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Volumn 45, Issue , 2015, Pages 24-31

Calcium signaling in membrane repair

Author keywords

Ca2+; Calcium sensor; Lysosomal exocytosis; Membrane repair; TRPML1

Indexed keywords

ANNEXIN; CADMIUM BINDING PROTEIN; CALCIUM CHANNEL; CALCIUM ION; CALPAIN; DYSFERLIN; ION CHANNEL; SYNAPTOTAGMIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL;

EID: 84949231181     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2015.10.031     Document Type: Review
Times cited : (71)

References (128)
  • 1
    • 20344402550 scopus 로고    scopus 로고
    • An emergency response team for membrane repair
    • McNeil P.L., Kirchhausen T. An emergency response team for membrane repair. Nat. Rev. Mol. Cell Biol. 2005, 6(6):499-505.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , Issue.6 , pp. 499-505
    • McNeil, P.L.1    Kirchhausen, T.2
  • 2
    • 84923820273 scopus 로고    scopus 로고
    • Damage control: cellular mechanisms of plasma membrane repair
    • Andrews N.W., Almeida P.E., Corrotte M. Damage control: cellular mechanisms of plasma membrane repair. Trends Cell Biol. 2014, 24(12):734-742.
    • (2014) Trends Cell Biol. , vol.24 , Issue.12 , pp. 734-742
    • Andrews, N.W.1    Almeida, P.E.2    Corrotte, M.3
  • 3
    • 84921777202 scopus 로고    scopus 로고
    • Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins
    • Suetsugu S., Kurisu S., Takenawa T. Dynamic shaping of cellular membranes by phospholipids and membrane-deforming proteins. Physiol. Rev. 2014, 94(4):1219-1248.
    • (2014) Physiol. Rev. , vol.94 , Issue.4 , pp. 1219-1248
    • Suetsugu, S.1    Kurisu, S.2    Takenawa, T.3
  • 4
    • 0034130361 scopus 로고    scopus 로고
    • Patching plasma membrane disruptions with cytoplasmic membrane
    • McNeil P.L., et al. Patching plasma membrane disruptions with cytoplasmic membrane. J. Cell Sci. 2000, 113(Pt 11):1891-1902.
    • (2000) J. Cell Sci. , vol.113 , pp. 1891-1902
    • McNeil, P.L.1
  • 5
    • 0028886494 scopus 로고
    • Expression of prothrombinase activity and CD9 antigen on the surface of small vesicles from stimulated human endothelial cells
    • Kagawa H., et al. Expression of prothrombinase activity and CD9 antigen on the surface of small vesicles from stimulated human endothelial cells. Thromb. Res. 1995, 80(6):451-460.
    • (1995) Thromb. Res. , vol.80 , Issue.6 , pp. 451-460
    • Kagawa, H.1
  • 6
    • 0035958557 scopus 로고    scopus 로고
    • 2+)-regulated exocytosis of lysosomes
    • 2+)-regulated exocytosis of lysosomes. Cell 2001, 106(2):157-169.
    • (2001) Cell , vol.106 , Issue.2 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 7
    • 40849118150 scopus 로고    scopus 로고
    • 2+-dependent endocytosis
    • 2+-dependent endocytosis. J. Cell Biol. 2008, 180(5):905-914.
    • (2008) J. Cell Biol. , vol.180 , Issue.5 , pp. 905-914
    • Idone, V.1
  • 8
    • 54049109535 scopus 로고    scopus 로고
    • Two-way traffic on the road to plasma membrane repair
    • Idone V., Tam C., Andrews N.W. Two-way traffic on the road to plasma membrane repair. Trends Cell Biol. 2008, 18(11):552-559.
    • (2008) Trends Cell Biol. , vol.18 , Issue.11 , pp. 552-559
    • Idone, V.1    Tam, C.2    Andrews, N.W.3
  • 9
    • 77953576191 scopus 로고    scopus 로고
    • Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair
    • Tam C., et al. Exocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair. J. Cell Biol. 2010, 189(6):1027-1038.
    • (2010) J. Cell Biol. , vol.189 , Issue.6 , pp. 1027-1038
    • Tam, C.1
  • 10
    • 84897624850 scopus 로고    scopus 로고
    • ESCRT machinery is required for plasma membrane repair
    • Jimenez A.J., et al. ESCRT machinery is required for plasma membrane repair. Science 2014, 343(6174):1247136.
    • (2014) Science , vol.343 , Issue.6174 , pp. 1247136
    • Jimenez, A.J.1
  • 11
    • 78650176977 scopus 로고    scopus 로고
    • Blebbing confers resistance against cell lysis
    • Babiychuk E.B., et al. Blebbing confers resistance against cell lysis. Cell Death Differ. 2011, 18(1):80-89.
    • (2011) Cell Death Differ. , vol.18 , Issue.1 , pp. 80-89
    • Babiychuk, E.B.1
  • 12
    • 67650760385 scopus 로고    scopus 로고
    • 2+) operates a switch between repair and lysis of streptolysin O-perforated cells
    • 2+) operates a switch between repair and lysis of streptolysin O-perforated cells. Cell Death Differ. 2009, 16(8):1126-1134.
    • (2009) Cell Death Differ. , vol.16 , Issue.8 , pp. 1126-1134
    • Babiychuk, E.B.1
  • 13
    • 84964312696 scopus 로고    scopus 로고
    • Mechanism of Ca(2)(+)-triggered ESCRT assembly and regulation of cell membrane repair
    • Scheffer L.L., et al. Mechanism of Ca(2)(+)-triggered ESCRT assembly and regulation of cell membrane repair. Nat. Commun. 2014, 5:5646.
    • (2014) Nat. Commun. , vol.5 , pp. 5646
    • Scheffer, L.L.1
  • 14
    • 79951952737 scopus 로고    scopus 로고
    • Plasma membrane repair and cellular damage control: the annexin survival kit
    • Draeger A., Monastyrskaya K., Babiychuk E.B. Plasma membrane repair and cellular damage control: the annexin survival kit. Biochem. Pharmacol. 2011, 81(6):703-712.
    • (2011) Biochem. Pharmacol. , vol.81 , Issue.6 , pp. 703-712
    • Draeger, A.1    Monastyrskaya, K.2    Babiychuk, E.B.3
  • 15
    • 58149354372 scopus 로고    scopus 로고
    • Membrane repair redux: redox of MG53
    • McNeil P. Membrane repair redux: redox of MG53. Nat. Cell Biol. 2009, 11(1):7-9.
    • (2009) Nat. Cell Biol. , vol.11 , Issue.1 , pp. 7-9
    • McNeil, P.1
  • 16
    • 58149326805 scopus 로고    scopus 로고
    • MG53 nucleates assembly of cell membrane repair machinery
    • Cai C., et al. MG53 nucleates assembly of cell membrane repair machinery. Nat. Cell Biol. 2009, 11(1):56-64.
    • (2009) Nat. Cell Biol. , vol.11 , Issue.1 , pp. 56-64
    • Cai, C.1
  • 17
    • 0042978564 scopus 로고    scopus 로고
    • Impaired membrane resealing and autoimmune myositis in synaptotagmin VII-deficient mice
    • Chakrabarti S., et al. Impaired membrane resealing and autoimmune myositis in synaptotagmin VII-deficient mice. J. Cell Biol. 2003, 162(4):543-549.
    • (2003) J. Cell Biol. , vol.162 , Issue.4 , pp. 543-549
    • Chakrabarti, S.1
  • 19
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham D.E. Calcium signaling. Cell 2007, 131(6):1047-1058.
    • (2007) Cell , vol.131 , Issue.6 , pp. 1047-1058
    • Clapham, D.E.1
  • 20
    • 84921960605 scopus 로고    scopus 로고
    • The intracellular Ca(2)(+) channel MCOLN1 is required for sarcolemma repair to prevent muscular dystrophy
    • Cheng X., et al. The intracellular Ca(2)(+) channel MCOLN1 is required for sarcolemma repair to prevent muscular dystrophy. Nat. Med. 2014, 20(10):1187-1192.
    • (2014) Nat. Med. , vol.20 , Issue.10 , pp. 1187-1192
    • Cheng, X.1
  • 22
    • 84930539972 scopus 로고    scopus 로고
    • Organellar channels and transporters
    • Xu H., Martinoia E., Szabo I. Organellar channels and transporters. Cell Calcium 2015, 58(1):1-10.
    • (2015) Cell Calcium , vol.58 , Issue.1 , pp. 1-10
    • Xu, H.1    Martinoia, E.2    Szabo, I.3
  • 23
    • 0030611431 scopus 로고    scopus 로고
    • 2+ clearance in the cytosol of adrenal chromaffin cells
    • 2+ clearance in the cytosol of adrenal chromaffin cells. Biophys. J. 1997, 73(1):532-545.
    • (1997) Biophys. J. , vol.73 , Issue.1 , pp. 532-545
    • Xu, T.1
  • 24
    • 0030611092 scopus 로고    scopus 로고
    • 2+] at the mouth of a calcium channel
    • 2+] at the mouth of a calcium channel. J. Neurosci. 1997, 17(18):6961-6973.
    • (1997) J. Neurosci. , vol.17 , Issue.18 , pp. 6961-6973
    • Naraghi, M.1    Neher, E.2
  • 25
    • 0035754144 scopus 로고    scopus 로고
    • The local Ca concentration profile in the vicinity of a Ca channel
    • Bauer P.J. The local Ca concentration profile in the vicinity of a Ca channel. Cell Biochem. Biophys. 2001, 35(1):49-61.
    • (2001) Cell Biochem. Biophys. , vol.35 , Issue.1 , pp. 49-61
    • Bauer, P.J.1
  • 26
    • 1942421320 scopus 로고    scopus 로고
    • Calcium pumps of plasma membrane and cell interior
    • Strehler E.E., Treiman M. Calcium pumps of plasma membrane and cell interior. Curr. Mol. Med. 2004, 4(3):323-335.
    • (2004) Curr. Mol. Med. , vol.4 , Issue.3 , pp. 323-335
    • Strehler, E.E.1    Treiman, M.2
  • 27
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill M., Copello J.A. Ryanodine receptor calcium release channels. Physiol. Rev. 2002, 82(4):893-922.
    • (2002) Physiol. Rev. , vol.82 , Issue.4 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 28
    • 84880577375 scopus 로고    scopus 로고
    • The endoplasmic reticulum and junctional membrane communication during calcium signaling
    • Lam A.K., Galione A. The endoplasmic reticulum and junctional membrane communication during calcium signaling. Biochim. Biophys. Acta 2013, 1833(11):2542-2559.
    • (2013) Biochim. Biophys. Acta , vol.1833 , Issue.11 , pp. 2542-2559
    • Lam, A.K.1    Galione, A.2
  • 29
    • 84880762970 scopus 로고    scopus 로고
    • Store-operated orai channels: structure and function
    • Prakriya M. Store-operated orai channels: structure and function. Curr. Top. Membr. 2013, 71:1-32.
    • (2013) Curr. Top. Membr. , vol.71 , pp. 1-32
    • Prakriya, M.1
  • 30
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • Csordas G., et al. Structural and functional features and significance of the physical linkage between ER and mitochondria. J. Cell Biol. 2006, 174(7):915-921.
    • (2006) J. Cell Biol. , vol.174 , Issue.7 , pp. 915-921
    • Csordas, G.1
  • 31
    • 80054015726 scopus 로고    scopus 로고
    • 2+ signalling in health and disease
    • 2+ signalling in health and disease. Biochem. J. 2011, 439(3):349-374.
    • (2011) Biochem. J. , vol.439 , Issue.3 , pp. 349-374
    • Morgan, A.J.1
  • 32
    • 55549134611 scopus 로고    scopus 로고
    • Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium
    • Lloyd-Evans E., et al. Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium. Nat. Med. 2008, 14(11):1247-1255.
    • (2008) Nat. Med. , vol.14 , Issue.11 , pp. 1247-1255
    • Lloyd-Evans, E.1
  • 33
    • 79953318136 scopus 로고    scopus 로고
    • Two-pore channels for integrative Ca signaling
    • Zhu M.X., et al. Two-pore channels for integrative Ca signaling. Commun. Integr. Biol. 2010, 3(1):12-17.
    • (2010) Commun. Integr. Biol. , vol.3 , Issue.1 , pp. 12-17
    • Zhu, M.X.1
  • 34
    • 77955291039 scopus 로고    scopus 로고
    • TPC2 proteins mediate nicotinic acid adenine dinucleotide phosphate (NAADP)- and agonist-evoked contractions of smooth muscle
    • Tugba Durlu-Kandilci N., et al. TPC2 proteins mediate nicotinic acid adenine dinucleotide phosphate (NAADP)- and agonist-evoked contractions of smooth muscle. J. Biol. Chem. 2010, 285(32):24925-24932.
    • (2010) J. Biol. Chem. , vol.285 , Issue.32 , pp. 24925-24932
    • Tugba Durlu-Kandilci, N.1
  • 35
    • 77951205549 scopus 로고    scopus 로고
    • 2+) signaling and endolysosomal trafficking
    • 2+) signaling and endolysosomal trafficking. Curr. Biol. 2010, 20(8):703-709.
    • (2010) Curr. Biol. , vol.20 , Issue.8 , pp. 703-709
    • Ruas, M.1
  • 36
    • 84892441168 scopus 로고    scopus 로고
    • Two-pore channels (TPCs): current controversies
    • Morgan A.J., Galione A. Two-pore channels (TPCs): current controversies. Bioessays 2014, 36(2):173-183.
    • (2014) Bioessays , vol.36 , Issue.2 , pp. 173-183
    • Morgan, A.J.1    Galione, A.2
  • 37
    • 84871303001 scopus 로고    scopus 로고
    • NAADP activates two-pore channels on T cell cytolytic granules to stimulate exocytosis and killing
    • Davis L.C., et al. NAADP activates two-pore channels on T cell cytolytic granules to stimulate exocytosis and killing. Curr. Biol. 2012, 22(24):2331-2337.
    • (2012) Curr. Biol. , vol.22 , Issue.24 , pp. 2331-2337
    • Davis, L.C.1
  • 38
    • 84934982329 scopus 로고    scopus 로고
    • TPC: the NAADP discovery channel?
    • Morgan A.J., et al. TPC: the NAADP discovery channel?. Biochem. Soc. Trans. 2015, 43(3):384-389.
    • (2015) Biochem. Soc. Trans. , vol.43 , Issue.3 , pp. 384-389
    • Morgan, A.J.1
  • 39
    • 84866361328 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization
    • Lee H.C. Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization. J. Biol. Chem. 2012, 287(38):31633-31640.
    • (2012) J. Biol. Chem. , vol.287 , Issue.38 , pp. 31633-31640
    • Lee, H.C.1
  • 40
    • 38049113166 scopus 로고    scopus 로고
    • 2+) stores in sea urchin eggs
    • 2+) stores in sea urchin eggs. J. Biol. Chem. 2007, 282(52):37730-37737.
    • (2007) J. Biol. Chem. , vol.282 , Issue.52 , pp. 37730-37737
    • Morgan, A.J.1    Galione, A.2
  • 41
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt R.A., Bi G., Alderton J.M. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science 1994, 263(5145):390-393.
    • (1994) Science , vol.263 , Issue.5145 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 42
    • 0026332408 scopus 로고
    • 2+ and proteolysis in lethal oxidative injury in endothelial cells
    • 2+ and proteolysis in lethal oxidative injury in endothelial cells. Am. J. Physiol. 1991, 261(5 Pt 1):C889-C896.
    • (1991) Am. J. Physiol. , vol.261 , Issue.5 , pp. C889-C896
    • Geeraerts, M.D.1
  • 43
    • 84859175854 scopus 로고    scopus 로고
    • Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release
    • Shen D., et al. Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release. Nat. Commun. 2012, 3:731.
    • (2012) Nat. Commun. , vol.3 , pp. 731
    • Shen, D.1
  • 44
    • 77949695459 scopus 로고    scopus 로고
    • TRP channels of intracellular membranes
    • Dong X.P., Wang X., Xu H. TRP channels of intracellular membranes. J. Neurochem. 2010, 113(2):313-328.
    • (2010) J. Neurochem. , vol.113 , Issue.2 , pp. 313-328
    • Dong, X.P.1    Wang, X.2    Xu, H.3
  • 46
    • 36749070036 scopus 로고    scopus 로고
    • The role of calcium and other ions in sorting and delivery in the late endocytic pathway
    • Luzio J.P., Bright N.A., Pryor P.R. The role of calcium and other ions in sorting and delivery in the late endocytic pathway. Biochem. Soc. Trans. 2007, 35(Pt 5):1088-1091.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1088-1091
    • Luzio, J.P.1    Bright, N.A.2    Pryor, P.R.3
  • 47
    • 0034729167 scopus 로고    scopus 로고
    • 2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • 2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. 2000, 149(5):1053-1062.
    • (2000) J. Cell Biol. , vol.149 , Issue.5 , pp. 1053-1062
    • Pryor, P.R.1
  • 48
    • 0025947123 scopus 로고
    • Alien intracellular calcium chelators attenuate neurotransmitter release at the squid giant synapse
    • Adler E.M., et al. Alien intracellular calcium chelators attenuate neurotransmitter release at the squid giant synapse. J. Neurosci. 1991, 11(6):1496-1507.
    • (1991) J. Neurosci. , vol.11 , Issue.6 , pp. 1496-1507
    • Adler, E.M.1
  • 49
    • 0042160096 scopus 로고    scopus 로고
    • Calcium and calmodulin in membrane fusion
    • Burgoyne R.D., Clague M.J. Calcium and calmodulin in membrane fusion. Biochim. Biophys. Acta 2003, 1641(2-3):137-143.
    • (2003) Biochim. Biophys. Acta , vol.1641 , Issue.2-3 , pp. 137-143
    • Burgoyne, R.D.1    Clague, M.J.2
  • 50
    • 84864236399 scopus 로고    scopus 로고
    • On-chip electroporation, membrane repair dynamics and transient in-cell recordings by arrays of gold mushroom-shaped microelectrodes
    • Hai A., Spira M.E. On-chip electroporation, membrane repair dynamics and transient in-cell recordings by arrays of gold mushroom-shaped microelectrodes. Lab Chip 2012, 12(16):2865-2873.
    • (2012) Lab Chip , vol.12 , Issue.16 , pp. 2865-2873
    • Hai, A.1    Spira, M.E.2
  • 51
    • 84921270286 scopus 로고    scopus 로고
    • Membrane damage-induced vesicle-vesicle fusion of dysferlin-containing vesicles in muscle cells requires microtubules and kinesin
    • McDade J.R., Michele D.E. Membrane damage-induced vesicle-vesicle fusion of dysferlin-containing vesicles in muscle cells requires microtubules and kinesin. Hum. Mol. Genet. 2013, 23(7):1677-1686.
    • (2013) Hum. Mol. Genet. , vol.23 , Issue.7 , pp. 1677-1686
    • McDade, J.R.1    Michele, D.E.2
  • 52
    • 84865196224 scopus 로고    scopus 로고
    • Sarcolemmal repair is a slow process and includes EHD2
    • Marg A., et al. Sarcolemmal repair is a slow process and includes EHD2. Traffic 2012, 13(9):1286-1294.
    • (2012) Traffic , vol.13 , Issue.9 , pp. 1286-1294
    • Marg, A.1
  • 53
    • 77949696020 scopus 로고    scopus 로고
    • Mucolipins: Intracellular TRPML1-3 channels
    • Cheng X., et al. Mucolipins: Intracellular TRPML1-3 channels. FEBS Lett. 2010, 584(10):2013-2021.
    • (2010) FEBS Lett. , vol.584 , Issue.10 , pp. 2013-2021
    • Cheng, X.1
  • 54
    • 84863317314 scopus 로고    scopus 로고
    • Role of TRPML and two-pore channels in endolysosomal cation homeostasis
    • Grimm C., et al. Role of TRPML and two-pore channels in endolysosomal cation homeostasis. J. Pharmacol. Exp. Ther. 2012, 342(2):236-244.
    • (2012) J. Pharmacol. Exp. Ther. , vol.342 , Issue.2 , pp. 236-244
    • Grimm, C.1
  • 55
    • 79955052958 scopus 로고    scopus 로고
    • Role of TRP channels in the regulation of the endosomal pathway
    • Abe K., Puertollano R. Role of TRP channels in the regulation of the endosomal pathway. Physiology (Bethesda) 2011, 26(1):14-22.
    • (2011) Physiology (Bethesda) , vol.26 , Issue.1 , pp. 14-22
    • Abe, K.1    Puertollano, R.2
  • 56
    • 0034641869 scopus 로고    scopus 로고
    • Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel
    • Sun M., et al. Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel. Hum. Mol. Genet. 2000, 9(17):2471-2478.
    • (2000) Hum. Mol. Genet. , vol.9 , Issue.17 , pp. 2471-2478
    • Sun, M.1
  • 57
    • 0033760264 scopus 로고    scopus 로고
    • Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV
    • Bassi M.T., et al. Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV. Am. J. Hum. Genet. 2000, 67(5):1110-1120.
    • (2000) Am. J. Hum. Genet. , vol.67 , Issue.5 , pp. 1110-1120
    • Bassi, M.T.1
  • 58
    • 0033822172 scopus 로고    scopus 로고
    • Identification of the gene causing mucolipidosis type IV
    • Bargal R., et al. Identification of the gene causing mucolipidosis type IV. Nat. Genet. 2000, 26(1):118-123.
    • (2000) Nat. Genet. , vol.26 , Issue.1 , pp. 118-123
    • Bargal, R.1
  • 59
    • 80051473235 scopus 로고    scopus 로고
    • PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca (2+) release channels in the endolysosome
    • Dong X.P., et al. PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca (2+) release channels in the endolysosome. Nat. Commun. 2010, 1:p38.
    • (2010) Nat. Commun. , vol.1 , pp. p38
    • Dong, X.P.1
  • 60
    • 84863922724 scopus 로고    scopus 로고
    • Phosphoinositide isoforms determine compartment-specific ion channel activity
    • Zhang X., Li X., Xu H. Phosphoinositide isoforms determine compartment-specific ion channel activity. Proc. Natl. Acad. Sci. U.S.A. 2012, 109(28):11384-11389.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , Issue.28 , pp. 11384-11389
    • Zhang, X.1    Li, X.2    Xu, H.3
  • 61
    • 77049105199 scopus 로고    scopus 로고
    • Small molecule activators of TRPML3
    • Grimm C., et al. Small molecule activators of TRPML3. Chem. Biol. 2010, 17(2):135-148.
    • (2010) Chem. Biol. , vol.17 , Issue.2 , pp. 135-148
    • Grimm, C.1
  • 62
    • 84925324770 scopus 로고    scopus 로고
    • Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation
    • Wang W., et al. Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation. Proc. Natl. Acad. Sci. U.S.A. 2015, 112(11):E1373-E1381.
    • (2015) Proc. Natl. Acad. Sci. U.S.A. , vol.112 , Issue.11 , pp. E1373-E1381
    • Wang, W.1
  • 63
    • 79956070911 scopus 로고    scopus 로고
    • Pairing phosphoinositides with calcium ions in endolysosomal dynamics: phosphoinositides control the direction and specificity of membrane trafficking by regulating the activity of calcium channels in the endolysosomes
    • Shen D., Wang X., Xu H. Pairing phosphoinositides with calcium ions in endolysosomal dynamics: phosphoinositides control the direction and specificity of membrane trafficking by regulating the activity of calcium channels in the endolysosomes. Bioessays 2011, 33(6):448-457.
    • (2011) Bioessays , vol.33 , Issue.6 , pp. 448-457
    • Shen, D.1    Wang, X.2    Xu, H.3
  • 64
    • 43049139220 scopus 로고    scopus 로고
    • Lysosomal trafficking functions of mucolipin-1 in murine macrophages
    • Thompson E.G., et al. Lysosomal trafficking functions of mucolipin-1 in murine macrophages. BMC Cell Biol. 2007, 8:p54.
    • (2007) BMC Cell Biol. , vol.8 , pp. p54
    • Thompson, E.G.1
  • 65
    • 49649089300 scopus 로고    scopus 로고
    • Autophagic dysfunction in mucolipidosis type IV patients
    • Vergarajauregui S., et al. Autophagic dysfunction in mucolipidosis type IV patients. Hum. Mol. Genet. 2008, 17(17):2723-2737.
    • (2008) Hum. Mol. Genet. , vol.17 , Issue.17 , pp. 2723-2737
    • Vergarajauregui, S.1
  • 66
    • 70450236985 scopus 로고    scopus 로고
    • Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis
    • Dong X.P., et al. Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis. J. Biol. Chem. 2009, 284(46):32040-32052.
    • (2009) J. Biol. Chem. , vol.284 , Issue.46 , pp. 32040-32052
    • Dong, X.P.1
  • 67
    • 84884154195 scopus 로고    scopus 로고
    • A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis
    • Samie M., et al. A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis. Dev. Cell 2013, 26(5):511-524.
    • (2013) Dev. Cell , vol.26 , Issue.5 , pp. 511-524
    • Samie, M.1
  • 68
    • 42449103570 scopus 로고    scopus 로고
    • A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype
    • Kim H.J., et al. A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype. EMBO J. 2008, 27(8):1197-1205.
    • (2008) EMBO J. , vol.27 , Issue.8 , pp. 1197-1205
    • Kim, H.J.1
  • 69
    • 84930413971 scopus 로고    scopus 로고
    • A TRP channel senses lysosome neutralization by pathogens to trigger their expulsion
    • Miao Y., et al. A TRP channel senses lysosome neutralization by pathogens to trigger their expulsion. Cell 2015, 161(6):1306-1319.
    • (2015) Cell , vol.161 , Issue.6 , pp. 1306-1319
    • Miao, Y.1
  • 70
    • 84867332863 scopus 로고    scopus 로고
    • Autophosphorylation of the C2 domain inhibits translocation of the novel protein kinase C (nPKC) Apl II
    • Farah C.A., et al. Autophosphorylation of the C2 domain inhibits translocation of the novel protein kinase C (nPKC) Apl II. J. Neurochem. 2012, 123(3):360-372.
    • (2012) J. Neurochem. , vol.123 , Issue.3 , pp. 360-372
    • Farah, C.A.1
  • 72
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: why so many?
    • Sudhof T.C. Synaptotagmins: why so many?. J. Biol. Chem. 2002, 277(10):7629-7632.
    • (2002) J. Biol. Chem. , vol.277 , Issue.10 , pp. 7629-7632
    • Sudhof, T.C.1
  • 75
    • 62549102934 scopus 로고    scopus 로고
    • Arabidopsis synaptotagmin 1 is required for the maintenance of plasma membrane integrity and cell viability
    • Schapire A.L., et al. Arabidopsis synaptotagmin 1 is required for the maintenance of plasma membrane integrity and cell viability. Plant Cell 2008, 20(12):3374-3388.
    • (2008) Plant Cell , vol.20 , Issue.12 , pp. 3374-3388
    • Schapire, A.L.1
  • 76
    • 0033603575 scopus 로고    scopus 로고
    • The subcellular localizations of atypical synaptotagmins III and VI, synaptotagmin III is enriched in synapses and synaptic plasma membranes but not in synaptic vesicles
    • Butz S., et al. The subcellular localizations of atypical synaptotagmins III and VI, synaptotagmin III is enriched in synapses and synaptic plasma membranes but not in synaptic vesicles. J. Biol. Chem. 1999, 274(26):18290-18296.
    • (1999) J. Biol. Chem. , vol.274 , Issue.26 , pp. 18290-18296
    • Butz, S.1
  • 77
    • 0030222771 scopus 로고    scopus 로고
    • Synaptotagmins: C2-domain proteins that regulate membrane traffic
    • Sudhof T.C., Rizo J. Synaptotagmins: C2-domain proteins that regulate membrane traffic. Neuron 1996, 17(3):379-388.
    • (1996) Neuron , vol.17 , Issue.3 , pp. 379-388
    • Sudhof, T.C.1    Rizo, J.2
  • 78
    • 2442584514 scopus 로고    scopus 로고
    • Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis
    • Rao S.K., et al. Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis. J. Biol. Chem. 2004, 279(19):20471-20479.
    • (2004) J. Biol. Chem. , vol.279 , Issue.19 , pp. 20471-20479
    • Rao, S.K.1
  • 80
    • 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
    • Jimenez J.L., Bashir R. 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. 2007, 260(1-2):114-123.
    • (2007) J. Neurol. Sci. , vol.260 , Issue.1-2 , pp. 114-123
    • Jimenez, J.L.1    Bashir, R.2
  • 81
    • 0034665195 scopus 로고    scopus 로고
    • The third human FER-1-like protein is highly similar to dysferlin
    • Britton S., et al. The third human FER-1-like protein is highly similar to dysferlin. Genomics 2000, 68(3):313-321.
    • (2000) Genomics , vol.68 , Issue.3 , pp. 313-321
    • Britton, S.1
  • 82
    • 0030972880 scopus 로고    scopus 로고
    • A nematode gene required for sperm vesicle fusion
    • Achanzar W.E., Ward S. A nematode gene required for sperm vesicle fusion. J. Cell Sci. 1997, 110(Pt 9):1073-1081.
    • (1997) J. Cell Sci. , vol.110 , pp. 1073-1081
    • Achanzar, W.E.1    Ward, S.2
  • 83
    • 77955001359 scopus 로고    scopus 로고
    • Phylogenetic analysis of ferlin genes reveals ancient eukaryotic origins
    • Lek A., et al. Phylogenetic analysis of ferlin genes reveals ancient eukaryotic origins. BMC Evol. Biol. 2010, 10:p231.
    • (2010) BMC Evol. Biol. , vol.10 , pp. p231
    • Lek, A.1
  • 84
    • 34548009359 scopus 로고    scopus 로고
    • Dysferlin and muscle membrane repair
    • Han R., Campbell K.P. Dysferlin and muscle membrane repair. Curr. Opin. Cell Biol. 2007, 19(4):409-416.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , Issue.4 , pp. 409-416
    • Han, R.1    Campbell, K.P.2
  • 85
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: structural and functional diversity
    • Nalefski E.A., Falke J.J. The C2 domain calcium-binding motif: structural and functional diversity. Prot. Sci. 1996, 5(12):2375-2390.
    • (1996) Prot. Sci. , vol.5 , Issue.12 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 86
    • 0035109410 scopus 로고    scopus 로고
    • Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype
    • Illa I., et al. Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype. Ann. Neurol. 2001, 49(1):130-134.
    • (2001) Ann. Neurol. , vol.49 , Issue.1 , pp. 130-134
    • Illa, I.1
  • 87
    • 17344363640 scopus 로고    scopus 로고
    • A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B
    • Bashir R., et al. A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B. Nat. Genet. 1998, 20(1):37-42.
    • (1998) Nat. Genet. , vol.20 , Issue.1 , pp. 37-42
    • Bashir, R.1
  • 88
    • 17344365600 scopus 로고    scopus 로고
    • Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy
    • Liu J., et al. Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nat. Genet. 1998, 20(1):31-36.
    • (1998) Nat. Genet. , vol.20 , Issue.1 , pp. 31-36
    • Liu, J.1
  • 89
    • 0037738510 scopus 로고    scopus 로고
    • Defective membrane repair in dysferlin-deficient muscular dystrophy
    • Bansal D., et al. Defective membrane repair in dysferlin-deficient muscular dystrophy. Nature 2003, 423(6936):168-172.
    • (2003) Nature , vol.423 , Issue.6936 , pp. 168-172
    • Bansal, D.1
  • 90
    • 0037151075 scopus 로고    scopus 로고
    • Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains
    • Davis D.B., et al. Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains. J. Biol. Chem. 2002, 277(25):22883-22888.
    • (2002) J. Biol. Chem. , vol.277 , Issue.25 , pp. 22883-22888
    • Davis, D.B.1
  • 91
    • 84877096510 scopus 로고    scopus 로고
    • Calpains, cleaved mini-dysferlinC72, and L-type channels underpin calcium-dependent muscle membrane repair
    • Lek A., et al. Calpains, cleaved mini-dysferlinC72, and L-type channels underpin calcium-dependent muscle membrane repair. J. Neurosci. 2013, 33(12):5085-5094.
    • (2013) J. Neurosci. , vol.33 , Issue.12 , pp. 5085-5094
    • Lek, A.1
  • 92
    • 84929233022 scopus 로고    scopus 로고
    • Calpain cleavage within dysferlin exon 40a releases a synaptotagmin-like module for membrane repair
    • Redpath G.M., et al. Calpain cleavage within dysferlin exon 40a releases a synaptotagmin-like module for membrane repair. Mol. Biol. Cell 2014, 25(19):3037-3048.
    • (2014) Mol. Biol. Cell , vol.25 , Issue.19 , pp. 3037-3048
    • Redpath, G.M.1
  • 93
    • 31144438673 scopus 로고    scopus 로고
    • Normal myoblast fusion requires myoferlin
    • Doherty K.R., et al. Normal myoblast fusion requires myoferlin. Development 2005, 132(24):5565-5575.
    • (2005) Development , vol.132 , Issue.24 , pp. 5565-5575
    • Doherty, K.R.1
  • 94
    • 0033972161 scopus 로고    scopus 로고
    • Myoferlin, a candidate gene and potential modifier of muscular dystrophy
    • Davis D.B., et al. Myoferlin, a candidate gene and potential modifier of muscular dystrophy. Hum. Mol. Genet. 2000, 9(2):217-226.
    • (2000) Hum. Mol. Genet. , vol.9 , Issue.2 , pp. 217-226
    • Davis, D.B.1
  • 95
    • 77954946990 scopus 로고    scopus 로고
    • Myoferlin regulation by NFAT in muscle injury, regeneration and repair
    • Demonbreun A.R., et al. Myoferlin regulation by NFAT in muscle injury, regeneration and repair. J. Cell Sci. 2010, 123(Pt 14):2413-2422.
    • (2010) J. Cell Sci. , vol.123 , pp. 2413-2422
    • Demonbreun, A.R.1
  • 98
    • 17644420707 scopus 로고    scopus 로고
    • Domain architecture of the smooth-muscle plasma membrane: regulation by annexins
    • Draeger A., Wray S., Babiychuk E.B. Domain architecture of the smooth-muscle plasma membrane: regulation by annexins. Biochem. J. 2005, 387(Pt 2):309-314.
    • (2005) Biochem. J. , vol.387 , pp. 309-314
    • Draeger, A.1    Wray, S.2    Babiychuk, E.B.3
  • 99
    • 0027858897 scopus 로고
    • Immunocytochemical localization of annexins V and VI in human placentae of different gestational ages
    • Rambotti M.G., Spreca A., Donato R. Immunocytochemical localization of annexins V and VI in human placentae of different gestational ages. Cell Mol. Biol. Res. 1993, 39(6):579-588.
    • (1993) Cell Mol. Biol. Res. , vol.39 , Issue.6 , pp. 579-588
    • Rambotti, M.G.1    Spreca, A.2    Donato, R.3
  • 100
    • 0030918361 scopus 로고    scopus 로고
    • Localization of five annexins in J774 macrophages and on isolated phagosomes
    • Diakonova M., et al. Localization of five annexins in J774 macrophages and on isolated phagosomes. J. Cell Sci. 1997, 110(Pt 10):1199-1213.
    • (1997) J. Cell Sci. , vol.110 , pp. 1199-1213
    • Diakonova, M.1
  • 101
    • 0344012479 scopus 로고    scopus 로고
    • The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes
    • Zobiack N., et al. The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes. Mol. Biol. Cell 2003, 14(12):4896-4908.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.12 , pp. 4896-4908
    • Zobiack, N.1
  • 102
    • 0037926403 scopus 로고    scopus 로고
    • Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells
    • Mayran N., Parton R.G., Gruenberg J. Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells. EMBO J. 2003, 22(13):3242-3253.
    • (2003) EMBO J. , vol.22 , Issue.13 , pp. 3242-3253
    • Mayran, N.1    Parton, R.G.2    Gruenberg, J.3
  • 103
    • 0033126054 scopus 로고    scopus 로고
    • Endocytic vesicles move at the tips of actin tails in cultured mast cells
    • Merrifield C.J., et al. Endocytic vesicles move at the tips of actin tails in cultured mast cells. Nat. Cell Biol. 1999, 1(1):72-74.
    • (1999) Nat. Cell Biol. , vol.1 , Issue.1 , pp. 72-74
    • Merrifield, C.J.1
  • 104
    • 84858198502 scopus 로고    scopus 로고
    • In vivo imaging of molecular interactions at damaged sarcolemma
    • Roostalu U., Strahle U. In vivo imaging of molecular interactions at damaged sarcolemma. Dev. Cell 2012, 22(3):515-529.
    • (2012) Dev. Cell , vol.22 , Issue.3 , pp. 515-529
    • Roostalu, U.1    Strahle, U.2
  • 105
    • 84924431318 scopus 로고    scopus 로고
    • Annexin-A5 promotes membrane resealing in human trophoblasts
    • Carmeille R., et al. Annexin-A5 promotes membrane resealing in human trophoblasts. Biochim. Biophys. Acta 2015, 1853(9):2033-2044.
    • (2015) Biochim. Biophys. Acta , vol.1853 , Issue.9 , pp. 2033-2044
    • Carmeille, R.1
  • 106
    • 0033535982 scopus 로고    scopus 로고
    • 2+-binding proteins
    • 2+-binding proteins. Biochemistry 1999, 38(23):7498-7508.
    • (1999) Biochemistry , vol.38 , Issue.23 , pp. 7498-7508
    • Lo, K.W.1
  • 107
    • 0033043513 scopus 로고    scopus 로고
    • Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein
    • Missotten M., et al. Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. Cell Death Differ. 1999, 6(2):124-129.
    • (1999) Cell Death Differ. , vol.6 , Issue.2 , pp. 124-129
    • Missotten, M.1
  • 108
    • 27744432641 scopus 로고    scopus 로고
    • The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B
    • Katoh K., et al. The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B. Biochem. J. 2005, 391(Pt 3):677-685.
    • (2005) Biochem. J. , vol.391 , pp. 677-685
    • Katoh, K.1
  • 109
    • 0036296413 scopus 로고    scopus 로고
    • ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner
    • Satoh H., et al. ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner. Biochem. Biophys. Res. Commun. 2002, 291(5):1166-1172.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , Issue.5 , pp. 1166-1172
    • Satoh, H.1
  • 110
    • 0037020677 scopus 로고    scopus 로고
    • 2+-dependent manner
    • 2+-dependent manner. Biochim. Biophys. Acta 2002, 1600(1-2):61-67.
    • (2002) Biochim. Biophys. Acta , vol.1600 , Issue.1-2 , pp. 61-67
    • Satoh, H.1
  • 111
    • 2442651872 scopus 로고    scopus 로고
    • ALG-2, a multifunctional calcium binding protein?
    • Tarabykina S., et al. ALG-2, a multifunctional calcium binding protein?. Front. Biosci. 2004, 9:1817-1832.
    • (2004) Front. Biosci. , vol.9 , pp. 1817-1832
    • Tarabykina, S.1
  • 112
    • 84906544287 scopus 로고    scopus 로고
    • Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: a potential effector pathway for luminal calcium
    • Helm J.R., et al. Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: a potential effector pathway for luminal calcium. J. Biol. Chem. 2014, 289(34):23609-23628.
    • (2014) J. Biol. Chem. , vol.289 , Issue.34 , pp. 23609-23628
    • Helm, J.R.1
  • 114
    • 82755189495 scopus 로고    scopus 로고
    • Calpains: an elaborate proteolytic system
    • Ono Y., Sorimachi H. Calpains: an elaborate proteolytic system. Biochim. Biophys. Acta 2012, 1824(1):224-236.
    • (2012) Biochim. Biophys. Acta , vol.1824 , Issue.1 , pp. 224-236
    • Ono, Y.1    Sorimachi, H.2
  • 115
    • 84900524773 scopus 로고    scopus 로고
    • Genetic basis of limb-girdle muscular dystrophies: the 2014 update
    • Nigro V., Savarese M. Genetic basis of limb-girdle muscular dystrophies: the 2014 update. Acta Myol. 2014, 33(1):1-12.
    • (2014) Acta Myol. , vol.33 , Issue.1 , pp. 1-12
    • Nigro, V.1    Savarese, M.2
  • 116
    • 0026006196 scopus 로고
    • 2+)-triggered protease activity and cytoskeletal disassembly
    • 2+)-triggered protease activity and cytoskeletal disassembly. J. Neurosci. 1991, 11(10):3257-3267.
    • (1991) J. Neurosci. , vol.11 , Issue.10 , pp. 3257-3267
    • Xie, X.Y.1    Barrett, J.N.2
  • 117
    • 0030902594 scopus 로고    scopus 로고
    • Calpain activity promotes the sealing of severed giant axons
    • Godell C.M., et al. Calpain activity promotes the sealing of severed giant axons. Proc. Natl. Acad. Sci. U.S.A. 1997, 94(9):4751-4756.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , Issue.9 , pp. 4751-4756
    • Godell, C.M.1
  • 118
    • 34047273570 scopus 로고    scopus 로고
    • Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane
    • Mellgren R.L., et al. Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane. J. Biol. Chem. 2007, 282(4):2567-2575.
    • (2007) J. Biol. Chem. , vol.282 , Issue.4 , pp. 2567-2575
    • Mellgren, R.L.1
  • 119
    • 71749109832 scopus 로고    scopus 로고
    • Calcium-dependent plasma membrane repair requires m- or mu-calpain, but not calpain-3, the proteasome, or caspases
    • Mellgren R.L., et al. Calcium-dependent plasma membrane repair requires m- or mu-calpain, but not calpain-3, the proteasome, or caspases. Biochim. Biophys. Acta 2009, 1793(12):1886-1893.
    • (2009) Biochim. Biophys. Acta , vol.1793 , Issue.12 , pp. 1886-1893
    • Mellgren, R.L.1
  • 120
    • 66149160256 scopus 로고    scopus 로고
    • TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals
    • Stohr H., et al. TMEM16B, a novel protein with calcium-dependent chloride channel activity, associates with a presynaptic protein complex in photoreceptor terminals. J. Neurosci. 2009, 29(21):6809-6818.
    • (2009) J. Neurosci. , vol.29 , Issue.21 , pp. 6809-6818
    • Stohr, H.1
  • 121
    • 55249091085 scopus 로고    scopus 로고
    • TMEM16A confers receptor-activated calcium-dependent chloride conductance
    • Yang Y.D., et al. TMEM16A confers receptor-activated calcium-dependent chloride conductance. Nature 2008, 455(7217):1210-1215.
    • (2008) Nature , vol.455 , Issue.7217 , pp. 1210-1215
    • Yang, Y.D.1
  • 122
    • 51549120559 scopus 로고    scopus 로고
    • Expression cloning of TMEM16A as a calcium-activated chloride channel subunit
    • Schroeder B.C., et al. Expression cloning of TMEM16A as a calcium-activated chloride channel subunit. Cell 2008, 134(6):1019-1029.
    • (2008) Cell , vol.134 , Issue.6 , pp. 1019-1029
    • Schroeder, B.C.1
  • 123
    • 54949112835 scopus 로고    scopus 로고
    • TMEM16A, a membrane protein associated with calcium-dependent chloride channel activity
    • Caputo A., et al. TMEM16A, a membrane protein associated with calcium-dependent chloride channel activity. Science 2008, 322(5901):590-594.
    • (2008) Science , vol.322 , Issue.5901 , pp. 590-594
    • Caputo, A.1
  • 124
    • 65749107370 scopus 로고    scopus 로고
    • 2+-activated Cl-channels
    • 2+-activated Cl-channels. J. Physiol. 2009, 587(Pt 10):2127-2139.
    • (2009) J. Physiol. , vol.587 , pp. 2127-2139
    • Hartzell, H.C.1
  • 125
    • 70350398260 scopus 로고    scopus 로고
    • TMEM16 proteins produce volume-regulated chloride currents that are reduced in mice lacking TMEM16A
    • Almaca J., et al. TMEM16 proteins produce volume-regulated chloride currents that are reduced in mice lacking TMEM16A. J. Biol. Chem. 2009, 284(42):28571-28578.
    • (2009) J. Biol. Chem. , vol.284 , Issue.42 , pp. 28571-28578
    • Almaca, J.1
  • 126
    • 33644628177 scopus 로고    scopus 로고
    • Phylogeny of the TMEM16 protein family: some members are overexpressed in cancer
    • Galindo B.E., Vacquier V.D. Phylogeny of the TMEM16 protein family: some members are overexpressed in cancer. Int. J. Mol. Med. 2005, 16(5):919-924.
    • (2005) Int. J. Mol. Med. , vol.16 , Issue.5 , pp. 919-924
    • Galindo, B.E.1    Vacquier, V.D.2
  • 127
    • 34147113231 scopus 로고    scopus 로고
    • Molecular characterization of GDD1/TMEM16E, the gene product responsible for autosomal dominant gnathodiaphyseal dysplasia
    • Mizuta K., et al. Molecular characterization of GDD1/TMEM16E, the gene product responsible for autosomal dominant gnathodiaphyseal dysplasia. Biochem. Biophys. Res. Commun. 2007, 357(1):126-132.
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , Issue.1 , pp. 126-132
    • Mizuta, K.1
  • 128
    • 84856292939 scopus 로고    scopus 로고
    • ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular proteins
    • Duran C., et al. ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular proteins. Am. J. Physiol. Cell Physiol. 2012, 302(3):C482-C493.
    • (2012) Am. J. Physiol. Cell Physiol. , vol.302 , Issue.3 , pp. C482-C493
    • Duran, C.1


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