메뉴 건너뛰기




Volumn 21, Issue 21, 2012, Pages 4573-4586

The retinitis pigmentosa 28 protein FAM161A is a novel ciliary protein involved in intermolecular protein interaction and microtubule association

Author keywords

[No Author keywords available]

Indexed keywords

NOCODAZOLE;

EID: 84867832407     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds268     Document Type: Article
Times cited : (47)

References (47)
  • 1
    • 78651278414 scopus 로고    scopus 로고
    • Retinitis pigmentosa and allied conditions today: a paradigm of translational research
    • Ayuso, C. and Millan, J.M. (2010) Retinitis pigmentosa and allied conditions today: a paradigm of translational research. Genome Med., 2, 34.
    • (2010) Genome Med. , vol.2 , pp. 34
    • Ayuso, C.1    Millan, J.M.2
  • 2
    • 49449101281 scopus 로고    scopus 로고
    • Intraflagellar transport and the sensory outer segment of vertebrate photoreceptors
    • Insinna, C. and Besharse, J.C. (2008) Intraflagellar transport and the sensory outer segment of vertebrate photoreceptors. Dev. Dyn., 237, 1982-1992.
    • (2008) Dev. Dyn. , vol.237 , pp. 1982-1992
    • Insinna, C.1    Besharse, J.C.2
  • 5
    • 0032830216 scopus 로고    scopus 로고
    • Autosomal recessive retinitis pigmentosa locus RP28 maps between D2S1337 and D2S286 on chromosome 2p11-p15 in an Indian family
    • Gu, S., Kumaramanickavel, G., Srikumari, C.R., Denton, M.J. and Gal, A. (1999) Autosomal recessive retinitis pigmentosa locus RP28 maps between D2S1337 and D2S286 on chromosome 2p11-p15 in an Indian family. J. Med. Genet., 36, 705-707.
    • (1999) J. Med. Genet. , vol.36 , pp. 705-707
    • Gu, S.1    Kumaramanickavel, G.2    Srikumari, C.R.3    Denton, M.J.4    Gal, A.5
  • 12
    • 0025688299 scopus 로고
    • Transmembrane assemblage of the photoreceptor connecting cilium and motile cilium transition zone contain a common immunologic epitope
    • Horst, C.J., Johnson, L.V. and Besharse, J.C. (1990) Transmembrane assemblage of the photoreceptor connecting cilium and motile cilium transition zone contain a common immunologic epitope. Cell Motility and the Cytoskeleton, 17, 329-344.
    • (1990) Cell Motility and the Cytoskeleton , vol.17 , pp. 329-344
    • Horst, C.J.1    Johnson, L.V.2    Besharse, J.C.3
  • 15
    • 0025249256 scopus 로고
    • Microtubule nucleation and organization in teleost photoreceptors: microtubule recovery after elimination by cold
    • Troutt, L.L., Wang, E., Pagh-Roehl, K. and Burnside, B. (1990) Microtubule nucleation and organization in teleost photoreceptors: microtubule recovery after elimination by cold. J. Neurocytol., 19, 213-223.
    • (1990) J. Neurocytol. , vol.19 , pp. 213-223
    • Troutt, L.L.1    Wang, E.2    Pagh-Roehl, K.3    Burnside, B.4
  • 18
    • 77950588006 scopus 로고    scopus 로고
    • Immunoelectron microscopy of vesicle transport to the primary cilium of photoreceptor cells
    • Sedmak, T., Sehn, E. and Wolfrum, U. (2009) Immunoelectron microscopy of vesicle transport to the primary cilium of photoreceptor cells. Methods Cell Biol., 94, 259-272.
    • (2009) Methods Cell Biol. , vol.94 , pp. 259-272
    • Sedmak, T.1    Sehn, E.2    Wolfrum, U.3
  • 19
    • 77950589400 scopus 로고    scopus 로고
    • Intraflagellar transport molecules in ciliary and nonciliary cells of the retina
    • Sedmak, T. and Wolfrum, U. (2010) Intraflagellar transport molecules in ciliary and nonciliary cells of the retina. J. Cell Biol., 189, 171-186.
    • (2010) J. Cell Biol. , vol.189 , pp. 171-186
    • Sedmak, T.1    Wolfrum, U.2
  • 20
    • 0026538817 scopus 로고
    • Gamma-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation
    • Joshi, H.C., Palacios, M.J., McNamara, L. and Cleveland, D.W. (1992) Gamma-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation. Nature, 356, 80-83.
    • (1992) Nature , vol.356 , pp. 80-83
    • Joshi, H.C.1    Palacios, M.J.2    McNamara, L.3    Cleveland, D.W.4
  • 21
    • 33748327050 scopus 로고    scopus 로고
    • The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly
    • Follit, J.A., Tuft, R.A., Fogarty, K.E. and Pazour, G.J. (2006) The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly. Mol. Biol. Cell, 17, 3781-3792.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3781-3792
    • Follit, J.A.1    Tuft, R.A.2    Fogarty, K.E.3    Pazour, G.J.4
  • 22
    • 77952531435 scopus 로고    scopus 로고
    • The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium
    • Evans, R.J., Schwarz, N., Nagel-Wolfrum, K., Wolfrum, U., Hardcastle, A.J. and Cheetham, M.E. (2010) The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium. Hum. Mol. Genet., 19, 1358-1367.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1358-1367
    • Evans, R.J.1    Schwarz, N.2    Nagel-Wolfrum, K.3    Wolfrum, U.4    Hardcastle, A.J.5    Cheetham, M.E.6
  • 23
    • 84859264546 scopus 로고    scopus 로고
    • The ciliary transition zone: from morphology and molecules to medicine
    • Czarnecki, P.G. and Shah, J.V. (2012) The ciliary transition zone: from morphology and molecules to medicine. Trends Cell Biol., 22, 201-210.
    • (2012) Trends Cell Biol. , vol.22 , pp. 201-210
    • Czarnecki, P.G.1    Shah, J.V.2
  • 24
    • 3242749615 scopus 로고    scopus 로고
    • The retinitis pigmentosa 1 protein is a photoreceptor microtubule-associated protein
    • Liu, Q., Zuo, J. and Pierce, E.A. (2004) The retinitis pigmentosa 1 protein is a photoreceptor microtubule-associated protein. J. Neurosci., 24, 6427-6436.
    • (2004) J. Neurosci. , vol.24 , pp. 6427-6436
    • Liu, Q.1    Zuo, J.2    Pierce, E.A.3
  • 27
    • 38349000827 scopus 로고    scopus 로고
    • Intraflagellar transport motors in cilia: moving along the cell's antenna
    • Scholey, J.M. (2008) Intraflagellar transport motors in cilia: moving along the cell's antenna. J. Cell Biol., 180, 23-29.
    • (2008) J. Cell Biol. , vol.180 , pp. 23-29
    • Scholey, J.M.1
  • 28
    • 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. and Besharse, J.C. (2009) Different roles for KIF17 and kinesin II in photoreceptor development and maintenance. Dev. Dyn., 238, 2211-2222.
    • (2009) Dev. Dyn. , vol.238 , pp. 2211-2222
    • Insinna, C.1    Humby, M.2    Sedmak, T.3    Wolfrum, U.4    Besharse, J.C.5
  • 29
    • 33749015997 scopus 로고    scopus 로고
    • Microtubule motors at the intersection of trafficking and transport
    • Caviston, J.P. and Holzbaur, E.L. (2006) Microtubule motors at the intersection of trafficking and transport. Trends Cell Biol., 16, 530-537.
    • (2006) Trends Cell Biol. , vol.16 , pp. 530-537
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 30
    • 0027102583 scopus 로고
    • Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau
    • Takemura, R., Okabe, S., Umeyama, T., Kanai, Y., Cowan, N.J. and Hirokawa, N. (1992) Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau. J. Cell Sci., 103, 953-964.
    • (1992) J. Cell Sci. , vol.103 , pp. 953-964
    • Takemura, R.1    Okabe, S.2    Umeyama, T.3    Kanai, Y.4    Cowan, N.J.5    Hirokawa, N.6
  • 31
    • 78651098722 scopus 로고    scopus 로고
    • Negative regulation of ciliary length by ciliary male germ cell-associated kinase (Mak) is required for retinal photoreceptor survival
    • Omori, Y., Chaya, T., Katoh, K., Kajimura, N., Sato, S., Muraoka, K., Ueno, S., Koyasu, T., Kondo, M. and Furukawa, T. (2010) Negative regulation of ciliary length by ciliary male germ cell-associated kinase (Mak) is required for retinal photoreceptor survival. Proc. Natl Acad. Sci. USA, 107, 22671-22676.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 22671-22676
    • Omori, Y.1    Chaya, T.2    Katoh, K.3    Kajimura, N.4    Sato, S.5    Muraoka, K.6    Ueno, S.7    Koyasu, T.8    Kondo, M.9    Furukawa, T.10
  • 34
    • 78650731392 scopus 로고    scopus 로고
    • The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
    • Shida, T., Cueva, J.G., Xu, Z., Goodman, M.B. and Nachury, M.V. (2010) The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl Acad. Sci. USA, 107, 21517-21522.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 21517-21522
    • Shida, T.1    Cueva, J.G.2    Xu, Z.3    Goodman, M.B.4    Nachury, M.V.5
  • 36
    • 82955207160 scopus 로고    scopus 로고
    • Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylation
    • Di Fulvio, S., Azakir, B.A., Therrien, C. and Sinnreich, M. (2011) Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylation. PLoS One, 6, e28563.
    • (2011) PLoS One , vol.6
    • Di Fulvio, S.1    Azakir, B.A.2    Therrien, C.3    Sinnreich, M.4
  • 39
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J.P., Godin, J.D., Charrin, B.C., Cordelières, F.P., King, S.J., Humbert, S. and Saudou, F. (2007) Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci., 27, 3571-3583.
    • (2007) J. Neurosci. , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelières, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 40
    • 0027215453 scopus 로고
    • Acetylated alpha-tubulin in the connecting cilium of developing rat photoreceptors
    • Arikawa, K. and Williams, D.S. (1993) Acetylated alpha-tubulin in the connecting cilium of developing rat photoreceptors. Invest. Ophthalmol. Vis. Sci., 34, 2145-2149.
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 2145-2149
    • Arikawa, K.1    Williams, D.S.2
  • 41
    • 33846388924 scopus 로고    scopus 로고
    • Localization of glutamate receptors to distal dendrites depends on subunit composition and the kinesin motor protein KIF17
    • Kayadjanian, N., Lee, H.S., Piña-Crespo, J. and Heinemann, S.F. (2007) Localization of glutamate receptors to distal dendrites depends on subunit composition and the kinesin motor protein KIF17. Mol. Cell. Neurosci., 34, 219-230.
    • (2007) Mol. Cell. Neurosci. , vol.34 , pp. 219-230
    • Kayadjanian, N.1    Lee, H.S.2    Piña-Crespo, J.3    Heinemann, S.F.4
  • 43
    • 9644264076 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with Veli3 at distinct intercellular junctions of the neurosensory retina
    • Stöhr, H., Molday, L.L., Molday, R.S., Weber, B.H., Biedermann, B., Reichenbach, A. and Krämer, F. (2005) Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with Veli3 at distinct intercellular junctions of the neurosensory retina. J. Comp. Neurol., 481, 31-41.
    • (2005) J. Comp. Neurol. , vol.481 , pp. 31-41
    • Stöhr, H.1    Molday, L.L.2    Molday, R.S.3    Weber, B.H.4    Biedermann, B.5    Reichenbach, A.6    Krämer, F.7
  • 44
    • 0021766626 scopus 로고
    • Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides
    • MacKenzie, D., Arendt, A., Hargrave, P., McDowell, J.H. and Molday, R.S. (1984) Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides. Biochemistry, 23, 6544-6549.
    • (1984) Biochemistry , vol.23 , pp. 6544-6549
    • MacKenzie, D.1    Arendt, A.2    Hargrave, P.3    McDowell, J.H.4    Molday, R.S.5
  • 46
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment
    • Katoh, K., Kuma, K., Toh, H. and Miyata, T. (2005) MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res., 33, 511-518.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 47
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole, C., Barber, J.D. and Barton, G.J. (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res., 36, W197-201.
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.