메뉴 건너뛰기




Volumn 8, Issue 1, 2014, Pages 1-9

C2 domains as protein-protein interaction modules in the ciliary transition zone

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GA BINDING PROTEIN; RETINITIS PIGMENTOSA G PROTEIN REGULATOR; RHEB PROTEIN; RPGR INTERACTING PROTEIN 1; UNCLASSIFIED DRUG; CALCIUM; EYE PROTEIN; PHOSPHOLIPID; PROTEIN; PROTEIN BINDING; RPGR PROTEIN, HUMAN; RPGRIP1 PROTEIN, HUMAN; BINDING PROTEIN; CALCIUM ION; REGULATOR PROTEIN; RETINITIS PIGMENTOSA G PROTEIN REGULATOR INTERACTING PROTEIN 1; RETINITIS PIGMENTOSA G PROTEIN REGULATOR INTERACTING PROTEIN 1 LIKE PROTEIN;

EID: 84904035877     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2014.05.049     Document Type: Article
Times cited : (35)

References (37)
  • 4
    • 0034284501 scopus 로고    scopus 로고
    • Identification of a novel protein interacting with RPGR
    • Boylan J.P., Wright A.F. Identification of a novel protein interacting with RPGR. Hum. Mol. Genet. 2000, 9:2085-2093.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2085-2093
    • Boylan, J.P.1    Wright, A.F.2
  • 5
    • 0042131538 scopus 로고    scopus 로고
    • RPGRIP1s with distinct neuronal localization and biochemical properties associate selectively with RanBP2 in amacrine neurons
    • Castagnet P., Mavlyutov T., Cai Y., Zhong F., Ferreira P. RPGRIP1s with distinct neuronal localization and biochemical properties associate selectively with RanBP2 in amacrine neurons. Hum. Mol. Genet. 2003, 12:1847-1863.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1847-1863
    • Castagnet, P.1    Mavlyutov, T.2    Cai, Y.3    Zhong, F.4    Ferreira, P.5
  • 7
    • 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 P.A., Arendt A., McDowell J.H. Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA. Proc. Natl. Acad. Sci. USA 1998, 95:10620-10625.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10620-10625
    • Deretic, D.1    Schmerl, S.2    Hargrave, P.A.3    Arendt, A.4    McDowell, J.H.5
  • 10
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen L.O., Perisic O., Cheung R., Katan M., Williams R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature 1996, 380:595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 13
    • 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 2009, 137:32-45.
    • (2009) Cell , vol.137 , pp. 32-45
    • Gerdes, J.M.1    Davis, E.E.2    Katsanis, N.3
  • 14
    • 79551689695 scopus 로고    scopus 로고
    • The crystal structure of the C[U+2082]A domain of otoferlin reveals an unconventional top loop region
    • Helfmann S., Neumann P., Tittmann K., Moser T., Ficner R., Reisinger E. The crystal structure of the C[U+2082]A domain of otoferlin reveals an unconventional top loop region. J.Mol. Biol. 2011, 406:479-490.
    • (2011) J.Mol. Biol. , vol.406 , pp. 479-490
    • Helfmann, S.1    Neumann, P.2    Tittmann, K.3    Moser, T.4    Ficner, R.5    Reisinger, E.6
  • 15
    • 77954321994 scopus 로고    scopus 로고
    • Attractive interactions between side chains of histidine-histidine and histidine-arginine-based cationic dipeptides in water
    • Heyda J., Mason P.E., Jungwirth P. Attractive interactions between side chains of histidine-histidine and histidine-arginine-based cationic dipeptides in water. J.Phys. Chem. B 2010, 114:8744-8749.
    • (2010) J.Phys. Chem. B , vol.114 , pp. 8744-8749
    • Heyda, J.1    Mason, P.E.2    Jungwirth, P.3
  • 16
    • 0034724168 scopus 로고    scopus 로고
    • A retinitis pigmentosa GTPase regulator (RPGR)-deficient mouse model for X-linked retinitis pigmentosa (RP3)
    • Hong D.H., Pawlyk B.S., Shang J., Sandberg M.A., Berson E.L., Li T. A retinitis pigmentosa GTPase regulator (RPGR)-deficient mouse model for X-linked retinitis pigmentosa (RP3). Proc. Natl. Acad. Sci. USA 2000, 97:3649-3654.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3649-3654
    • Hong, D.H.1    Pawlyk, B.S.2    Shang, J.3    Sandberg, M.A.4    Berson, E.L.5    Li, T.6
  • 17
    • 77957731333 scopus 로고    scopus 로고
    • Otoferlin is a calcium sensor thatdirectly regulates SNARE-mediated membrane fusion
    • Johnson C.P., Chapman E.R. Otoferlin is a calcium sensor thatdirectly regulates SNARE-mediated membrane fusion. J.Cell Biol. 2010, 191:187-197.
    • (2010) J.Cell Biol. , vol.191 , pp. 187-197
    • Johnson, C.P.1    Chapman, E.R.2
  • 20
    • 0033573979 scopus 로고    scopus 로고
    • The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase
    • Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J. The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase. Proc. Natl. Acad. Sci. USA 1999, 96:1315-1320.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1315-1320
    • Linari, M.1    Ueffing, M.2    Manson, F.3    Wright, A.4    Meitinger, T.5    Becker, J.6
  • 21
    • 19744371800 scopus 로고    scopus 로고
    • Limited proteolysis differentially modulates the stability and subcellular localization of domains of RPGRIP1 that are distinctly affected by mutations in Leber's congenital amaurosis
    • Lu X., Guruju M., Oswald J., Ferreira P.A. Limited proteolysis differentially modulates the stability and subcellular localization of domains of RPGRIP1 that are distinctly affected by mutations in Leber's congenital amaurosis. Hum. Mol. Genet. 2005, 14:1327-1340.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1327-1340
    • Lu, X.1    Guruju, M.2    Oswald, J.3    Ferreira, P.A.4
  • 23
    • 0036667989 scopus 로고    scopus 로고
    • Species-specific subcellular localization of RPGR and RPGRIP isoforms: implications for the phenotypic variability of congenital retinopathies among species
    • Mavlyutov T.A., Zhao H., Ferreira P.A. Species-specific subcellular localization of RPGR and RPGRIP isoforms: implications for the phenotypic variability of congenital retinopathies among species. Hum. Mol. Genet. 2002, 11:1899-1907.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1899-1907
    • Mavlyutov, T.A.1    Zhao, H.2    Ferreira, P.A.3
  • 25
    • 0035943428 scopus 로고    scopus 로고
    • Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains
    • Ochoa W.F., Garcia-Garcia J., Fita I., Corbalan-Garcia S., Verdaguer N., Gomez-Fernandez J.C. Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains. J.Mol. Biol. 2001, 311:837-849.
    • (2001) J.Mol. Biol. , vol.311 , pp. 837-849
    • Ochoa, W.F.1    Garcia-Garcia, J.2    Fita, I.3    Corbalan-Garcia, S.4    Verdaguer, N.5    Gomez-Fernandez, J.C.6
  • 28
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold
    • Sutton R.B., Davletov B.A., Berghuis A.M., Südhof T.C., Sprang S.R. Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell 1995, 80:929-938.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Südhof, T.C.4    Sprang, S.R.5
  • 32
    • 0036185994 scopus 로고    scopus 로고
    • Transport to the photoreceptor outer segment by myosin VIIa and kinesin II
    • Williams D.S. Transport to the photoreceptor outer segment by myosin VIIa and kinesin II. Vision Res. 2002, 42:455-462.
    • (2002) Vision Res. , vol.42 , pp. 455-462
    • Williams, D.S.1
  • 33
    • 79955513961 scopus 로고    scopus 로고
    • MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis
    • Williams C.L., Li C., Kida K., Inglis P.N., Mohan S., Semenec L., Bialas N.J., Stupay R.M., Chen N., Blacque O.E., et al. MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis. J.Cell Biol. 2011, 192:1023-1041.
    • (2011) J.Cell Biol. , vol.192 , pp. 1023-1041
    • Williams, C.L.1    Li, C.2    Kida, K.3    Inglis, P.N.4    Mohan, S.5    Semenec, L.6    Bialas, N.J.7    Stupay, R.M.8    Chen, N.9    Blacque, O.E.10
  • 34
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parametersto model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., Murshudov G.N. Use of TLS parametersto model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 2001, 57:122-133.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 35
    • 77957866592 scopus 로고    scopus 로고
    • Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes
    • Zhang D., Aravind L. Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes. Gene 2010, 469:18-30.
    • (2010) Gene , vol.469 , pp. 18-30
    • Zhang, D.1    Aravind, L.2
  • 36
    • 84868028170 scopus 로고    scopus 로고
    • Novel transglutaminase-like peptidase and C2 domains elucidate the structure, biogenesis and evolution of the ciliary compartment
    • Zhang D., Aravind L. Novel transglutaminase-like peptidase and C2 domains elucidate the structure, biogenesis and evolution of the ciliary compartment. Cell Cycle 2012, 11:3861-3875.
    • (2012) Cell Cycle , vol.11 , pp. 3861-3875
    • Zhang, D.1    Aravind, L.2
  • 37
    • 0037389431 scopus 로고    scopus 로고
    • The retinitis pigmentosa GTPase regulator (RPGR)- interacting protein: subserving RPGR function and participating in disk morphogenesis
    • Zhao Y., Hong D.H., Pawlyk B., Yue G., Adamian M., Grynberg M., Godzik A., Li T. The retinitis pigmentosa GTPase regulator (RPGR)- interacting protein: subserving RPGR function and participating in disk morphogenesis. Proc. Natl. Acad. Sci. USA 2003, 100:3965-3970.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3965-3970
    • Zhao, Y.1    Hong, D.H.2    Pawlyk, B.3    Yue, G.4    Adamian, M.5    Grynberg, M.6    Godzik, A.7    Li, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.