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Volumn 52, Issue 33, 2013, Pages 5585-5592

The C2 domains of otoferlin, dysferlin, and myoferlin alter the packing of lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE MEASUREMENTS; HIGH SALT CONCENTRATION; MEMBRANE FUSION AND FISSION; NEGATIVELY CHARGED; NONELECTROSTATIC COMPONENTS; PHOSPHATIDYLGLYCEROLS; PHOSPHATIDYLSERINE; SMALL UNILAMELLAR VESICLE;

EID: 84882697463     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400432f     Document Type: Article
Times cited : (38)

References (31)
  • 1
    • 84855912661 scopus 로고    scopus 로고
    • Ferlins: Regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repair
    • Lek, A., Evesson, F. J., Sutton, R. B., North, K. N., and Cooper, S. T. (2012) Ferlins: Regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repair Traffic 13, 185-194
    • (2012) Traffic , vol.13 , pp. 185-194
    • Lek, A.1    Evesson, F.J.2    Sutton, R.B.3    North, K.N.4    Cooper, S.T.5
  • 2
    • 33746054560 scopus 로고    scopus 로고
    • 2+-mediated membrane fusion during C. Elegans spermatogenesis
    • 2+-mediated membrane fusion during C. elegans spermatogenesis J. Cell Sci. 119, 2552-2562
    • (2006) J. Cell Sci. , vol.119 , pp. 2552-2562
    • Washington, N.L.1    Ward, S.2
  • 3
    • 0042972741 scopus 로고    scopus 로고
    • The Drosophila misfire gene has an essential role in sperm activation during fertilization
    • Ohsako, T., Hirai, K., and Yamamoto, M. T. (2003) The Drosophila misfire gene has an essential role in sperm activation during fertilization Genes Genet. Syst. 78, 253-266
    • (2003) Genes Genet. Syst. , vol.78 , pp. 253-266
    • Ohsako, T.1    Hirai, K.2    Yamamoto, M.T.3
  • 4
    • 69449092161 scopus 로고    scopus 로고
    • Otoferlin is critical for a highly sensitive and linear calcium-dependent exocytosis at vestibular hair cell ribbon synapses
    • Dulon, D., Safieddine, S., Jones, S. M., and Petit, C. (2009) Otoferlin is critical for a highly sensitive and linear calcium-dependent exocytosis at vestibular hair cell ribbon synapses J. Neurosci. 29, 10474-10487
    • (2009) J. Neurosci. , vol.29 , pp. 10474-10487
    • Dulon, D.1    Safieddine, S.2    Jones, S.M.3    Petit, C.4
  • 11
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski, E. A. and Falke, J. J. (1996) The C2 domain calcium-binding motif: Structural and functional diversity Protein Sci. 5, 2375-2390
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 14
    • 79960149724 scopus 로고    scopus 로고
    • Synaptotagmin 1 modulates lipid acyl chain order in lipid bilayers by demixing phosphatidylserine
    • Lai, A. L., Tamm, L. K., Ellena, J. F., and Cafiso, D. S. (2011) Synaptotagmin 1 modulates lipid acyl chain order in lipid bilayers by demixing phosphatidylserine J. Biol. Chem. 286, 25291-25300
    • (2011) J. Biol. Chem. , vol.286 , pp. 25291-25300
    • Lai, A.L.1    Tamm, L.K.2    Ellena, J.F.3    Cafiso, D.S.4
  • 15
    • 77957731333 scopus 로고    scopus 로고
    • Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion
    • Johnson, C. P. and Chapman, E. R. (2010) Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion J. Cell Biol. 191, 187-197
    • (2010) J. Cell Biol. , vol.191 , pp. 187-197
    • Johnson, C.P.1    Chapman, E.R.2
  • 16
    • 64849112183 scopus 로고    scopus 로고
    • Characterization of lipid binding specificities of dysferlin C2 domains reveals novel interactions with phosphoinositides
    • Therrien, C., Di Fulvio, S., Pickles, S., and Sinnreich, M. (2009) Characterization of lipid binding specificities of dysferlin C2 domains reveals novel interactions with phosphoinositides Biochemistry 48, 2377-2384
    • (2009) Biochemistry , vol.48 , pp. 2377-2384
    • Therrien, C.1    Di Fulvio, S.2    Pickles, S.3    Sinnreich, M.4
  • 17
    • 0037151075 scopus 로고    scopus 로고
    • Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains
    • Davis, D. B., Doherty, K. R., Delmonte, A. J., and McNally, E. M. (2002) Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains J. Biol. Chem. 277, 22883-22888
    • (2002) J. Biol. Chem. , vol.277 , pp. 22883-22888
    • Davis, D.B.1    Doherty, K.R.2    Delmonte, A.J.3    McNally, E.M.4
  • 18
    • 0031807765 scopus 로고    scopus 로고
    • Water dynamics in glycosphingolipid aggregates studied by LAURDAN fluorescence
    • Bagatolli, L. A., Gratton, E., and Fidelio, G. D. (1998) Water dynamics in glycosphingolipid aggregates studied by LAURDAN fluorescence Biophys. J. 75, 331-341
    • (1998) Biophys. J. , vol.75 , pp. 331-341
    • Bagatolli, L.A.1    Gratton, E.2    Fidelio, G.D.3
  • 19
    • 12244278268 scopus 로고    scopus 로고
    • Giant vesicles, Laurdan, and two-photon fluorescence microscopy: Evidence of lipid lateral separation in bilayers
    • Bagatolli, L. A., Sanchez, S. A., Hazlett, T., and Gratton, E. (2003) Giant vesicles, Laurdan, and two-photon fluorescence microscopy: Evidence of lipid lateral separation in bilayers Methods Enzymol. 360, 481-500
    • (2003) Methods Enzymol. , vol.360 , pp. 481-500
    • Bagatolli, L.A.1    Sanchez, S.A.2    Hazlett, T.3    Gratton, E.4
  • 20
    • 34547792309 scopus 로고    scopus 로고
    • In silico functional and structural characterisation of ferlin proteins by mapping disease-causing mutations and evolutionary information onto three-dimensional models of their C2 domains
    • Jiménez, J. L. and Bashir, R. (2007) In silico functional and structural characterisation of ferlin proteins by mapping disease-causing mutations and evolutionary information onto three-dimensional models of their C2 domains J. Neurol. Sci. 260, 114-123
    • (2007) J. Neurol. Sci. , vol.260 , pp. 114-123
    • Jiménez, J.L.1    Bashir, R.2
  • 22
    • 59449093847 scopus 로고    scopus 로고
    • Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3
    • Ramakrishnan, N. A., Drescher, M. J., and Drescher, D. G. (2009) Direct interaction of otoferlin with syntaxin 1A, SNAP-25, and the L-type voltage-gated calcium channel Cav1.3 J. Biol. Chem. 284, 1364-1372
    • (2009) J. Biol. Chem. , vol.284 , pp. 1364-1372
    • Ramakrishnan, N.A.1    Drescher, M.J.2    Drescher, D.G.3
  • 23
    • 84867906699 scopus 로고    scopus 로고
    • Otoferlin: A multi-C2 domain protein essential for hearing
    • Pangršič, T., Reisinger, E., and Moser, T. (2012) Otoferlin: A multi-C2 domain protein essential for hearing Trends Neurosci. 35, 671-680
    • (2012) Trends Neurosci. , vol.35 , pp. 671-680
    • Pangršič, T.1    Reisinger, E.2    Moser, T.3
  • 24
    • 78649763791 scopus 로고    scopus 로고
    • Laurdan and di-4-ANEPPDHQ do not respond to membrane-inserted peptides and are good probes for lipid packing
    • Dinic, J., BiverstaÌŠhl, H., Mäler, L., and Parmryd, I. (2011) Laurdan and di-4-ANEPPDHQ do not respond to membrane-inserted peptides and are good probes for lipid packing Biochim. Biophys. Acta 1808, 298-306
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 298-306
    • Dinic, J.1    Biverstaìšhl, H.2    Mäler, L.3    Parmryd, I.4
  • 25
    • 0037144117 scopus 로고    scopus 로고
    • Use of laurdan fluorescence intensity and polarization to distinguish between changes in membrane fluidity and phospholipid order
    • Harris, F. M., Best, K. B., and Bell, J. D. (2002) Use of laurdan fluorescence intensity and polarization to distinguish between changes in membrane fluidity and phospholipid order Biochim. Biophys. Acta 1565, 123-128
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 123-128
    • Harris, F.M.1    Best, K.B.2    Bell, J.D.3
  • 26
    • 70350784080 scopus 로고    scopus 로고
    • PI(4,5)P2 degradation promotes the formation of cytoskeleton-free model membrane systems
    • Keller, H., Lorizate, M., and Schwille, P. (2009) PI(4,5)P2 degradation promotes the formation of cytoskeleton-free model membrane systems ChemPhysChem 10, 2805-2812
    • (2009) ChemPhysChem , vol.10 , pp. 2805-2812
    • Keller, H.1    Lorizate, M.2    Schwille, P.3
  • 27
    • 84867077527 scopus 로고    scopus 로고
    • Hydrophobic contributions to the membrane docking of synaptotagmin 7 C2A domain: Mechanistic contrast between isoforms 1 and 7
    • Brandt, D. S., Coffman, M. D., Falke, J. J., and Knight, J. D. (2012) Hydrophobic contributions to the membrane docking of synaptotagmin 7 C2A domain: Mechanistic contrast between isoforms 1 and 7 Biochemistry 51, 7654-7664
    • (2012) Biochemistry , vol.51 , pp. 7654-7664
    • Brandt, D.S.1    Coffman, M.D.2    Falke, J.J.3    Knight, J.D.4
  • 29
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman, E. R. (2008) How does synaptotagmin trigger neurotransmitter release? Annu. Rev. Biochem. 77, 615-641
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 31
    • 0036161583 scopus 로고    scopus 로고
    • Electrostatic control of the membrane targeting of C2 domains
    • Murray, D. and Honig, B. (2002) Electrostatic control of the membrane targeting of C2 domains Mol. Cell 9, 145-154
    • (2002) Mol. Cell , vol.9 , pp. 145
    • Murray, D.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.