메뉴 건너뛰기




Volumn 4, Issue SEP, 2013, Pages

The functional significance of synaptotagmin diversity in neuroendocrine secretion

Author keywords

Calcium; Dense core vesicle; Exocytosis; Fusion pores; Insulin; Kiss and run; Neuropeptides; Norepinephrine

Indexed keywords


EID: 84886068895     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2013.00124     Document Type: Short Survey
Times cited : (68)

References (91)
  • 1
    • 0025309605 scopus 로고
    • Pathways to regulated exocytosis in neurons
    • doi:10.1146/annurev.ph.52.030190.003205
    • De Camilli P, Jahn R. Pathways to regulated exocytosis in neurons. Annu Rev Physiol (1990) 52:625-45. doi:10.1146/annurev.ph.52.030190.003205.
    • (1990) Annu Rev Physiol , vol.52 , pp. 625-645
    • De Camilli, P.1    Jahn, R.2
  • 4
    • 77957343236 scopus 로고    scopus 로고
    • Proteomics of dense core secretory vesicles reveal distinct protein categories for secretion of neuroeffectors for cell-cell communication
    • doi:10.1021/pr1003104
    • Wegrzyn JL, Bark SJ, Funkelstein L, Mosier C, Yap A, Kazemi-Esfarjani P, et al. Proteomics of dense core secretory vesicles reveal distinct protein categories for secretion of neuroeffectors for cell-cell communication. J Proteome Res (2010) 9:5002-24. doi:10.1021/pr1003104.
    • (2010) J Proteome Res , vol.9 , pp. 5002-5024
    • Wegrzyn, J.L.1    Bark, S.J.2    Funkelstein, L.3    Mosier, C.4    Yap, A.5    Kazemi-Esfarjani, P.6
  • 5
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion:grappling with SNARE and SM proteins
    • doi:10.1126/science.1161748
    • Sudhof TC, Rothman JE. Membrane fusion:grappling with SNARE and SM proteins. Science (2009) 323:474-7. doi:10.1126/science.1161748.
    • (2009) Science , vol.323 , pp. 474-477
    • Sudhof, T.C.1    Rothman, J.E.2
  • 6
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs-engines for membrane fusion
    • doi:10.1038/nrm2002
    • Jahn R, Scheller RH. SNAREs-engines for membrane fusion. Nat Rev Mol Cell Biol (2006) 7:631-43. doi:10.1038/nrm2002.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 7
    • 84867295592 scopus 로고    scopus 로고
    • Molecular machines governing exocytosis of synaptic vesicles
    • doi:10.1038/nature11320
    • Jahn R, Fasshauer D. Molecular machines governing exocytosis of synaptic vesicles. Nature (2012) 490:201-7. doi:10.1038/nature11320.
    • (2012) Nature , vol.490 , pp. 201-207
    • Jahn, R.1    Fasshauer, D.2
  • 8
    • 0043161982 scopus 로고    scopus 로고
    • Tuning exocytosis for speed:fast and slow modes
    • doi:10.1016/S0167-4889(03)00093-4
    • Martin TF. Tuning exocytosis for speed:fast and slow modes. Biochim Biophys Acta (2003) 1641:157-65. doi:10.1016/S0167-4889(03)00093-4.
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 157-165
    • Martin, T.F.1
  • 9
    • 0018967377 scopus 로고
    • The molecular organization of adrenal chromaffin granules
    • doi:10.1016/0306-4522(80)90031-7
    • Winkler H, Westhead E. The molecular organization of adrenal chromaffin granules. Neuroscience (1980) 5:1803-23. doi:10.1016/0306-4522(80)90031-7.
    • (1980) Neuroscience , vol.5 , pp. 1803-1823
    • Winkler, H.1    Westhead, E.2
  • 11
    • 23744436392 scopus 로고    scopus 로고
    • Activity-dependent differential transmitter release in mouse adrenal chromaffin cells
    • doi:10.1523/JNEUROSCI.2042-05.2005
    • Fulop T, Radabaugh S, Smith C. Activity-dependent differential transmitter release in mouse adrenal chromaffin cells. J Neurosci (2005) 25:7324-32. doi:10.1523/JNEUROSCI.2042-05.2005.
    • (2005) J Neurosci , vol.25 , pp. 7324-7332
    • Fulop, T.1    Radabaugh, S.2    Smith, C.3
  • 12
    • 33748946239 scopus 로고    scopus 로고
    • Release of small transmitters through kiss-and-run fusion pores in rat pancreatic beta cells
    • doi:10.1016/j.cmet.2006.08.011
    • MacDonald PE, Braun M, Galvanovskis J, Rorsman P. Release of small transmitters through kiss-and-run fusion pores in rat pancreatic beta cells. Cell Metab (2006) 4:283-90. doi:10.1016/j.cmet.2006.08.011.
    • (2006) Cell Metab , vol.4 , pp. 283-290
    • MacDonald, P.E.1    Braun, M.2    Galvanovskis, J.3    Rorsman, P.4
  • 13
    • 33745773331 scopus 로고    scopus 로고
    • Near simultaneous release of classical and peptide cotransmitters from chromaffin cells
    • doi:10.1523/JNEUROSCI.5100-05.2006
    • Whim MD. Near simultaneous release of classical and peptide cotransmitters from chromaffin cells. J Neurosci (2006) 26:6637-42. doi:10.1523/JNEUROSCI.5100-05.2006.
    • (2006) J Neurosci , vol.26 , pp. 6637-6642
    • Whim, M.D.1
  • 14
    • 50649106484 scopus 로고    scopus 로고
    • Prothyrotropin-releasing hormone targets its processing products to different vesicles of the secretory pathway
    • doi:10.1074/jbc. M800732200
    • Perello M, Stuart R, Nillni EA. Prothyrotropin-releasing hormone targets its processing products to different vesicles of the secretory pathway. J Biol Chem (2008) 283:19936-47. doi:10.1074/jbc. M800732200.
    • (2008) J Biol Chem , vol.283 , pp. 19936-47
    • Perello, M.1    Stuart, R.2    Nillni, E.A.3
  • 15
    • 0026168519 scopus 로고
    • Biosynthesis and sorting of neuropeptides
    • doi:10.1016/0959-4388(91)90013-W
    • Sossin WS, Scheller RH. Biosynthesis and sorting of neuropeptides. Curr Opin Neurobiol (1991) 1:79-83. doi:10.1016/0959-4388(91)90013-W.
    • (1991) Curr Opin Neurobiol , vol.1 , pp. 79-83
    • Sossin, W.S.1    Scheller, R.H.2
  • 16
    • 0027238820 scopus 로고
    • Release of secretory products during transient vesicle fusion
    • doi:10.1038/363554a0
    • Alvarez de Toledo G, Fernández-Chacón R, Fernández JM. Release of secretory products during transient vesicle fusion. Nature (1993) 363:554-8. doi:10.1038/363554a0.
    • (1993) Nature , vol.363 , pp. 554-558
    • Alvarez de Toledo, G.1    Fernández-Chacón, R.2    Fernández, J.M.3
  • 17
    • 0021687960 scopus 로고
    • Capacitance measurements reveal stepwise fusion events in degranulating mast cells
    • doi:10.1038/312453a0
    • Fernandez JM, Neher E, Gomperts BD. Capacitance measurements reveal stepwise fusion events in degranulating mast cells. Nature (1984) 312:453-5. doi:10.1038/312453a0.
    • (1984) Nature , vol.312 , pp. 453-455
    • Fernandez, J.M.1    Neher, E.2    Gomperts, B.D.3
  • 18
    • 0037019347 scopus 로고    scopus 로고
    • Capacitance steps and fusion pores of small and large-dense-core vesicles in nerve terminals
    • doi:10.1038/nature00852
    • Klyachko VA, Jackson MB. Capacitance steps and fusion pores of small and large-dense-core vesicles in nerve terminals. Nature (2002) 418:89-92. doi:10.1038/nature00852.
    • (2002) Nature , vol.418 , pp. 89-92
    • Klyachko, V.A.1    Jackson, M.B.2
  • 19
    • 0013657423 scopus 로고
    • Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells
    • doi:10.1073/pnas.79.21.6712
    • Neher E, Marty A. Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells. Proc Natl Acad Sci U S A (1982) 79:6712-6. doi:10.1073/pnas.79.21.6712.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 6712-6716
    • Neher, E.1    Marty, A.2
  • 21
    • 0035368680 scopus 로고    scopus 로고
    • How does calcium trigger neurotransmitter release?
    • doi:10.1016/S0959-4388(00)00214-2
    • Augustine GJ. How does calcium trigger neurotransmitter release? Curr Opin Neurobiol (2001) 11:320-6. doi:10.1016/S0959-4388(00)00214-2.
    • (2001) Curr Opin Neurobiol , vol.11 , pp. 320-326
    • Augustine, G.J.1
  • 22
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • doi:10.1146/annurev.biochem.77.062005.101135
    • Chapman ER. How does synaptotagmin trigger neurotransmitter release? Annu Rev Biochem (2008) 77:615-41. doi:10.1146/annurev.biochem.77.062005.101135.
    • (2008) Annu Rev Biochem , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 23
    • 0141960930 scopus 로고    scopus 로고
    • Synaptotagmin I, a Ca2+ sensor for neurotransmitter release
    • doi:10.1016/S0166-2236(03)00195-4
    • Koh TW, Bellen HJ. Synaptotagmin I, a Ca2+ sensor for neurotransmitter release. Trends Neurosci (2003) 26:413-22. doi:10.1016/S0166-2236(03)00195-4.
    • (2003) Trends Neurosci , vol.26 , pp. 413-422
    • Koh, T.W.1    Bellen, H.J.2
  • 24
    • 0033126053 scopus 로고    scopus 로고
    • High calcium concentrations shift the mode of exocytosis to the kiss-and-run mechanism
    • doi:10.1038/9012
    • Ales E, Tabares L, Poyato JM, Valero V, Lindau M, Alvarez de Toledo G. High calcium concentrations shift the mode of exocytosis to the kiss-and-run mechanism. Nat Cell Biol (1999) 1:40-4. doi:10.1038/9012.
    • (1999) Nat Cell Biol , vol.1 , pp. 40-44
    • Ales, E.1    Tabares, L.2    Poyato, J.M.3    Valero, V.4    Lindau, M.5    Alvarez de Toledo, G.6
  • 25
    • 0028906872 scopus 로고
    • Cytosolic calcium facilitates release of secretory products after exocytotic vesicle fusion
    • doi:10.1016/0014-5793(95)00319-5
    • Fernandez-Chacon R, Alvarez de Toledo G. Cytosolic calcium facilitates release of secretory products after exocytotic vesicle fusion. FEBS Lett (1995) 363:221-5. doi:10.1016/0014-5793(95)00319-5.
    • (1995) FEBS Lett , vol.363 , pp. 221-225
    • Fernandez-Chacon, R.1    Alvarez de Toledo, G.2
  • 26
    • 33644865767 scopus 로고    scopus 로고
    • 2+ triggers two sequential steps in regulated exocytosis in rat PC12 cells:fusion pore opening and fusion pore dilation
    • 2+ triggers two sequential steps in regulated exocytosis in rat PC12 cells:fusion pore opening and fusion pore dilation. J Physiol (2006) 570:295-307.
    • (2006) J Physiol , vol.570 , pp. 295-307
    • Wang, C.T.1    Bai, J.2    Chang, P.Y.3    Chapman, E.R.4    Jackson, M.B.5
  • 27
    • 1842475284 scopus 로고    scopus 로고
    • Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions
    • doi:10.1016/S0896-6273(04)00117-5
    • Bai J, Wang CT, Richards DA, Jackson MB, Chapman ER. Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions. Neuron (2004) 41:929-42. doi:10.1016/S0896-6273(04)00117-5.
    • (2004) Neuron , vol.41 , pp. 929-942
    • Bai, J.1    Wang, C.T.2    Richards, D.A.3    Jackson, M.B.4    Chapman, E.R.5
  • 28
    • 0035798162 scopus 로고    scopus 로고
    • Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles
    • doi:10.1126/science.1064002
    • Wang CT, Grishanin R, Earles CA, Chang PY, Martin TF, Chapman ER, et al. Synaptotagmin modulation of fusion pore kinetics in regulated exocytosis of dense-core vesicles. Science (2001) 294:1111-5. doi:10.1126/science.1064002.
    • (2001) Science , vol.294 , pp. 1111-1115
    • Wang, C.T.1    Grishanin, R.2    Earles, C.A.3    Chang, P.Y.4    Martin, T.F.5    Chapman, E.R.6
  • 29
    • 0041858035 scopus 로고    scopus 로고
    • Different domains of synaptotagmin control the choice between kiss-and-run and full fusion
    • doi:10.1038/nature01857
    • Wang CT, Lu JC, Bai J, Chang PY, Martin TF, Chapman ER, et al. Different domains of synaptotagmin control the choice between kiss-and-run and full fusion. Nature (2003) 424:943-7. doi:10.1038/nature01857.
    • (2003) Nature , vol.424 , pp. 943-947
    • Wang, C.T.1    Lu, J.C.2    Bai, J.3    Chang, P.Y.4    Martin, T.F.5    Chapman, E.R.6
  • 30
    • 77955638309 scopus 로고    scopus 로고
    • Regulation of exocytosis and fusion pores by synaptotagmin-effector interactions
    • doi:10.1091/mbc. E10-04-0285
    • Zhang Z, Hui E, Chapman ER, Jackson MB. Regulation of exocytosis and fusion pores by synaptotagmin-effector interactions. Mol Biol Cell (2010) 21:2821-31. doi:10.1091/mbc. E10-04-0285.
    • (2010) Mol Biol Cell , vol.21 , pp. 2821-2831
    • Zhang, Z.1    Hui, E.2    Chapman, E.R.3    Jackson, M.B.4
  • 31
    • 0037380131 scopus 로고    scopus 로고
    • Multiple forms of "kiss-and-run" exocytosis revealed by evanescent wave microscopy
    • doi:10.1016/S0960-9822(03)00176-3
    • Tsuboi T, Rutter GA. Multiple forms of "kiss-and-run" exocytosis revealed by evanescent wave microscopy. Curr Biol (2003) 13:563-7. doi:10.1016/S0960-9822(03)00176-3.
    • (2003) Curr Biol , vol.13 , pp. 563-567
    • Tsuboi, T.1    Rutter, G.A.2
  • 32
    • 79959896913 scopus 로고    scopus 로고
    • Release mode of large and small dense-core vesicles specified by different synaptotagmin isoforms in PC12 cells
    • doi:10.1091/mbc. E11-02-0159
    • Zhang Z, Wu Y, Wang Z, Dunning FM, Rehfuss J, Ramanan D, et al. Release mode of large and small dense-core vesicles specified by different synaptotagmin isoforms in PC12 cells. Mol Biol Cell (2011) 22:2324-36. doi:10.1091/mbc. E11-02-0159.
    • (2011) Mol Biol Cell , vol.22 , pp. 2324-2336
    • Zhang, Z.1    Wu, Y.2    Wang, Z.3    Dunning, F.M.4    Rehfuss, J.5    Ramanan, D.6
  • 33
    • 34547945659 scopus 로고    scopus 로고
    • Synaptotagmin I and IX function redundantly in controlling fusion pore of large dense core vesicles
    • doi:10.1016/j.bbrc.2007.07.083
    • Zhu D, Zhou W, Liang T, Yang F, Zhang RY, Wu ZX, et al. Synaptotagmin I and IX function redundantly in controlling fusion pore of large dense core vesicles. Biochem Biophys Res Commun (2007) 361:922-7. doi:10.1016/j.bbrc.2007.07.083.
    • (2007) Biochem Biophys Res Commun , vol.361 , pp. 922-927
    • Zhu, D.1    Zhou, W.2    Liang, T.3    Yang, F.4    Zhang, R.Y.5    Wu, Z.X.6
  • 34
    • 0032527312 scopus 로고    scopus 로고
    • Ca2+ binding to synaptotagmin:how many Ca2+ ions bind to the tip of a C2-domain?
    • doi:10.1093/emboj/17.14.3921
    • Ubach J, Zhang X, Shao X, Sudhof TC, Rizo J. Ca2+ binding to synaptotagmin:how many Ca2+ ions bind to the tip of a C2-domain? EMBO J (1998) 17:3921-30. doi:10.1093/emboj/17.14.3921.
    • (1998) EMBO J , vol.17 , pp. 3921-3930
    • Ubach, J.1    Zhang, X.2    Shao, X.3    Sudhof, T.C.4    Rizo, J.5
  • 35
    • 76949098455 scopus 로고    scopus 로고
    • A manual collection of Syt, Esyt, Rph3a, Rph3al, Doc2, and Dblc2 genes from 46 metazoan genomes-an open access resource for neuroscience and evolutionary biology
    • doi:10.1186/1471-2164-11-37
    • Craxton M. A manual collection of Syt, Esyt, Rph3a, Rph3al, Doc2, and Dblc2 genes from 46 metazoan genomes-an open access resource for neuroscience and evolutionary biology. BMC Genomics (2010) 11:37. doi:10.1186/1471-2164-11-37.
    • (2010) BMC Genomics , vol.11 , pp. 37
    • Craxton, M.1
  • 36
    • 0038066072 scopus 로고    scopus 로고
    • Synaptotagmins in membrane traffic:which vesicles do the tagmins tag?
    • doi:10.1016/S0300-9084(00)00220-0
    • Marqueze B, Berton F, Seagar M. Synaptotagmins in membrane traffic:which vesicles do the tagmins tag? Biochimie (2000) 82:409-20. doi:10.1016/S0300-9084(00)00220-0.
    • (2000) Biochimie , vol.82 , pp. 409-420
    • Marqueze, B.1    Berton, F.2    Seagar, M.3
  • 37
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins:why so many?
    • doi:10.1074/jbc. R100052200
    • Sudhof TC. Synaptotagmins:why so many? J Biol Chem (2002) 277:7629-32. doi:10.1074/jbc. R100052200.
    • (2002) J Biol Chem , vol.277 , pp. 7629-7632
    • Sudhof, T.C.1
  • 38
    • 17044369192 scopus 로고    scopus 로고
    • Three distinct kinetic groupings of the synaptotagmin family:candidate sensors for rapid and delayed exocytosis
    • doi:10.1073/pnas.0500941102
    • Hui E, Bai J, Wang P, Sugimori M, Llinas RR, Chapman ER. Three distinct kinetic groupings of the synaptotagmin family:candidate sensors for rapid and delayed exocytosis. Proc Natl Acad Sci U S A (2005) 102:5210-4. doi:10.1073/pnas.0500941102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5210-5214
    • Hui, E.1    Bai, J.2    Wang, P.3    Sugimori, M.4    Llinas, R.R.5    Chapman, E.R.6
  • 39
    • 26244435478 scopus 로고    scopus 로고
    • 2+ concentration to SNARE-mediated membrane fusion
    • doi:10.1091/mbc. E05-04-0277
    • 2+ concentration to SNARE-mediated membrane fusion. Mol Biol Cell (2005) 16:4755-64. doi:10.1091/mbc. E05-04-0277.
    • (2005) Mol Biol Cell , vol.16 , pp. 4755-4764
    • Bhalla, A.1    Tucker, W.C.2    Chapman, E.R.3
  • 40
    • 52049100831 scopus 로고    scopus 로고
    • Analysis of the synaptotagmin family during reconstituted membrane fusion. Uncovering a class of inhibitory isoforms
    • doi:10.1074/jbc. M709628200
    • Bhalla A, Chicka MC, Chapman ER. Analysis of the synaptotagmin family during reconstituted membrane fusion. Uncovering a class of inhibitory isoforms. J Biol Chem (2008) 283:21799-807. doi:10.1074/jbc. M709628200.
    • (2008) J Biol Chem , vol.283 , pp. 21799-807
    • Bhalla, A.1    Chicka, M.C.2    Chapman, E.R.3
  • 41
    • 0028989281 scopus 로고
    • Ca(2+)-dependent and -independent activities of neural and non-neural synaptotagmins
    • doi:10.1038/375594a0
    • Li C, Ullrich B, Zhang JZ, Anderson RG, Brose N, Südhof TC. Ca(2+)-dependent and -independent activities of neural and non-neural synaptotagmins. Nature (1995) 375:594-9. doi:10.1038/375594a0.
    • (1995) Nature , vol.375 , pp. 594-599
    • Li, C.1    Ullrich, B.2    Zhang, J.Z.3    Anderson, R.G.4    Brose, N.5    Südhof, T.C.6
  • 42
    • 0036469818 scopus 로고    scopus 로고
    • Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct Ca(2+) affinities
    • doi:10.1093/emboj/21.3.270
    • Sugita S, Shin OH, Han W, Lao Y, Sudhof TC. Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct Ca(2+) affinities. EMBO J (2002) 21:270-80. doi:10.1093/emboj/21.3.270.
    • (2002) EMBO J , vol.21 , pp. 270-280
    • Sugita, S.1    Shin, O.H.2    Han, W.3    Lao, Y.4    Sudhof, T.C.5
  • 43
    • 0027127386 scopus 로고
    • Neurotransmitter release from synaptotagmin-deficient clonal variants of PC12 cells
    • Shoji-Kasai Y, Yoshida A, Sato K, Hoshino T, Ogura A, Kondo S, et al. Neurotransmitter release from synaptotagmin-deficient clonal variants of PC12 cells. Science (1992) 256:1821-3.
    • (1992) Science , vol.256 , pp. 1821-1823
    • Shoji-Kasai, Y.1    Yoshida, A.2    Sato, K.3    Hoshino, T.4    Ogura, A.5    Kondo, S.6
  • 44
    • 33947312324 scopus 로고    scopus 로고
    • Synaptotagmins I and IX function redundantly in regulated exocytosis but not endocytosis in PC12 cells
    • doi:10.1242/jcs.03375
    • Lynch KL, Martin TF. Synaptotagmins I and IX function redundantly in regulated exocytosis but not endocytosis in PC12 cells. J Cell Sci (2007) 120:617-27. doi:10.1242/jcs.03375.
    • (2007) J Cell Sci , vol.120 , pp. 617-627
    • Lynch, K.L.1    Martin, T.F.2
  • 45
    • 59449087443 scopus 로고    scopus 로고
    • Synaptotagmin-1 utilizes membrane bending and SNARE binding to drive fusion pore expansion
    • doi:10.1091/mbc. E08-03-0235
    • Lynch KL, Gerona RR, Kielar DM, Martens S, McMahon HT, Martin TF. Synaptotagmin-1 utilizes membrane bending and SNARE binding to drive fusion pore expansion. Mol Biol Cell (2008) 19:5093-103. doi:10.1091/mbc. E08-03-0235.
    • (2008) Mol Biol Cell , vol.19 , pp. 5093-5103
    • Lynch, K.L.1    Gerona, R.R.2    Kielar, D.M.3    Martens, S.4    McMahon, H.T.5    Martin, T.F.6
  • 46
    • 0035949679 scopus 로고    scopus 로고
    • Intracellular calcium dependence of large dense-core vesicle exocytosis in the absence of synaptotagmin I
    • doi:10.1073/pnas.201398798
    • Voets T, Moser T, Lund PE, Chow RH, Geppert M, Sudhof TC, et al. Intracellular calcium dependence of large dense-core vesicle exocytosis in the absence of synaptotagmin I. Proc Natl Acad Sci U S A (2001) 98:11680-5. doi:10.1073/pnas.201398798.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11680-5
    • Voets, T.1    Moser, T.2    Lund, P.E.3    Chow, R.H.4    Geppert, M.5    Sudhof, T.C.6
  • 47
    • 41649102893 scopus 로고    scopus 로고
    • Synaptotagmin-1 and -7 are functionally overlapping Ca2+ sensors for exocytosis in adrenal chromaffin cells
    • doi:10.1073/pnas.0712373105
    • Schonn JS, Maximov A, Lao Y, Sudhof TC, Sorensen JB. Synaptotagmin-1 and -7 are functionally overlapping Ca2+ sensors for exocytosis in adrenal chromaffin cells. Proc Natl Acad Sci U S A (2008) 105:3998-4003. doi:10.1073/pnas.0712373105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3998-4003
    • Schonn, J.S.1    Maximov, A.2    Lao, Y.3    Sudhof, T.C.4    Sorensen, J.B.5
  • 48
    • 0141563427 scopus 로고    scopus 로고
    • Examining synaptotagmin 1 function in dense core vesicle exocytosis under direct control of Ca2+
    • doi:10.1085/jgp.200308855
    • Sorensen JB, Fernandez-Chacon R, Sudhof TC, Neher E. Examining synaptotagmin 1 function in dense core vesicle exocytosis under direct control of Ca2+. J Gen Physiol (2003) 122:265-76. doi:10.1085/jgp.200308855.
    • (2003) J Gen Physiol , vol.122 , pp. 265-276
    • Sorensen, J.B.1    Fernandez-Chacon, R.2    Sudhof, T.C.3    Neher, E.4
  • 49
    • 77956363476 scopus 로고    scopus 로고
    • Distinct roles for two synaptotagmin isoforms in synchronous and asynchronous transmitter release at zebrafish neuromuscular junction
    • doi:10.1073/pnas.1008598107
    • Wen H, LinhoffMW, McGinley MJ, Li GL, Corson GM, Mandel G, et al. Distinct roles for two synaptotagmin isoforms in synchronous and asynchronous transmitter release at zebrafish neuromuscular junction. Proc Natl Acad Sci U S A (2010) 107:13906-11. doi:10.1073/pnas.1008598107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13906-11
    • Wen, H.1    Linhoff, M.W.2    McGinley, M.J.3    Li, G.L.4    Corson, G.M.5    Mandel, G.6
  • 50
    • 41649086377 scopus 로고    scopus 로고
    • Impaired insulin secretion and glucose intolerance in synaptotagmin-7 null mutant mice
    • doi:10.1073/pnas.0711700105
    • Gustavsson N, Lao Y, Maximov A, Chuang JC, Kostromina E, Repa JJ, et al. Impaired insulin secretion and glucose intolerance in synaptotagmin-7 null mutant mice. Proc Natl Acad Sci U S A (2008) 105:3992-7. doi:10.1073/pnas.0711700105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3992-3997
    • Gustavsson, N.1    Lao, Y.2    Maximov, A.3    Chuang, J.C.4    Kostromina, E.5    Repa, J.J.6
  • 52
    • 34548420547 scopus 로고    scopus 로고
    • Regulation of insulin secretion and GLUT4 trafficking by the calcium sensor synaptotagmin VII
    • doi:10.1016/j.bbrc.2007.08.023
    • Li Y, Wang P, Xu J, Gorelick F, Yamazaki H, Andrews N, et al. Regulation of insulin secretion and GLUT4 trafficking by the calcium sensor synaptotagmin VII. Biochem Biophys Res Commun (2007) 362:658-64. doi:10.1016/j.bbrc.2007.08.023.
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 658-664
    • Li, Y.1    Wang, P.2    Xu, J.3    Gorelick, F.4    Yamazaki, H.5    Andrews, N.6
  • 53
    • 42449140088 scopus 로고    scopus 로고
    • Confusion in the nomenclature of synaptotagmins V and IX
    • Fukuda M, Sagi-Eisenberg R. Confusion in the nomenclature of synaptotagmins V and IX. Calcium Bind Proteins (2008) 3:1-4.
    • (2008) Calcium Bind Proteins , vol.3 , pp. 1-4
    • Fukuda, M.1    Sagi-Eisenberg, R.2
  • 54
    • 0037085255 scopus 로고    scopus 로고
    • Synaptotagmin IX regulates Ca2+-dependent secretion in PC12 cells
    • doi:10.1074/jbc. C100588200
    • Fukuda M, Kowalchyk JA, Zhang X, Martin TF, Mikoshiba K. Synaptotagmin IX regulates Ca2+-dependent secretion in PC12 cells. J Biol Chem (2002) 277:4601-4. doi:10.1074/jbc. C100588200.
    • (2002) J Biol Chem , vol.277 , pp. 4601-4604
    • Fukuda, M.1    Kowalchyk, J.A.2    Zhang, X.3    Martin, T.F.4    Mikoshiba, K.5
  • 55
    • 0042672953 scopus 로고    scopus 로고
    • Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells
    • doi:10.1083/jcb.200302060
    • Tucker WC, Edwardson JM, Bai J, Kim HJ, Martin TF, Chapman ER. Identification of synaptotagmin effectors via acute inhibition of secretion from cracked PC12 cells. J Cell Biol (2003) 162:199-209. doi:10.1083/jcb.200302060.
    • (2003) J Cell Biol , vol.162 , pp. 199-209
    • Tucker, W.C.1    Edwardson, J.M.2    Bai, J.3    Kim, H.J.4    Martin, T.F.5    Chapman, E.R.6
  • 56
    • 24944458103 scopus 로고    scopus 로고
    • Adenovirus-mediated silencing of synaptotagmin 9 inhibits Ca2+-dependent insulin secretion in islets
    • doi:10.1016/j.febslet.2005.08.047
    • Iezzi M, Eliasson L, Fukuda M, Wollheim CB. Adenovirus-mediated silencing of synaptotagmin 9 inhibits Ca2+-dependent insulin secretion in islets. FEBS Lett (2005) 579:5241-6. doi:10.1016/j.febslet.2005.08.047.
    • (2005) FEBS Lett , vol.579 , pp. 5241-5246
    • Iezzi, M.1    Eliasson, L.2    Fukuda, M.3    Wollheim, C.B.4
  • 57
    • 78649729986 scopus 로고    scopus 로고
    • Neuronal calcium sensor synaptotagmin-9 is not involved in the regulation of glucose homeostasis or insulin secretion
    • doi:10.1371/journal.pone.0015414
    • Gustavsson N, Wang X, Wang Y, Seah T, Xu J, Radda GK, et al. Neuronal calcium sensor synaptotagmin-9 is not involved in the regulation of glucose homeostasis or insulin secretion. PLoS One (2010) 5:e15414. doi:10.1371/journal.pone.0015414.
    • (2010) PLoS One , vol.5
    • Gustavsson, N.1    Wang, X.2    Wang, Y.3    Seah, T.4    Xu, J.5    Radda, G.K.6
  • 58
    • 0030952081 scopus 로고    scopus 로고
    • The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding
    • doi:10.1074/jbc.272.22.14314
    • von Poser C, Ichtchenko K, Shao X, Rizo J, Sudhof TC. The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding. J Biol Chem (1997) 272:14314-9. doi:10.1074/jbc.272.22.14314.
    • (1997) J Biol Chem , vol.272 , pp. 14314-9
    • von Poser, C.1    Ichtchenko, K.2    Shao, X.3    Rizo, J.4    Sudhof, T.C.5
  • 59
    • 0028901750 scopus 로고
    • Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain
    • doi:10.1073/pnas.92.6.2164
    • Vician L, Lim IK, Ferguson G, Tocco G, Baudry M, Herschman HR. Synaptotagmin IV is an immediate early gene induced by depolarization in PC12 cells and in brain. Proc Natl Acad Sci U S A (1995) 92:2164-8. doi:10.1073/pnas.92.6.2164.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2164-2168
    • Vician, L.1    Lim, I.K.2    Ferguson, G.3    Tocco, G.4    Baudry, M.5    Herschman, H.R.6
  • 60
    • 33845785944 scopus 로고    scopus 로고
    • Singing, but not seizure, induces synaptotagmin IV in zebra finch song circuit nuclei
    • doi:10.1002/neu.20329
    • Poopatanapong A, Teramitsu I, Byun JS, Vician LJ, Herschman HR, White SA. Singing, but not seizure, induces synaptotagmin IV in zebra finch song circuit nuclei. J Neurobiol (2006) 66:1613-29. doi:10.1002/neu.20329.
    • (2006) J Neurobiol , vol.66 , pp. 1613-1629
    • Poopatanapong, A.1    Teramitsu, I.2    Byun, J.S.3    Vician, L.J.4    Herschman, H.R.5    White, S.A.6
  • 62
    • 77949589647 scopus 로고    scopus 로고
    • Synaptotagmin IV modulation of vesicle size and fusion pores in PC12 cells
    • doi:10.1016/j.bpj.2009.11.024
    • Zhang Z, Zhang Z, Jackson MB. Synaptotagmin IV modulation of vesicle size and fusion pores in PC12 cells. Biophys J (2010) 98:968-78. doi:10.1016/j.bpj.2009.11.024.
    • (2010) Biophys J , vol.98 , pp. 968-978
    • Zhang, Z.1    Zhang, Z.2    Jackson, M.B.3
  • 63
    • 58849162392 scopus 로고    scopus 로고
    • Synaptotagmin IV:a multifunctional regulator of peptidergic nerve terminals
    • doi:10.1038/nn.2252
    • Zhang Z, Bhalla A, Dean C, Chapman ER, Jackson MB. Synaptotagmin IV:a multifunctional regulator of peptidergic nerve terminals. Nat Neurosci (2009) 12:163-71. doi:10.1038/nn.2252.
    • (2009) Nat Neurosci , vol.12 , pp. 163-171
    • Zhang, Z.1    Bhalla, A.2    Dean, C.3    Chapman, E.R.4    Jackson, M.B.5
  • 64
    • 33646112380 scopus 로고    scopus 로고
    • Synaptotagmin IV is necessary for the maturation of secretory granules in PC12 cells
    • doi:10.1083/jcb.200506163
    • Ahras M, Otto GP, Tooze SA. Synaptotagmin IV is necessary for the maturation of secretory granules in PC12 cells. J Cell Biol (2006) 173(2):242-51. doi:10.1083/jcb.200506163.
    • (2006) J Cell Biol , vol.173 , Issue.2 , pp. 242-251
    • Ahras, M.1    Otto, G.P.2    Tooze, S.A.3
  • 65
    • 0034307475 scopus 로고    scopus 로고
    • Biogenesis of regulated exocytotic carriers in neuroendocrine cells
    • Eaton BA, Haugwitz M, Lau D, Moore HP. Biogenesis of regulated exocytotic carriers in neuroendocrine cells. J Neurosci (2000) 20:7334-44.
    • (2000) J Neurosci , vol.20 , pp. 7334-7344
    • Eaton, B.A.1    Haugwitz, M.2    Lau, D.3    Moore, H.P.4
  • 66
    • 0344012489 scopus 로고    scopus 로고
    • Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a nonadditive manner
    • doi:10.1074/jbc. M306728200
    • Wang P, Wang CT, Bai J, Jackson MB, Chapman ER. Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a nonadditive manner. J Biol Chem (2003) 278:47030-7. doi:10.1074/jbc. M306728200.
    • (2003) J Biol Chem , vol.278 , pp. 47030-7
    • Wang, P.1    Wang, C.T.2    Bai, J.3    Jackson, M.B.4    Chapman, E.R.5
  • 67
    • 0035016467 scopus 로고    scopus 로고
    • Expression and localisation of synaptotagmin isoforms in endocrine beta-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 beta-cells:their function in insulin exocytosis. J Cell Sci (2001) 114:1709-16.
    • (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
  • 68
    • 32144443300 scopus 로고    scopus 로고
    • Synaptotagmin 8 is expressed both as a calcium-insensitive soluble and membrane protein in neurons, neuroendocrine and endocrine cells
    • doi:10.1016/j.bbamcr.2005.11.008
    • Monterrat C, Boal F, Grise F, Hemar A, Lang J. Synaptotagmin 8 is expressed both as a calcium-insensitive soluble and membrane protein in neurons, neuroendocrine and endocrine cells. Biochim Biophys Acta (2006) 1763:73-81. doi:10.1016/j.bbamcr.2005.11.008.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 73-81
    • Monterrat, C.1    Boal, F.2    Grise, F.3    Hemar, A.4    Lang, J.5
  • 69
    • 84867518459 scopus 로고    scopus 로고
    • Reduced insulin secretion correlates with decreased expression of exocytotic genes in pancreatic islets from patients with type 2 diabetes
    • doi:10.1016/j.mce.2012.08.009
    • Andersson SA, Olsson AH, Esguerra JL, Heimann E, Ladenvall C, Edlund A, et al. Reduced insulin secretion correlates with decreased expression of exocytotic genes in pancreatic islets from patients with type 2 diabetes. Mol Cell Endocrinol (2012) 364:36-45. doi:10.1016/j.mce.2012.08.009.
    • (2012) Mol Cell Endocrinol , vol.364 , pp. 36-45
    • Andersson, S.A.1    Olsson, A.H.2    Esguerra, J.L.3    Heimann, E.4    Ladenvall, C.5    Edlund, A.6
  • 70
    • 79952360420 scopus 로고    scopus 로고
    • Mapping of INS promoter interactions reveals its role in long-range regulation of SYT8 transcription
    • doi:10.1038/nsmb.1993
    • Xu Z, Wei G, Chepelev I, Zhao K, Felsenfeld G. Mapping of INS promoter interactions reveals its role in long-range regulation of SYT8 transcription. Nat Struct Mol Biol (2011) 18:372-8. doi:10.1038/nsmb.1993.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 372-378
    • Xu, Z.1    Wei, G.2    Chepelev, I.3    Zhao, K.4    Felsenfeld, G.5
  • 71
    • 0344734112 scopus 로고    scopus 로고
    • Analysis of synaptotagmin I-IV messenger RNA expression and developmental regulation in the rat hypothalamus and pituitary
    • doi:10.1016/S0306-4522(98)00234-6
    • Xi D, Chin H, Gainer H. Analysis of synaptotagmin I-IV messenger RNA expression and developmental regulation in the rat hypothalamus and pituitary. Neuroscience (1999) 88:425-35. doi:10.1016/S0306-4522(98)00234-6.
    • (1999) Neuroscience , vol.88 , pp. 425-435
    • Xi, D.1    Chin, H.2    Gainer, H.3
  • 72
    • 79951717108 scopus 로고    scopus 로고
    • Synaptotagmin increases the dynamic range of synapses by driving Ca(2)+-evoked release and by clamping a near-linear remaining Ca(2)+ sensor
    • doi:10.1016/j.neuron.2011.01.013
    • Kochubey O, Schneggenburger R. Synaptotagmin increases the dynamic range of synapses by driving Ca(2)+-evoked release and by clamping a near-linear remaining Ca(2)+ sensor. Neuron (2011) 69:736-48. doi:10.1016/j.neuron.2011.01.013.
    • (2011) Neuron , vol.69 , pp. 736-748
    • Kochubey, O.1    Schneggenburger, R.2
  • 73
    • 36749078085 scopus 로고    scopus 로고
    • A dual-Ca2+-sensor model for neurotransmitter release in a central synapse
    • doi:10.1038/nature06308
    • Sun J, Pang ZP, Qin D, Fahim AT, Adachi R, Südhof TC. A dual-Ca2+-sensor model for neurotransmitter release in a central synapse. Nature (2007) 450:676-82. doi:10.1038/nature06308.
    • (2007) Nature , vol.450 , pp. 676-682
    • Sun, J.1    Pang, Z.P.2    Qin, D.3    Fahim, A.T.4    Adachi, R.5    Südhof, T.C.6
  • 74
    • 0033068160 scopus 로고    scopus 로고
    • Comparative biology of Ca2+-dependent exocytosis:implications of kinetic diversity for secretory function
    • doi:10.1016/S0166-2236(98)01293-4
    • Kasai H. Comparative biology of Ca2+-dependent exocytosis:implications of kinetic diversity for secretory function. Trends Neurosci (1999) 22:88-93. doi:10.1016/S0166-2236(98)01293-4.
    • (1999) Trends Neurosci , vol.22 , pp. 88-93
    • Kasai, H.1
  • 75
    • 0032008553 scopus 로고    scopus 로고
    • Vesicle pools and Ca2+ microdomains:new tools for understanding their roles in neurotransmitter release
    • doi:10.1016/S0896-6273(00)80983-6
    • Neher E. Vesicle pools and Ca2+ microdomains:new tools for understanding their roles in neurotransmitter release. Neuron (1998) 20:389-99. doi:10.1016/S0896-6273(00)80983-6.
    • (1998) Neuron , vol.20 , pp. 389-399
    • Neher, E.1
  • 76
    • 0032435180 scopus 로고    scopus 로고
    • Usefulness and limitations of linear approximations to the understanding of Ca++ signals
    • doi:10.1016/S0143-4160(98)90058-6
    • Neher E. Usefulness and limitations of linear approximations to the understanding of Ca++ signals. Cell Calcium (1998) 24:345-57. doi:10.1016/S0143-4160(98)90058-6.
    • (1998) Cell Calcium , vol.24 , pp. 345-357
    • Neher, E.1
  • 77
    • 0141987862 scopus 로고    scopus 로고
    • Local calcium signaling in neurons
    • doi:10.1016/S0896-6273(03)00639-1
    • Augustine GJ, Santamaria F, Tanaka K. Local calcium signaling in neurons. Neuron (2003) 40:331-46. doi:10.1016/S0896-6273(03)00639-1.
    • (2003) Neuron , vol.40 , pp. 331-346
    • Augustine, G.J.1    Santamaria, F.2    Tanaka, K.3
  • 78
    • 0026519666 scopus 로고
    • Time course of transmitter release calculated from simulations of a calcium diffusion model
    • doi:10.1016/S0006-3495(92)81872-6
    • Yamada WM, Zucker RS. Time course of transmitter release calculated from simulations of a calcium diffusion model. Biophys J (1992) 61:671-82. doi:10.1016/S0006-3495(92)81872-6.
    • (1992) Biophys J , vol.61 , pp. 671-682
    • Yamada, W.M.1    Zucker, R.S.2
  • 79
    • 33644993894 scopus 로고    scopus 로고
    • Double patch clamp reveals that transient fusion (kiss-and-run) is a major mechanism of secretion in calf adrenal chromaffin cells:high calcium shifts the mechanism from kiss-and-run to complete fusion
    • doi:10.1523/JNEUROSCI.5275-05.2006
    • Elhamdani A, Azizi F, Artalejo CR. Double patch clamp reveals that transient fusion (kiss-and-run) is a major mechanism of secretion in calf adrenal chromaffin cells:high calcium shifts the mechanism from kiss-and-run to complete fusion. J Neurosci (2006) 26:3030-6. doi:10.1523/JNEUROSCI.5275-05.2006.
    • (2006) J Neurosci , vol.26 , pp. 3030-3036
    • Elhamdani, A.1    Azizi, F.2    Artalejo, C.R.3
  • 81
    • 10044280469 scopus 로고    scopus 로고
    • Fluorescent cargo proteins in pancreatic beta-cells:design determines secretion kinetics at exocytosis
    • doi:10.1529/biophysj.104.052175
    • Michael DJ, Geng X, Cawley NX, Loh YP, Rhodes CJ, Drain P, et al. Fluorescent cargo proteins in pancreatic beta-cells:design determines secretion kinetics at exocytosis. Biophys J (2004) 87:L03-5. doi:10.1529/biophysj.104.052175.
    • (2004) Biophys J , vol.87
    • Michael, D.J.1    Geng, X.2    Cawley, N.X.3    Loh, Y.P.4    Rhodes, C.J.5    Drain, P.6
  • 82
    • 0028305903 scopus 로고
    • Synaptotagmin III is a novel isoform of rat synaptotagmin expressed in endocrine and neuronal cells
    • Mizuta M, Inagaki N, Nemoto Y, Matsukura S, Takahashi M, Seino S. Synaptotagmin III is a novel isoform of rat synaptotagmin expressed in endocrine and neuronal cells. J Biol Chem (1994) 269:11675-8.
    • (1994) J Biol Chem , vol.269 , pp. 11675-8
    • Mizuta, M.1    Inagaki, N.2    Nemoto, Y.3    Matsukura, S.4    Takahashi, M.5    Seino, S.6
  • 83
    • 0037025304 scopus 로고    scopus 로고
    • Synaptotagmin V is targeted to dense-core vesicles that undergo calcium-dependent exocytosis in PC12 cells
    • doi:10.1074/jbc. M202767200
    • Saegusa C, Fukuda M, Mikoshiba K. Synaptotagmin V is targeted to dense-core vesicles that undergo calcium-dependent exocytosis in PC12 cells. J Biol Chem (2002) 277:24499-505. doi:10.1074/jbc. M202767200.
    • (2002) J Biol Chem , vol.277 , pp. 24499-505
    • Saegusa, C.1    Fukuda, M.2    Mikoshiba, K.3
  • 84
    • 79953821048 scopus 로고    scopus 로고
    • Differential distribution of synaptotagmin-1, -4, -7, and -9 in rat adrenal chromaffin cells
    • doi:10.1007/s00441-011-1131-8
    • Matsuoka H, Harada K, Nakamura J, Fukuda M, Inoue M. Differential distribution of synaptotagmin-1, -4, -7, and -9 in rat adrenal chromaffin cells. Cell Tissue Res (2011) 344:41-50. doi:10.1007/s00441-011-1131-8.
    • (2011) Cell Tissue Res , vol.344 , pp. 41-50
    • Matsuoka, H.1    Harada, K.2    Nakamura, J.3    Fukuda, M.4    Inoue, M.5
  • 85
    • 44349112878 scopus 로고    scopus 로고
    • Synaptotagmin IV regulates dense core vesicle (DCV) release in LbetaT2 cells
    • doi:10.1016/j.bbrc.2008.04.174
    • Hu ZT, Chen MR, Ping Z, Dong YM, Zhang RY, Xu T, et al. Synaptotagmin IV regulates dense core vesicle (DCV) release in LbetaT2 cells. Biochem Biophys Res Commun (2008) 371:781-6. doi:10.1016/j.bbrc.2008.04.174.
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 781-786
    • Hu, Z.T.1    Chen, M.R.2    Ping, Z.3    Dong, Y.M.4    Zhang, R.Y.5    Xu, T.6
  • 86
    • 0037303864 scopus 로고    scopus 로고
    • Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells
    • doi:10.1152/ajpcell.00333.2002
    • Kreft M, Kuster V, Grilc S, Rupnik M, Milisav I, Zorec R. Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells. Am J Physiol Cell Physiol (2003) 284:C547-54. doi:10.1152/ajpcell.00333.2002.
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Kreft, M.1    Kuster, V.2    Grilc, S.3    Rupnik, M.4    Milisav, I.5    Zorec, R.6
  • 87
    • 0034680831 scopus 로고    scopus 로고
    • Synaptotagmin III/VII isoforms mediate Ca2+-induced insulin secretion in pancreatic islet beta-cells
    • doi:10.1074/jbc. M004284200
    • Gao Z, Reavey-Cantwell J, Young RA, Jegier P, Wolf BA. Synaptotagmin III/VII isoforms mediate Ca2+-induced insulin secretion in pancreatic islet beta-cells. J Biol Chem (2000) 275:36079-85. doi:10.1074/jbc. M004284200.
    • (2000) J Biol Chem , vol.275 , pp. 36079-85
    • Gao, Z.1    Reavey-Cantwell, J.2    Young, R.A.3    Jegier, P.4    Wolf, B.A.5
  • 88
    • 0030727151 scopus 로고    scopus 로고
    • Localization and functional role of synaptotagmin III in insulin secretory vesicles in pancreatic beta-cells
    • doi:10.2337/diabetes.46.12.2002
    • Mizuta M, Kurose T, Miki T, Shoji-Kasai Y, Takahashi M, Seino S, et al. Localization and functional role of synaptotagmin III in insulin secretory vesicles in pancreatic beta-cells. Diabetes (1997) 46:2002-6. doi:10.2337/diabetes.46.12.2002.
    • (1997) Diabetes , vol.46 , pp. 2002-2006
    • Mizuta, M.1    Kurose, T.2    Miki, T.3    Shoji-Kasai, Y.4    Takahashi, M.5    Seino, S.6
  • 89
    • 3042827047 scopus 로고    scopus 로고
    • Synaptotagmin V and IX isoforms control Ca2+-dependent insulin exocytosis
    • doi:10.1242/jcs.01179
    • Iezzi M, Kouri G, Fukuda M, Wollheim CB. Synaptotagmin V and IX isoforms control Ca2+-dependent insulin exocytosis. J Cell Sci (2004) 117:3119-27. doi:10.1242/jcs.01179.
    • (2004) J Cell Sci , vol.117 , pp. 3119-3127
    • Iezzi, M.1    Kouri, G.2    Fukuda, M.3    Wollheim, C.B.4
  • 90
    • 0034089335 scopus 로고    scopus 로고
    • Synaptotagmin III isoform is compartmentalized in pancreatic beta-cells and has a functional role in exocytosis
    • doi:10.2337/diabetes.49.3.383
    • Brown H, Meister B, Deeney J, Corkey BE, Yang SN, Larsson O, et al. Synaptotagmin III isoform is compartmentalized in pancreatic beta-cells and has a functional role in exocytosis. Diabetes (2000) 49:383-91. doi:10.2337/diabetes.49.3.383.
    • (2000) Diabetes , vol.49 , pp. 383-391
    • Brown, H.1    Meister, B.2    Deeney, J.3    Corkey, B.E.4    Yang, S.N.5    Larsson, O.6
  • 91
    • 0030868429 scopus 로고    scopus 로고
    • The first C2 domain of synaptotagmin is required for exocytosis of insulin from pancreatic beta-cells:action of synaptotagmin at low micromolar calcium
    • doi:10.1093/emboj/16.19.5837
    • Lang J, Fukuda M, Zhang H, Mikoshiba K, Wollheim CB. The first C2 domain of synaptotagmin is required for exocytosis of insulin from pancreatic beta-cells:action of synaptotagmin at low micromolar calcium. EMBO J (1997) 16:5837-46. doi:10.1093/emboj/16.19.5837.
    • (1997) EMBO J , vol.16 , pp. 5837-5846
    • Lang, J.1    Fukuda, M.2    Zhang, H.3    Mikoshiba, K.4    Wollheim, C.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.