humby, M.2    Sedmak, T.3    Wolfrum, U.4    Besharse, J.C.5
  • 15
    • 33748335482 scopus 로고    scopus 로고
    • The ciliary proteome database: An integrated community resource for the genetic and functional dissection of cilia
    • Gherman, A., Davis, E. E. & Katsanis, N. The ciliary proteome database: an integrated community resource for the genetic and functional dissection of cilia. Nat. Genet. 38, 961-962 (2006).
    • (2006) Nat. Genet. , vol.38 , pp. 961-962
    • Gherman, A.1    Davis, E.E.2    Katsanis, N.3
  • 16
    • 0015335860 scopus 로고
    • The ciliary necklace. A ciliary membrane specialization
    • Gilula, N. B. & Satir, P. The ciliary necklace. A ciliary membrane specialization. J. Cell Biol. 53, 494-509 (1972).
    • (1972) J. Cell Biol. , vol.53 , pp. 494-509
    • Gilula, N.B.1    Satir, P.2
  • 17
    • 38749125109 scopus 로고    scopus 로고
    • Spatial distribution of intraflagellar transport proteins in vertebrate photoreceptors
    • Luby-Phelps, K., Fogerty, J., Baker, S. A., Pazour, G. J. & Besharse, J. C. Spatial distribution of intraflagellar transport proteins in vertebrate photoreceptors. Vision Res. 48, 413-423 (2008).
    • (2008) Vision Res. , vol.48 , pp. 413-423
    • Luby-Phelps, K.1    Fogerty, J.2    Baker, S.A.3    Pazour, G.J.4    Besharse, J.C.5
  • 18
    • 0035899865 scopus 로고    scopus 로고
    • Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles
    • Deane, J. A., Cole, D. G., Seeley, E. S., Diener, D. R. & Rosenbaum, J. L. Localization of intraflagellar transport protein IFT52 identifies basal body transitional fibers as the docking site for IFT particles. Curr. Biol. 11, 1586-1590 (2001).
    • (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
  • 19
    • 0033215992 scopus 로고    scopus 로고
    • An olfactory sensory neuron line, Odora, properly targets olfactory proteins and responds to odorants
    • Murrell, J. R. & Hunter, D. D. An olfactory sensory neuron line, Odora, properly targets olfactory proteins and responds to odorants. J. Neurosci. 19, 8260-8270 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 8260-8270
    • Murrell, J.R.1    Hunter, D.D.2
  • 20
    • 33644533515 scopus 로고    scopus 로고
    • Evolution of intraflagellar transport from coated vesicles and autogenous origin of the eukaryotic cilium
    • Jekely, G. & Arendt, D. Evolution of intraflagellar transport from coated vesicles and autogenous origin of the eukaryotic cilium. Bioessays 28, 191-198 (2006).
    • (2006) Bioessays , vol.28 , pp. 191-198
    • Jekely, G.1    Arendt, D.2
  • 21
    • 9444273167 scopus 로고    scopus 로고
    • Components of coated vesicles and nuclear pore complexes share a common molecular architecture
    • Devos, D. et al. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLOS biol. 2, 2085-2093 (2004).
    • (2004) PLOS Biol. , vol.2 , pp. 2085-2093
    • Devos, D.1
  • 22
    • 33846211025 scopus 로고    scopus 로고
    • Sensory cilia and integration of signal transduction in human health and disease
    • Christensen, S. T., Pedersen, L. B., Schneider, L. & Satir, P. Sensory cilia and integration of signal transduction in human health and disease. Traffic 8, 97-109 (2007).
    • (2007) Traffic , vol.8 , pp. 97-109
    • Christensen, S.T.1    Pedersen, L.B.2    Schneider, L.3    Satir, P.4
  • 23
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee, B. J. et al. Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126, 543-558 (2006).
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1
  • 24
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8, 195-208 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 195-208
    • Stewart, M.1
  • 25
    • 34548429735 scopus 로고    scopus 로고
    • The proteome of the mouse photoreceptor sensory cilium complex
    • Liu, Q. et al. The proteome of the mouse photoreceptor sensory cilium complex. Mol. Cell. Proteomics 6, 1299-1317 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1299-1317
    • Liu, Q.1
  • 26
    • 0029026774 scopus 로고
    • The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, Ran-GAP, and HTF9A/RanBP1
    • Richards, S. A., Lounsbury, K. M. & Macara, I. G. The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, Ran-GAP, and HTF9A/RanBP1. J. Biol. Chem. 270, 14405-14411 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14405-14411
    • Richards, S.A.1    Lounsbury, K.M.2    MacAra, I.G.3
  • 27
    • 0030462224 scopus 로고    scopus 로고
    • Mutations within the Ran/TC4 GTPase-Effects on regulatory factor interactions and subcellular localization
    • Lounsbury, K. M., Richards, S. A., Carey, K. L. & Macara, I. G. Mutations within the Ran/TC4 GTPase-Effects on regulatory factor interactions and subcellular localization. J. Biol. Chem. 271, 32834-32841 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 32834-32841
    • Lounsbury, K.M.1    Richards, S.A.2    Carey, K.L.3    MacAra, I.G.4
  • 28
    • 33748195107 scopus 로고    scopus 로고
    • A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules
    • Banaszynski, L. A., Chen, L. C., Maynard-Smith, L. A., Ooi, A. G.L. & Wandless, T. J. A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell 126, 995-1004 (2006).
    • (2006) Cell , vol.126 , pp. 995-1004
    • Banaszynski, L.A.1    Chen, L.C.2    Maynard-Smith, L.A.3    Ooi, A.G.L.4    Wandless, T.J.5
  • 29
    • 34548297903 scopus 로고    scopus 로고
    • A directed approach for engineering conditional protein stability using biologically silent small molecules
    • Maynard-Smith, L. A., Chen, L. C., Banaszynski, L. A., Ooi, A. G.L. & Wandless, T. J. A directed approach for engineering conditional protein stability using biologically silent small molecules. J. Biol. Chem. 282, 24866-24872 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 24866-24872
    • Maynard-Smith, L.A.1    Chen, L.C.2    Banaszynski, L.A.3    Ooi, A.G.L.4    Wandless, T.J.5
  • 30
    • 58849085972 scopus 로고    scopus 로고
    • Conditional fast expression and function of multimeric TRPV5 channels using Shield-1
    • Schoeber, J. P. H. et al. Conditional fast expression and function of multimeric TRPV5 channels using Shield-1. Am. J. Physiol. Renal Physiol. 296, F204-F211 (2009).
    • (2009) Am. J. Physiol. Renal Physiol. , vol.296
    • Schoeber, J.P.H.1
  • 31
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • Weis, K. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112, 441-451 (2003).
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 32
    • 34547574593 scopus 로고    scopus 로고
    • A novel Crumbs3 isoform regulates cell division and ciliogenesis via importin beta interactions
    • Fan, S. L. et al. A novel Crumbs3 isoform regulates cell division and ciliogenesis via importin beta interactions. J. Cell Biol. 178, 387-398 (2007).
    • (2007) J. Cell Biol. , vol.178 , pp. 387-398
    • Fan, S.L.1
  • 33
    • 0346099347 scopus 로고    scopus 로고
    • Importin alpha/beta and Ran-GTP regulate XCTK2 microtubule binding through a bipartite nuclear localization signal
    • Ems-McClung, S. C., Zheng, Y. X. & Walczak, C. E. Importin alpha/beta and Ran-GTP regulate XCTK2 microtubule binding through a bipartite nuclear localization signal. Mol. Biol. Cell 15, 46-57 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 46-57
    • Ems-Mcclung, S.C.1    Zheng, Y.X.2    Walczak, C.E.3
  • 34
    • 39049089174 scopus 로고    scopus 로고
    • Importin-beta and the small guanosine triphosphatase Ran mediate chromosome loading of the human chromokinesin Kid
    • Tahara, K. et al. Importin-beta and the small guanosine triphosphatase Ran mediate chromosome loading of the human chromokinesin Kid. J. Cell. Biol. 180, 493-506 (2008).
    • (2008) J. Cell. Biol. , vol.180 , pp. 493-506
    • Tahara, K.1
  • 35
    • 59649128407 scopus 로고    scopus 로고
    • Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4
    • Mazelova, J. et al. Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4. EMBO J. 28, 183-192 (2009).
    • (2009) EMBO J. , vol.28 , pp. 183-192
    • Mazelova, J.1
  • 36
    • 33646764178 scopus 로고    scopus 로고
    • Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif
    • Geng, L. et al. Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif. J. Cell. Sci. 119, 1383-1395 (2006).
    • (2006) J. Cell. Sci. , vol.119 , pp. 1383-1395
    • Geng, L.1
  • 37
    • 58149485065 scopus 로고    scopus 로고
    • Targeting proteins to the ciliary membrane
    • Pazour, G. J. & Bloodgood, R. A. Targeting proteins to the ciliary membrane. Curr. Top. Dev. Biol. 85, 115-149 (2008).
    • (2008) Curr. Top. Dev. Biol. , vol.85 , pp. 115-149
    • Pazour, G.J.1    Bloodgood, R.A.2
  • 38
    • 0025013079 scopus 로고
    • Cell body and flagellar agglutinins in Chlamydomonas reinhardtii-the cell body plasma-membrane is a reservoir for agglu-tinins whose migration to the flagella is regulated by a functional barrier
    • Hunnicutt, G. R., Kosfiszer, M. G. & Snell, W. J. Cell body and flagellar agglutinins in Chlamydomonas reinhardtii-the cell body plasma-membrane is a reservoir for agglu-tinins whose migration to the flagella is regulated by a functional barrier. J. Cell. Biol. 111, 1605-1616 (1990).
    • (1990) J. Cell. Biol. , vol.111 , pp. 1605-1616
    • Hunnicutt, G.R.1    Kosfiszer, M.G.2    Snell, W.J.3
  • 39
    • 0032951298 scopus 로고    scopus 로고
    • Association of Rab25 and Rab11a with the apical recycling system of polarized Madin-Darby canine kidney cells
    • Casanova, J. E. et al. Association of Rab25 and Rab11a with the apical recycling system of polarized Madin-Darby canine kidney cells. Mol. Biol. Cell 10, 47-61 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 47-61
    • Casanova, J.E.1
  • 40
    • 4444279347 scopus 로고    scopus 로고
    • Redistribution of the kinesin-II subunit KAP from cilia to nuclei during the mitotic and ciliogenic cycles in sea urchin embryos
    • Morris, R. L. et al. Redistribution of the kinesin-II subunit KAP from cilia to nuclei during the mitotic and ciliogenic cycles in sea urchin embryos. Dev. Biol. 274, 56-69 (2004).
    • (2004) Dev. Biol. , vol.274 , pp. 56-69
    • Morris, R.L.1
  • 41
    • 33845993250 scopus 로고    scopus 로고
    • Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells
    • Cai, D. W., Hoppe, A. D., Swanson, J. A. & Verhey, K. J. Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells. J. Cell. Biol. 176, 51-63 (2007).
    • (2007) J. Cell. Biol. , vol.176 , pp. 51-63
    • Cai, D.W.1    Hoppe, A.D.2    Swanson, J.A.3    Verhey, K.J.4
  • 42
    • 39749086896 scopus 로고    scopus 로고
    • Proteomic analysis of a membrane preparation from rat olfactory sensory cilia
    • Mayer, U. et al. Proteomic analysis of a membrane preparation from rat olfactory sensory cilia. Chem. Senses 33, 145-162 (2008).
    • (2008) Chem. Senses , vol.33 , pp. 145-162
    • Mayer, U.1
  • 43
    • 60349100142 scopus 로고    scopus 로고
    • The proteome of rat olfactory sensory cilia
    • Mayer, U. et al. The proteome of rat olfactory sensory cilia. Proteomics 9, 322-334 (2009).
    • (2009) Proteomics , vol.9 , pp. 322-334
    • Mayer, U.1
  • 44
    • 84985204554 scopus 로고
    • Preparation of the mammalian organ of Corti for scanning electron-microscopy
    • Davies, S. & Forge, A. Preparation of the mammalian organ of Corti for scanning electron-microscopy. J. Microsc-Oxford 147, 89-101 (1987).
    • (1987) J. Microsc-Oxford , vol.147 , pp. 89-101
    • Davies, S.1    Forge, A.2


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