메뉴 건너뛰기




Volumn 17, Issue 3, 2016, Pages 245-266

Ferlins Show Tissue-Specific Expression and Segregate as Plasma Membrane/Late Endosomal or Trans-Golgi/Recycling Ferlins

Author keywords

Dysferlin; Fer1L4; Fer1L5; Fer1L6; Late endosome; Myoferlin; Otoferlin; Rab7; Recycling endosome; Trans Golgi

Indexed keywords

CALRETICULIN; DYSFERLIN; FER1L4; FER1L5; FER1L6; GM130 PROTEIN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; MEMBRANE PROTEIN; MYOFERLIN; OTOFERLIN; PEX 14 PROTEIN; PEX30P PROTEIN; PEX31P PROTEIN; PROTEIN; RAB11 PROTEIN; TRANS GOLGI NETWORK INTEGRAL MEMBRANE PROTEIN 2; UNCLASSIFIED DRUG; WHEAT GERM AGGLUTININ; CALCIUM BINDING PROTEIN; MUSCLE PROTEIN; MYOF PROTEIN, HUMAN; OTOF PROTEIN, HUMAN; RAB PROTEIN;

EID: 84959061752     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12370     Document Type: Article
Times cited : (40)

References (59)
  • 1
    • 84855912661 scopus 로고    scopus 로고
    • Ferlins: regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repair
    • Lek A, Evesson FJ, Sutton RB, North KN, Cooper ST. Ferlins: regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repair. Traffic 2012;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
  • 4
    • 41649109400 scopus 로고    scopus 로고
    • Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris
    • Yan M, Rachubinski DA, Joshi S, Rachubinski RA, Subramani S. Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris. Mol Biol Cell 2008;19:885-898.
    • (2008) Mol Biol Cell , vol.19 , pp. 885-898
    • Yan, M.1    Rachubinski, D.A.2    Joshi, S.3    Rachubinski, R.A.4    Subramani, S.5
  • 5
    • 77955001359 scopus 로고    scopus 로고
    • Phylogenetic analysis of ferlin genes reveals ancient eukaryotic origins
    • Lek A, Lek M, North K, Cooper S. Phylogenetic analysis of ferlin genes reveals ancient eukaryotic origins. BMC Evol Biol 2010;10:231.
    • (2010) BMC Evol Biol , vol.10 , pp. 231
    • Lek, A.1    Lek, M.2    North, K.3    Cooper, S.4
  • 6
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold
    • Sutton RB, Davletov BA, Berghuis AM, Sudhof TC, Sprang SR. 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    Sudhof, T.C.4    Sprang, S.R.5
  • 7
    • 55549100557 scopus 로고    scopus 로고
    • The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function
    • Xue M, Ma C, Craig TK, Rosenmund C, Rizo J. The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function. Nat Struct Mol Biol 2008;15:1160-1168.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1160-1168
    • Xue, M.1    Ma, C.2    Craig, T.K.3    Rosenmund, C.4    Rizo, J.5
  • 8
    • 0032577067 scopus 로고    scopus 로고
    • Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers
    • Chapman ER, Davis AF. Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers. J Biol Chem 1998;273:13995-14001.
    • (1998) J Biol Chem , vol.273 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 9
    • 77649139375 scopus 로고    scopus 로고
    • Membrane curvature in synaptic vesicle fusion and beyond
    • McMahon HT, Kozlov MM, Martens S. Membrane curvature in synaptic vesicle fusion and beyond. Cell 2010;140:601-605.
    • (2010) Cell , vol.140 , pp. 601-605
    • McMahon, H.T.1    Kozlov, M.M.2    Martens, S.3
  • 11
    • 79551689695 scopus 로고    scopus 로고
    • The crystal structure of the C2A 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 C2A 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
  • 12
    • 84892753234 scopus 로고    scopus 로고
    • Quantitation of the calcium and membrane binding properties of the c2 domains of dysferlin
    • Abdullah N, Padmanarayana M, Marty NJ, Johnson CP. Quantitation of the calcium and membrane binding properties of the c2 domains of dysferlin. Biophys J 2014;106:382-389.
    • (2014) Biophys J , vol.106 , pp. 382-389
    • Abdullah, N.1    Padmanarayana, M.2    Marty, N.J.3    Johnson, C.P.4
  • 14
    • 84905695329 scopus 로고    scopus 로고
    • Characterization of the lipid binding properties of otoferlin reveals specific interactions between PI(4,5)P2 and the C2C and C2F domains
    • Padmanarayana M, Hams N, Speight LC, Petersson EJ, Mehl RA, Johnson CP. Characterization of the lipid binding properties of otoferlin reveals specific interactions between PI(4, 5)P2 and the C2C and C2F domains. Biochemistry 2014;53:5023-5033.
    • (2014) Biochemistry , vol.53 , pp. 5023-5033
    • Padmanarayana, M.1    Hams, N.2    Speight, L.C.3    Petersson, E.J.4    Mehl, R.A.5    Johnson, C.P.6
  • 18
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt R, Bi G, Alderton J. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science 1994;263:390-393.
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.1    Bi, G.2    Alderton, J.3
  • 20
    • 84858198502 scopus 로고    scopus 로고
    • In vivo imaging of molecular interactions at damaged sarcolemma
    • Roostalu U, Strähle U. In vivo imaging of molecular interactions at damaged sarcolemma. Dev Cell 2012;22:515-529.
    • (2012) Dev Cell , vol.22 , pp. 515-529
    • Roostalu, U.1    Strähle, U.2
  • 22
    • 0033846745 scopus 로고    scopus 로고
    • OTOF encodes multiple long and short isoforms: genetic evidence that the long ones underlie recessive deafness DFNB9
    • Si Yasunaga, Grati Mh, Chardenoux S, Smith TN, Friedman TB, Lalwani AK, Wilcox ER, Petit C. OTOF encodes multiple long and short isoforms: genetic evidence that the long ones underlie recessive deafness DFNB9. Am J Hum Genet 2000;67:591-600.
    • (2000) Am J Hum Genet , vol.67 , pp. 591-600
    • Si, Y.1    Grati, M.2    Chardenoux, S.3    Smith, T.N.4    Friedman, T.B.5    Lalwani, A.K.6    Wilcox, E.R.7    Petit, C.8
  • 27
    • 84876529480 scopus 로고    scopus 로고
    • Expression of myoferlin in human and murine carcinoma tumors: role in membrane repair, cell proliferation, and tumorigenesis
    • Leung C, Yu C, Lin MI, Tognon C, Bernatchez P. Expression of myoferlin in human and murine carcinoma tumors: role in membrane repair, cell proliferation, and tumorigenesis. Am J Pathol 2013;182:1900-1909.
    • (2013) Am J Pathol , vol.182 , pp. 1900-1909
    • Leung, C.1    Yu, C.2    Lin, M.I.3    Tognon, C.4    Bernatchez, P.5
  • 28
    • 84883493436 scopus 로고    scopus 로고
    • iTRAQ-based quantitative proteomics reveals myoferlin as a novel prognostic predictor in pancreatic adenocarcinoma
    • Wang W-S, Liu X-H, Liu L-X, Lou W-H, Jin D-Y, Yang P-Y, Wang X-L. iTRAQ-based quantitative proteomics reveals myoferlin as a novel prognostic predictor in pancreatic adenocarcinoma. J Proteomics 2013;91:453-465.
    • (2013) J Proteomics , vol.91 , pp. 453-465
    • Wang, W.-S.1    Liu, X.-H.2    Liu, L.-X.3    Lou, W.-H.4    Jin, D.-Y.5    Yang, P.-Y.6    Wang, X.-L.7
  • 29
    • 0033972161 scopus 로고    scopus 로고
    • Myoferlin, a candidate gene and potential modifier of muscular dystrophy
    • Davis DB, Delmonte AJ, Ly CT, McNally EM. Myoferlin, a candidate gene and potential modifier of muscular dystrophy. Hum Mol Genet 2000;9:217-226.
    • (2000) Hum Mol Genet , vol.9 , pp. 217-226
    • Davis, D.B.1    Delmonte, A.J.2    Ly, C.T.3    McNally, E.M.4
  • 33
    • 0029036903 scopus 로고
    • Identification of a nonneuronal isoform of synaptotagmin
    • Hudson AW, Birnbaum MJ. Identification of a nonneuronal isoform of synaptotagmin. Proc Natl Acad Sci 1995;92:5895-5899.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 5895-5899
    • Hudson, A.W.1    Birnbaum, M.J.2
  • 35
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many?
    • Südhof TC. Synaptotagmins: Why so many? J Biol Chem 2002;277:7629-7632.
    • (2002) J Biol Chem , vol.277 , pp. 7629-7632
    • Südhof, T.C.1
  • 36
    • 3042796387 scopus 로고    scopus 로고
    • Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons
    • T-i Nishiki, Augustine GJ. Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons. J Neurosci 2004;24:6127-6132.
    • (2004) J Neurosci , vol.24 , pp. 6127-6132
    • T-i, N.1    Augustine, G.J.2
  • 37
    • 70349488728 scopus 로고    scopus 로고
    • Differential but convergent functions of Ca2+ binding to synaptotagmin-1 C2 domains mediate neurotransmitter release
    • Shin O-H, Xu J, Rizo J, Südhof TC. Differential but convergent functions of Ca2+ binding to synaptotagmin-1 C2 domains mediate neurotransmitter release. Proc Natl Acad Sci 2009;106:16469-16474.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 16469-16474
    • Shin, O.-H.1    Xu, J.2    Rizo, J.3    Südhof, T.C.4
  • 38
    • 0035016467 scopus 로고    scopus 로고
    • Expression and localisation of synaptotagmin isoforms in endocrine (β)-cells: their function in insulin exocytosis
    • Gut A, Kiraly CE, Fukuda M, Mikoshiba K, Wollheim CB, Lang J. Expression and localisation of synaptotagmin isoforms in endocrine (β)-cells: their function in insulin exocytosis. J Cell Sci 2001;114:1709-1716.
    • (2001) J Cell Sci , vol.114 , pp. 1709-1716
    • Gut, A.1    Kiraly, C.E.2    Fukuda, M.3    Mikoshiba, K.4    Wollheim, C.B.5    Lang, J.6
  • 41
    • 77956542690 scopus 로고    scopus 로고
    • Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway
    • Evesson FJ, Peat RA, Lek A, Brilot F, Lo HP, Dale RC, Parton RG, North KN, Cooper ST. Reduced plasma membrane expression of dysferlin mutants is attributed to accelerated endocytosis via a syntaxin-4-associated pathway. J Biol Chem 2010;285:28529-28539.
    • (2010) J Biol Chem , vol.285 , pp. 28529-28539
    • Evesson, F.J.1    Peat, R.A.2    Lek, A.3    Brilot, F.4    Lo, H.P.5    Dale, R.C.6    Parton, R.G.7    North, K.N.8    Cooper, S.T.9
  • 43
    • 0026570788 scopus 로고
    • Perturbation of the morphology of the trans-Golgi network following Brefeldin A treatment: redistribution of a TGN-specific integral membrane protein, TGN38
    • Reaves B, Banting G. Perturbation of the morphology of the trans-Golgi network following Brefeldin A treatment: redistribution of a TGN-specific integral membrane protein, TGN38. J Cell Biol 1992;116:85-94.
    • (1992) J Cell Biol , vol.116 , pp. 85-94
    • Reaves, B.1    Banting, G.2
  • 44
    • 78751683605 scopus 로고    scopus 로고
    • Impaired muscle growth and response to insulin-like growth factor 1 in dysferlin-mediated muscular dystrophy
    • Demonbreun AR, Fahrenbach JP, Deveaux K, Earley JU, Pytel P, McNally EM. Impaired muscle growth and response to insulin-like growth factor 1 in dysferlin-mediated muscular dystrophy. Hum Mol Genet 2011;20:779-789.
    • (2011) Hum Mol Genet , vol.20 , pp. 779-789
    • Demonbreun, A.R.1    Fahrenbach, J.P.2    Deveaux, K.3    Earley, J.U.4    Pytel, P.5    McNally, E.M.6
  • 48
    • 56049124302 scopus 로고    scopus 로고
    • Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form
    • Heidrych P, Zimmermann U, Breß A, Pusch CM, Ruth P, Pfister M, Knipper M, Blin N. Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form. Hum Mol Genet 2008;17:3814-3821.
    • (2008) Hum Mol Genet , vol.17 , pp. 3814-3821
    • Heidrych, P.1    Zimmermann, U.2    Breß, A.3    Pusch, C.M.4    Ruth, P.5    Pfister, M.6    Knipper, M.7    Blin, N.8
  • 49
    • 84905842790 scopus 로고    scopus 로고
    • Exocytotic machineries of vestibular type I and cochlear ribbon synapses display similar intrinsic otoferlin-dependent Ca2+ sensitivity but a different coupling to Ca2+ channels
    • Vincent PF, Bouleau Y, Safieddine S, Petit C, Dulon D. Exocytotic machineries of vestibular type I and cochlear ribbon synapses display similar intrinsic otoferlin-dependent Ca2+ sensitivity but a different coupling to Ca2+ channels. J Neurosci 2014;34:10853-10869.
    • (2014) J Neurosci , vol.34 , pp. 10853-10869
    • Vincent, P.F.1    Bouleau, Y.2    Safieddine, S.3    Petit, C.4    Dulon, D.5
  • 50
    • 84863714858 scopus 로고    scopus 로고
    • Expression of myoferlin in human airway epithelium and its role in cell adhesion and zonula occludens-1 expression
    • Leung C, Shaheen F, Bernatchez P, Hackett T-L. Expression of myoferlin in human airway epithelium and its role in cell adhesion and zonula occludens-1 expression. PLoS One 2012;7:e40478.
    • (2012) PLoS One , vol.7 , pp. e40478
    • Leung, C.1    Shaheen, F.2    Bernatchez, P.3    Hackett, T.-L.4
  • 57
    • 84866719247 scopus 로고    scopus 로고
    • 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis
    • Strauss MP, Liew ATF, Turnbull L, Whitchurch CB, Monahan LG, Harry EJ. 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis. PLoS Biol 2012;10:e1001389.
    • (2012) PLoS Biol , vol.10 , pp. e1001389
    • Strauss, M.P.1    Liew, A.T.F.2    Turnbull, L.3    Whitchurch, C.B.4    Monahan, L.G.5    Harry, E.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.