메뉴 건너뛰기




Volumn 4, Issue DEC, 2013, Pages

CAPS and Munc13: CATCHRs that SNARE vesicles

Author keywords

CAPS (aka CADPS); Multi subunit tethering complexes; Munc13; Priming factors; SNAREs; Vesicle fusion

Indexed keywords

CALCIUM DEPENDENT ACTIVATOR PROTEIN FOR SECRETION; COMPLEX ASSOCIATED WITH TETHERING CONTAINING HELICAL RODS; MULTI SUBUNIT TETHERING COMPLEX; MULTIPROTEIN COMPLEX; MUNC13 PROTEIN; PROTEIN SM; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 84892186479     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2013.00187     Document Type: Review
Times cited : (64)

References (131)
  • 1
    • 52549126992 scopus 로고    scopus 로고
    • Regulation of secretory vesicle traffic by Rab small GTPases
    • doi:10.1007/s00018-008-8351-4
    • Fukuda M. Regulation of secretory vesicle traffic by Rab small GTPases. Cell Mol Life Sci (2008) 65:2801-13. doi:10.1007/s00018-008-8351-4.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2801-2813
    • Fukuda, M.1
  • 2
    • 78751656754 scopus 로고    scopus 로고
    • Role of Rab GTPases in membrane traffic and cell physiology
    • doi:10.1152/physrev.00059.2009
    • Hutagalung AH, Novick PJ. Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev (2011) 91:119-49. doi:10.1152/physrev.00059.2009.
    • (2011) Physiol Rev , vol.91 , pp. 119-149
    • Hutagalung, A.H.1    Novick, P.J.2
  • 3
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • doi:10.1038/nature05185
    • Di Paolo G, De Camilli P. Phosphoinositides in cell regulation and membrane dynamics. Nature (2006) 443:651-7. doi:10.1038/nature05185.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 4
    • 0035424240 scopus 로고    scopus 로고
    • PI(4,5)P(2) regulation of surface membrane traffic
    • doi:10.1016/S0955-0674(00)00241-6
    • Martin TF. PI(4,5)P(2) regulation of surface membrane traffic. Curr Opin Cell Biol (2001) 13:493-9. doi:10.1016/S0955-0674(00)00241-6.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 5
    • 80054056038 scopus 로고    scopus 로고
    • The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors
    • doi:10.1016/j.str.2011.07.012
    • Li W, Ma C, Guan R, Xu Y, Tomchick DR, Rizo J. The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors. Structure (2011) 19:1443-55. doi:10.1016/j.str.2011.07.012.
    • (2011) Structure , vol.19 , pp. 1443-1455
    • Li, W.1    Ma, C.2    Guan, R.3    Xu, Y.4    Tomchick, D.R.5    Rizo, J.6
  • 6
    • 67651160303 scopus 로고    scopus 로고
    • Remote homology between Munc13 MUN domain and vesicle tethering complexes
    • doi:10.1016/j.jmb.2009.06.054
    • Pei J, Ma C, Rizo J, Grishin NV. Remote homology between Munc13 MUN domain and vesicle tethering complexes. J Mol Biol (2009) 391:509-17. doi:10.1016/j.jmb.2009.06.054.
    • (2009) J Mol Biol , vol.391 , pp. 509-517
    • Pei, J.1    Ma, C.2    Rizo, J.3    Grishin, N.V.4
  • 8
    • 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
  • 9
    • 52549098624 scopus 로고    scopus 로고
    • Membrane fusion: SNAREs and regulation
    • doi:10.1007/s00018-008-8352-3
    • Malsam J, Kreye S, Sollner TH. Membrane fusion: SNAREs and regulation. Cell Mol Life Sci (2008) 65:2814-32. doi:10.1007/s00018-008-8352-3.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2814-2832
    • Malsam, J.1    Kreye, S.2    Sollner, T.H.3
  • 10
    • 0027219725 scopus 로고
    • Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25
    • doi:10.1038/365160a0
    • Blasi J, Chapman ER, Link E, Binz T, Yamasaki S, De Camilli P, et al. Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature (1993) 365:160-3. doi:10.1038/365160a0.
    • (1993) Nature , vol.365 , pp. 160-163
    • Blasi, J.1    Chapman, E.R.2    Link, E.3    Binz, T.4    Yamasaki, S.5    De Camilli, P.6
  • 11
    • 0027432376 scopus 로고
    • Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin
    • Blasi J, Chapman ER, Yamasaki S, Binz T, Niemann H, Jahn R. Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin. EMBO J (1993) 12:4821-8.
    • (1993) EMBO J , vol.12 , pp. 4821-4828
    • Blasi, J.1    Chapman, E.R.2    Yamasaki, S.3    Binz, T.4    Niemann, H.5    Jahn, R.6
  • 12
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly
    • Hayashi T, McMahon H, Yamasaki S, Binz T, Hata Y, Sudhof TC, et al. Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J (1994) 13:5051-61.
    • (1994) EMBO J , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Sudhof, T.C.6
  • 13
    • 0027097028 scopus 로고
    • Tetanus toxin action: inhibition of neurotransmitter release linked to synaptobrevin proteolysis
    • doi:10.1016/0006-291X(92)92305-H
    • Link E, Edelmann L, Chou JH, Binz T, Yamasaki S, Eisel U, et al. Tetanus toxin action: inhibition of neurotransmitter release linked to synaptobrevin proteolysis. Biochem Biophys Res Commun (1992) 189:1017-23. doi:10.1016/0006-291X(92)92305-H.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1017-1023
    • Link, E.1    Edelmann, L.2    Chou, J.H.3    Binz, T.4    Yamasaki, S.5    Eisel, U.6
  • 14
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • doi:10.1038/359832a0
    • Schiavo G, Benfenati F, Poulain B, Rossetto O, Polverino de Laureto P, DasGupta BR, et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature (1992) 359:832-5. doi:10.1038/359832a0.
    • (1992) Nature , vol.359 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3    Rossetto, O.4    Polverino de Laureto, P.5    DasGupta, B.R.6
  • 15
    • 70349303129 scopus 로고    scopus 로고
    • Differences in the SNARE evolution of fungi and metazoa
    • doi:10.1042/BST0370787
    • Kienle N, Kloepper TH, Fasshauer D. Differences in the SNARE evolution of fungi and metazoa. Biochem Soc Trans (2009) 37:787-91. doi:10.1042/BST0370787.
    • (2009) Biochem Soc Trans , vol.37 , pp. 787-791
    • Kienle, N.1    Kloepper, T.H.2    Fasshauer, D.3
  • 16
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs
    • doi:10.1073/pnas.95.26.15781
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q-and R-SNAREs. Proc Natl Acad Sci U S A (1998) 95:15781-6. doi:10.1073/pnas.95.26.15781.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 17
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: minimal machinery for membrane fusion
    • doi:10.1016/S0092-8674(00)81404-X
    • Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, et al. SNAREpins: minimal machinery for membrane fusion. Cell (1998) 92:759-72. doi:10.1016/S0092-8674(00)81404-X.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3    Westermann, B.4    Gmachl, M.5    Parlati, F.6
  • 18
    • 33644770187 scopus 로고    scopus 로고
    • Structure and function of SNARE and SNARE-interacting proteins
    • doi:10.1017/S0033583505004051
    • Brunger AT. Structure and function of SNARE and SNARE-interacting proteins. Q Rev Biophys (2005) 38:1-47. doi:10.1017/S0033583505004051.
    • (2005) Q Rev Biophys , vol.38 , pp. 1-47
    • Brunger, A.T.1
  • 19
    • 0041659220 scopus 로고    scopus 로고
    • Structural insights into the SNARE mechanism
    • doi:10.1016/S0167-4889(03)00090-9
    • Fasshauer D. Structural insights into the SNARE mechanism. Biochim Biophys Acta (2003) 1641:87-97. doi:10.1016/S0167-4889(03)00090-9.
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 87-97
    • Fasshauer, D.1
  • 20
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • doi:10.1038/26412
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature (1998) 395:347-53. doi:10.1038/26412.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 21
    • 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
  • 22
    • 0035034079 scopus 로고    scopus 로고
    • Sequential SNARE assembly underlies priming and triggering of exocytosis
    • doi:10.1016/S0896-6273(01)00270-7
    • Chen YA, Scales SJ, Scheller RH. Sequential SNARE assembly underlies priming and triggering of exocytosis. Neuron (2001) 30:161-70. doi:10.1016/S0896-6273(01)00270-7.
    • (2001) Neuron , vol.30 , pp. 161-170
    • Chen, Y.A.1    Scales, S.J.2    Scheller, R.H.3
  • 23
    • 77949511830 scopus 로고    scopus 로고
    • Structure and dynamics of a two-helix SNARE complex in live cells
    • doi:10.1111/j.1600-0854.2009.01020.x
    • Halemani ND, Bethani I, Rizzoli SO, Lang T. Structure and dynamics of a two-helix SNARE complex in live cells. Traffic (2010) 11:394-404. doi:10.1111/j.1600-0854.2009.01020.x.
    • (2010) Traffic , vol.11 , pp. 394-404
    • Halemani, N.D.1    Bethani, I.2    Rizzoli, S.O.3    Lang, T.4
  • 24
    • 84867706752 scopus 로고    scopus 로고
    • Distinct initial SNARE configurations underlying the diversity of exocytosis
    • doi:10.1152/physrev.00007.2012
    • Kasai H, Takahashi N, Tokumaru H. Distinct initial SNARE configurations underlying the diversity of exocytosis. Physiol Rev (2012) 92:1915-64. doi:10.1152/physrev.00007.2012.
    • (2012) Physiol Rev , vol.92 , pp. 1915-1964
    • Kasai, H.1    Takahashi, N.2    Tokumaru, H.3
  • 25
    • 33750805030 scopus 로고    scopus 로고
    • Molecular anatomy of a trafficking organelle
    • doi:10.1016/j.cell.2006.10.030
    • Takamori S, Holt M, Stenius K, Lemke EA, Gronborg M, Riedel D, et al. Molecular anatomy of a trafficking organelle. Cell (2006) 127:831-46. doi:10.1016/j.cell.2006.10.030.
    • (2006) Cell , vol.127 , pp. 831-846
    • Takamori, S.1    Holt, M.2    Stenius, K.3    Lemke, E.A.4    Gronborg, M.5    Riedel, D.6
  • 26
    • 0034648836 scopus 로고    scopus 로고
    • Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
    • doi:10.1038/35025000
    • McNew JA, Parlati F, Fukuda R, Johnston RJ, Paz K, Paumet F, et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature (2000) 407:153-9. doi:10.1038/35025000.
    • (2000) Nature , vol.407 , pp. 153-159
    • McNew, J.A.1    Parlati, F.2    Fukuda, R.3    Johnston, R.J.4    Paz, K.5    Paumet, F.6
  • 27
    • 0034648797 scopus 로고    scopus 로고
    • Topological restriction of SNARE-dependent membrane fusion
    • doi:10.1038/35025076
    • Parlati F, McNew JA, Fukuda R, Miller R, Sollner TH, Rothman JE. Topological restriction of SNARE-dependent membrane fusion. Nature (2000) 407:194-8. doi:10.1038/35025076.
    • (2000) Nature , vol.407 , pp. 194-198
    • Parlati, F.1    McNew, J.A.2    Fukuda, R.3    Miller, R.4    Sollner, T.H.5    Rothman, J.E.6
  • 28
    • 33644515632 scopus 로고    scopus 로고
    • Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity
    • doi:10.1073/pnas.0511138103
    • Brandhorst D, Zwilling D, Rizzoli SO, Lippert U, Lang T, Jahn R. Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity. Proc Natl Acad Sci U S A (2006) 103:2701-6. doi:10.1073/pnas.0511138103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2701-2706
    • Brandhorst, D.1    Zwilling, D.2    Rizzoli, S.O.3    Lippert, U.4    Lang, T.5    Jahn, R.6
  • 29
    • 84856241071 scopus 로고    scopus 로고
    • Distinct contributions of vacuolar Qabc-and R-SNARE proteins to membrane fusion specificity
    • doi:10.1074/jbc.M111.307439
    • Izawa R, Onoue T, Furukawa N, Mima J. Distinct contributions of vacuolar Qabc-and R-SNARE proteins to membrane fusion specificity. J Biol Chem (2012) 287:3445-53. doi:10.1074/jbc.M111.307439.
    • (2012) J Biol Chem , vol.287 , pp. 3445-3453
    • Izawa, R.1    Onoue, T.2    Furukawa, N.3    Mima, J.4
  • 30
    • 33845987734 scopus 로고    scopus 로고
    • Selective activation of cognate SNAREpins by Sec1/Munc18 proteins
    • doi:10.1016/j.cell.2006.12.016
    • Shen J, Tareste DC, Paumet F, Rothman JE, Melia TJ. Selective activation of cognate SNAREpins by Sec1/Munc18 proteins. Cell (2007) 128:183-95. doi:10.1016/j.cell.2006.12.016.
    • (2007) Cell , vol.128 , pp. 183-195
    • Shen, J.1    Tareste, D.C.2    Paumet, F.3    Rothman, J.E.4    Melia, T.J.5
  • 31
    • 84883339791 scopus 로고    scopus 로고
    • Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins
    • doi:10.1073/pnas.1311232110
    • Yu H, Rathore SS, Lopez JA, Davis EM, James DE, Martin JL, et al. Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins. Proc Natl Acad Sci U S A (2013) 110:E3271-80. doi:10.1073/pnas.1311232110.
    • (2013) Proc Natl Acad Sci U S A , vol.110
    • Yu, H.1    Rathore, S.S.2    Lopez, J.A.3    Davis, E.M.4    James, D.E.5    Martin, J.L.6
  • 32
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • doi:10.1038/366347a0
    • Hata Y, Slaughter CA, Sudhof TC. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature (1993) 366:347-51. doi:10.1038/366347a0.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Sudhof, T.C.3
  • 33
    • 0026582816 scopus 로고
    • The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans
    • doi:10.1111/j.1471-4159.1992.tb11373.x
    • Hosono R, Hekimi S, Kamiya Y, Sassa T, Murakami S, Nishiwaki K, et al. The unc-18 gene encodes a novel protein affecting the kinetics of acetylcholine metabolism in the nematode Caenorhabditis elegans. J Neurochem (1992) 58:1517-25. doi:10.1111/j.1471-4159.1992.tb11373.x.
    • (1992) J Neurochem , vol.58 , pp. 1517-1525
    • Hosono, R.1    Hekimi, S.2    Kamiya, Y.3    Sassa, T.4    Murakami, S.5    Nishiwaki, K.6
  • 34
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • doi:10.1016/0092-8674(80)90128-2
    • Novick P, Field C, Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell (1980) 21:205-15. doi:10.1016/0092-8674(80)90128-2.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 35
    • 0035796402 scopus 로고    scopus 로고
    • Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation
    • doi:10.1093/emboj/20.13.3380
    • Bryant NJ, James DE. Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation. EMBO J (2001) 20:3380-8. doi:10.1093/emboj/20.13.3380.
    • (2001) EMBO J , vol.20 , pp. 3380-3388
    • Bryant, N.J.1    James, D.E.2
  • 37
    • 84870502774 scopus 로고    scopus 로고
    • Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex
    • doi:10.1091/mbc.E12-05-0343
    • Lobingier BT, Merz AJ. Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex. Mol Biol Cell (2012) 23:4611-22. doi:10.1091/mbc.E12-05-0343.
    • (2012) Mol Biol Cell , vol.23 , pp. 4611-4622
    • Lobingier, B.T.1    Merz, A.J.2
  • 38
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • doi:10.1016/S1534-5807(02)00125-9
    • Yamaguchi T, Dulubova I, Min SW, Chen X, Rizo J, Sudhof TC. Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev Cell (2002) 2:295-305. doi:10.1016/S1534-5807(02)00125-9.
    • (2002) Dev Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3    Chen, X.4    Rizo, J.5    Sudhof, T.C.6
  • 39
    • 0037422556 scopus 로고    scopus 로고
    • Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteins
    • doi:10.1073/pnas.232701299
    • Dulubova I, Yamaguchi T, Arac D, Li H, Huryeva I, Min SW, et al. Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteins. Proc Natl Acad Sci U S A (2003) 100:32-7. doi:10.1073/pnas.232701299.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 32-37
    • Dulubova, I.1    Yamaguchi, T.2    Arac, D.3    Li, H.4    Huryeva, I.5    Min, S.W.6
  • 40
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • doi:10.1038/35006120
    • Misura KM, Scheller RH, Weis WI. Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature (2000) 404:355-62. doi:10.1038/35006120.
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 41
    • 0033575749 scopus 로고    scopus 로고
    • A conformational switch in syntaxin during exocytosis: role of munc18
    • doi:10.1093/emboj/18.16.4372
    • Dulubova I, Sugita S, Hill S, Hosaka M, Fernandez I, Sudhof TC, et al. A conformational switch in syntaxin during exocytosis: role of munc18. EMBO J (1999) 18:4372-82. doi:10.1093/emboj/18.16.4372.
    • (1999) EMBO J , vol.18 , pp. 4372-4382
    • Dulubova, I.1    Sugita, S.2    Hill, S.3    Hosaka, M.4    Fernandez, I.5    Sudhof, T.C.6
  • 42
    • 0034603030 scopus 로고    scopus 로고
    • Synaptic assembly of the brain in the absence of neurotransmitter secretion
    • doi:10.1126/science.287.5454.864
    • Verhage M, Maia AS, Plomp JJ, Brussaard AB, Heeroma JH, Vermeer H, et al. Synaptic assembly of the brain in the absence of neurotransmitter secretion. Science (2000) 287:864-9. doi:10.1126/science.287.5454.864.
    • (2000) Science , vol.287 , pp. 864-869
    • Verhage, M.1    Maia, A.S.2    Plomp, J.J.3    Brussaard, A.B.4    Heeroma, J.H.5    Vermeer, H.6
  • 43
    • 80052247975 scopus 로고    scopus 로고
    • Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay
    • doi:10.1074/jbc.M111.269886
    • Schollmeier Y, Krause JM, Kreye S, Malsam J, Sollner TH. Resolving the function of distinct Munc18-1/SNARE protein interaction modes in a reconstituted membrane fusion assay. J Biol Chem (2011) 286:30582-90. doi:10.1074/jbc.M111.269886.
    • (2011) J Biol Chem , vol.286 , pp. 30582-30590
    • Schollmeier, Y.1    Krause, J.M.2    Kreye, S.3    Malsam, J.4    Sollner, T.H.5
  • 44
    • 84870232182 scopus 로고    scopus 로고
    • The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices-guilty as charged?
    • doi:10.1146/annurev-cellbio-101011-155818
    • Rizo J, Sudhof TC. The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices-guilty as charged? Annu Rev Cell Dev Biol (2012) 28:279-308. doi:10.1146/annurev-cellbio-101011-155818.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 279-308
    • Rizo, J.1    Sudhof, T.C.2
  • 45
    • 77957020175 scopus 로고    scopus 로고
    • Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles
    • doi:10.1146/annurev-cellbio-100109-104131
    • Wickner W. Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles. Annu Rev Cell Dev Biol (2010) 26:115-36. doi:10.1146/annurev-cellbio-100109-104131.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 115-136
    • Wickner, W.1
  • 46
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • Whyte JR, Munro S. Vesicle tethering complexes in membrane traffic. J Cell Sci (2002) 115:2627-37.
    • (2002) J Cell Sci , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 47
    • 34247623568 scopus 로고    scopus 로고
    • Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle
    • doi:10.1016/j.devcel.2007.04.005
    • Cai H, Reinisch K, Ferro-Novick S. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell (2007) 12:671-82. doi:10.1016/j.devcel.2007.04.005.
    • (2007) Dev Cell , vol.12 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 48
    • 33847648364 scopus 로고    scopus 로고
    • Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins
    • doi:10.1186/1471-2148-7-29
    • Koumandou VL, Dacks JB, Coulson RM, Field MC. Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins. BMC Evol Biol (2007) 7:29. doi:10.1186/1471-2148-7-29.
    • (2007) BMC Evol Biol , vol.7 , pp. 29
    • Koumandou, V.L.1    Dacks, J.B.2    Coulson, R.M.3    Field, M.C.4
  • 49
    • 79952103459 scopus 로고    scopus 로고
    • Transport according to GARP: receiving retrograde cargo at the trans-Golgi network
    • doi:10.1016/j.tcb.2010.11.003
    • Bonifacino JS, Hierro A. Transport according to GARP: receiving retrograde cargo at the trans-Golgi network. Trends Cell Biol (2011) 21:159-67. doi:10.1016/j.tcb.2010.11.003.
    • (2011) Trends Cell Biol , vol.21 , pp. 159-167
    • Bonifacino, J.S.1    Hierro, A.2
  • 50
    • 78049368534 scopus 로고    scopus 로고
    • Tethering factors as organizers of intracellular vesicular traffic
    • doi:10.1146/annurev.cellbio.042308.113327
    • Yu IM, Hughson FM. Tethering factors as organizers of intracellular vesicular traffic. Annu Rev Cell Dev Biol (2010) 26:137-56. doi:10.1146/annurev.cellbio.042308.113327.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 137-156
    • Yu, I.M.1    Hughson, F.M.2
  • 51
    • 77954194779 scopus 로고    scopus 로고
    • HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly
    • doi:10.1091/mbc.E10-01-0044
    • Hickey CM, Wickner W. HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Mol Biol Cell (2010) 21:2297-305. doi:10.1091/mbc.E10-01-0044.
    • (2010) Mol Biol Cell , vol.21 , pp. 2297-2305
    • Hickey, C.M.1    Wickner, W.2
  • 52
    • 84877886601 scopus 로고    scopus 로고
    • CORVET and HOPS tethering complexes-coordinators of endosome and lysosome fusion
    • doi:10.1242/jcs.107805
    • Balderhaar HJ, Ungermann C. CORVET and HOPS tethering complexes-coordinators of endosome and lysosome fusion. J Cell Sci (2013) 126:1307-16. doi:10.1242/jcs.107805.
    • (2013) J Cell Sci , vol.126 , pp. 1307-1316
    • Balderhaar, H.J.1    Ungermann, C.2
  • 53
    • 84857132605 scopus 로고    scopus 로고
    • Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex
    • doi:10.1073/pnas.1117797109
    • Brocker C, Kuhlee A, Gatsogiannis C, Balderhaar HJ, Honscher C, Engelbrecht-Vandre S, et al. Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex. Proc Natl Acad Sci U S A (2012) 109:1991-6. doi:10.1073/pnas.1117797109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1991-1996
    • Brocker, C.1    Kuhlee, A.2    Gatsogiannis, C.3    Balderhaar, H.J.4    Honscher, C.5    Engelbrecht-Vandre, S.6
  • 54
    • 84856474438 scopus 로고    scopus 로고
    • Sequential analysis of trans-SNARE formation in intracellular membrane fusion
    • doi:10.1371/journal.pbio.1001243
    • Alpadi K, Kulkarni A, Comte V, Reinhardt M, Schmidt A, Namjoshi S, et al. Sequential analysis of trans-SNARE formation in intracellular membrane fusion. PLoS Biol (2012) 10:e1001243. doi:10.1371/journal.pbio.1001243.
    • (2012) PLoS Biol , vol.10
    • Alpadi, K.1    Kulkarni, A.2    Comte, V.3    Reinhardt, M.4    Schmidt, A.5    Namjoshi, S.6
  • 55
    • 79960303122 scopus 로고    scopus 로고
    • HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites
    • doi:10.1091/mbc.E11-02-0104
    • Kramer L, Ungermann C. HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell (2011) 22:2601-11. doi:10.1091/mbc.E11-02-0104.
    • (2011) Mol Biol Cell , vol.22 , pp. 2601-2611
    • Kramer, L.1    Ungermann, C.2
  • 56
    • 84879479583 scopus 로고    scopus 로고
    • Crystal structures of the Sec1/Munc18 (SM) protein Vps33, alone and bound to the homotypic fusion and vacuolar protein sorting (HOPS) subunit Vps16*
    • doi:10.1371/journal.pone.0067409
    • Baker RW, Jeffrey PD, Hughson FM. Crystal structures of the Sec1/Munc18 (SM) protein Vps33, alone and bound to the homotypic fusion and vacuolar protein sorting (HOPS) subunit Vps16*. PLoS One (2013) 8:e67409. doi:10.1371/journal.pone.0067409.
    • (2013) PLoS One , vol.8
    • Baker, R.W.1    Jeffrey, P.D.2    Hughson, F.M.3
  • 57
    • 84862268931 scopus 로고    scopus 로고
    • Exorcising the exocyst complex
    • doi:10.1111/j.1600-0854.2012.01353.x
    • Heider MR, Munson M. Exorcising the exocyst complex. Traffic (2012) 13:898-907. doi:10.1111/j.1600-0854.2012.01353.x.
    • (2012) Traffic , vol.13 , pp. 898-907
    • Heider, M.R.1    Munson, M.2
  • 58
    • 10344263403 scopus 로고    scopus 로고
    • Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p
    • doi:10.1083/jcb.200408124
    • Boyd C, Hughes T, Pypaert M, Novick P. Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J Cell Biol (2004) 167:889-901. doi:10.1083/jcb.200408124.
    • (2004) J Cell Biol , vol.167 , pp. 889-901
    • Boyd, C.1    Hughes, T.2    Pypaert, M.3    Novick, P.4
  • 59
    • 0033558032 scopus 로고    scopus 로고
    • The sec6/8 complex is located at neurite outgrowth and axonal synapse-assembly domains
    • Hazuka CD, Foletti DL, Hsu SC, Kee Y, Hopf FW, Scheller RH. The sec6/8 complex is located at neurite outgrowth and axonal synapse-assembly domains. J Neurosci (1999) 19:1324-34.
    • (1999) J Neurosci , vol.19 , pp. 1324-1334
    • Hazuka, C.D.1    Foletti, D.L.2    Hsu, S.C.3    Kee, Y.4    Hopf, F.W.5    Scheller, R.H.6
  • 60
    • 34648823113 scopus 로고    scopus 로고
    • Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane
    • doi:10.1038/sj.emboj.7601834
    • He B, Xi F, Zhang X, Zhang J, Guo W. Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane. EMBO J (2007) 26:4053-65. doi:10.1038/sj.emboj.7601834.
    • (2007) EMBO J , vol.26 , pp. 4053-4065
    • He, B.1    Xi, F.2    Zhang, X.3    Zhang, J.4    Guo, W.5
  • 61
    • 35848947444 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate mediates the targeting of the exocyst to the plasma membrane for exocytosis in mammalian cells
    • doi:10.1091/mbc.E07-05-0461
    • Liu J, Zuo X, Yue P, Guo W. Phosphatidylinositol 4,5-bisphosphate mediates the targeting of the exocyst to the plasma membrane for exocytosis in mammalian cells. Mol Biol Cell (2007) 18:4483-92. doi:10.1091/mbc.E07-05-0461.
    • (2007) Mol Biol Cell , vol.18 , pp. 4483-4492
    • Liu, J.1    Zuo, X.2    Yue, P.3    Guo, W.4
  • 62
    • 28544432477 scopus 로고    scopus 로고
    • The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
    • Dong G, Hutagalung AH, Fu C, Novick P, Reinisch KM. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol (2005) 12:1094-100.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1094-1100
    • Dong, G.1    Hutagalung, A.H.2    Fu, C.3    Novick, P.4    Reinisch, K.M.5
  • 63
    • 17644416413 scopus 로고    scopus 로고
    • Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p
    • doi:10.1021/bi048008z
    • Sivaram MV, Saporita JA, Furgason ML, Boettcher AJ, Munson M. Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p. Biochemistry (2005) 44:6302-11. doi:10.1021/bi048008z.
    • (2005) Biochemistry , vol.44 , pp. 6302-6311
    • Sivaram, M.V.1    Saporita, J.A.2    Furgason, M.L.3    Boettcher, A.J.4    Munson, M.5
  • 64
    • 84855884898 scopus 로고    scopus 로고
    • Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
    • doi:10.1091/mbc.E11-08-0670
    • Morgera F, Sallah MR, Dubuke ML, Gandhi P, Brewer DN, Carr CM, et al. Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1. Mol Biol Cell (2012) 23:337-46. doi:10.1091/mbc.E11-08-0670.
    • (2012) Mol Biol Cell , vol.23 , pp. 337-346
    • Morgera, F.1    Sallah, M.R.2    Dubuke, M.L.3    Gandhi, P.4    Brewer, D.N.5    Carr, C.M.6
  • 65
    • 64049100409 scopus 로고    scopus 로고
    • Sec6p anchors the assembled exocyst complex at sites of secretion
    • doi:10.1091/mbc.E08-09-0968
    • Songer JA, Munson M. Sec6p anchors the assembled exocyst complex at sites of secretion. Mol Biol Cell (2009) 20:973-82. doi:10.1091/mbc.E08-09-0968.
    • (2009) Mol Biol Cell , vol.20 , pp. 973-982
    • Songer, J.A.1    Munson, M.2
  • 66
    • 24344480456 scopus 로고    scopus 로고
    • Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
    • doi:10.1091/mbc.E05-01-0056
    • Kraynack BA, Chan A, Rosenthal E, Essid M, Umansky B, Waters MG, et al. Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. Mol Biol Cell (2005) 16:3963-77. doi:10.1091/mbc.E05-01-0056.
    • (2005) Mol Biol Cell , vol.16 , pp. 3963-3977
    • Kraynack, B.A.1    Chan, A.2    Rosenthal, E.3    Essid, M.4    Umansky, B.5    Waters, M.G.6
  • 67
    • 84862241805 scopus 로고    scopus 로고
    • The DSL1 complex: the smallest but not the least CATCHR
    • doi:10.1111/j.1600-0854.2012.01362.x
    • Spang A. The DSL1 complex: the smallest but not the least CATCHR. Traffic (2012) 13:908-13. doi:10.1111/j.1600-0854.2012.01362.x.
    • (2012) Traffic , vol.13 , pp. 908-913
    • Spang, A.1
  • 68
    • 71149117138 scopus 로고    scopus 로고
    • A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1
    • doi:10.1016/j.cell.2009.11.002
    • Ren Y, Yip CK, Tripathi A, Huie D, Jeffrey PD, Walz T, et al. A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1. Cell (2009) 139:1119-29. doi:10.1016/j.cell.2009.11.002.
    • (2009) Cell , vol.139 , pp. 1119-1129
    • Ren, Y.1    Yip, C.K.2    Tripathi, A.3    Huie, D.4    Jeffrey, P.D.5    Walz, T.6
  • 69
    • 0347695021 scopus 로고    scopus 로고
    • Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat
    • doi:10.1074/jbc.M308740200
    • Andag U, Schmitt HD. Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat. J Biol Chem (2003) 278:51722-34. doi:10.1074/jbc.M308740200.
    • (2003) J Biol Chem , vol.278 , pp. 51722-51734
    • Andag, U.1    Schmitt, H.D.2
  • 70
    • 79960118861 scopus 로고    scopus 로고
    • The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation
    • doi:10.1074/jbc.M110.215327
    • Meiringer CT, Rethmeier R, Auffarth K, Wilson J, Perz A, Barlowe C, et al. The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation. J Biol Chem (2011) 286:25039-46. doi:10.1074/jbc.M110.215327.
    • (2011) J Biol Chem , vol.286 , pp. 25039-25046
    • Meiringer, C.T.1    Rethmeier, R.2    Auffarth, K.3    Wilson, J.4    Perz, A.5    Barlowe, C.6
  • 71
    • 11144354092 scopus 로고    scopus 로고
    • Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi
    • doi:10.1038/sj.emboj.7600135
    • Hirose H, Arasaki K, Dohmae N, Takio K, Hatsuzawa K, Nagahama M, et al. Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi. EMBO J (2004) 23:1267-78. doi:10.1038/sj.emboj.7600135.
    • (2004) EMBO J , vol.23 , pp. 1267-1278
    • Hirose, H.1    Arasaki, K.2    Dohmae, N.3    Takio, K.4    Hatsuzawa, K.5    Nagahama, M.6
  • 72
    • 0030857288 scopus 로고    scopus 로고
    • Stages of regulated exocytosis
    • doi:10.1016/S0962-8924(97)01060-X
    • Martin TF. Stages of regulated exocytosis. Trends Cell Biol (1997) 7:271-6. doi:10.1016/S0962-8924(97)01060-X.
    • (1997) Trends Cell Biol , vol.7 , pp. 271-276
    • Martin, T.F.1
  • 73
    • 0037174660 scopus 로고    scopus 로고
    • Emerging roles of presynaptic proteins in Ca++-triggered exocytosis
    • doi:10.1126/science.1075375
    • Rettig J, Neher E. Emerging roles of presynaptic proteins in Ca++-triggered exocytosis. Science (2002) 298:781-5. doi:10.1126/science.1075375.
    • (2002) Science , vol.298 , pp. 781-785
    • Rettig, J.1    Neher, E.2
  • 74
    • 67649871266 scopus 로고    scopus 로고
    • A common molecular basis for membrane docking and functional priming of synaptic vesicles
    • doi:10.1111/j.1460-9568.2009.06811.x
    • Siksou L, Varoqueaux F, Pascual O, Triller A, Brose N, Marty S. A common molecular basis for membrane docking and functional priming of synaptic vesicles. Eur J Neurosci (2009) 30:49-56. doi:10.1111/j.1460-9568.2009.06811.x.
    • (2009) Eur J Neurosci , vol.30 , pp. 49-56
    • Siksou, L.1    Varoqueaux, F.2    Pascual, O.3    Triller, A.4    Brose, N.5    Marty, S.6
  • 75
    • 33846942621 scopus 로고    scopus 로고
    • Primed vesicles can be distinguished from docked vesicles by analyzing their mobility
    • doi:10.1523/JNEUROSCI.4714-06.2007
    • Nofal S, Becherer U, Hof D, Matti U, Rettig J. Primed vesicles can be distinguished from docked vesicles by analyzing their mobility. J Neurosci (2007) 27:1386-95. doi:10.1523/JNEUROSCI.4714-06.2007.
    • (2007) J Neurosci , vol.27 , pp. 1386-1395
    • Nofal, S.1    Becherer, U.2    Hof, D.3    Matti, U.4    Rettig, J.5
  • 76
    • 76349098018 scopus 로고    scopus 로고
    • Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis
    • doi:10.1083/jcb.200907018
    • Walter AM, Wiederhold K, Bruns D, Fasshauer D, Sorensen JB. Synaptobrevin N-terminally bound to syntaxin-SNAP-25 defines the primed vesicle state in regulated exocytosis. J Cell Biol (2010) 188:401-13. doi:10.1083/jcb.200907018.
    • (2010) J Cell Biol , vol.188 , pp. 401-413
    • Walter, A.M.1    Wiederhold, K.2    Bruns, D.3    Fasshauer, D.4    Sorensen, J.B.5
  • 77
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • doi:10.1038/642
    • Xu T, Binz T, Niemann H, Neher E. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nat Neurosci (1998) 1:192-200. doi:10.1038/642.
    • (1998) Nat Neurosci , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 78
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • doi:10.1038/22768
    • Augustin I, Rosenmund C, Sudhof TC, Brose N. Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature (1999) 400:457-61. doi:10.1038/22768.
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Sudhof, T.C.3    Brose, N.4
  • 79
    • 0037172972 scopus 로고    scopus 로고
    • Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming
    • doi:10.1073/pnas.122623799
    • Varoqueaux F, Sigler A, Rhee JS, Brose N, Enk C, Reim K, et al. Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming. Proc Natl Acad Sci U S A (2002) 99:9037-42. doi:10.1073/pnas.122623799.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9037-9042
    • Varoqueaux, F.1    Sigler, A.2    Rhee, J.S.3    Brose, N.4    Enk, C.5    Reim, K.6
  • 80
    • 36049025863 scopus 로고    scopus 로고
    • CAPS-1 and CAPS-2 are essential synaptic vesicle priming proteins
    • doi:10.1016/j.cell.2007.11.002
    • Jockusch WJ, Speidel D, Sigler A, Sorensen JB, Varoqueaux F, Rhee JS, et al. CAPS-1 and CAPS-2 are essential synaptic vesicle priming proteins. Cell (2007) 131:796-808. doi:10.1016/j.cell.2007.11.002.
    • (2007) Cell , vol.131 , pp. 796-808
    • Jockusch, W.J.1    Speidel, D.2    Sigler, A.3    Sorensen, J.B.4    Varoqueaux, F.5    Rhee, J.S.6
  • 81
    • 0034679721 scopus 로고    scopus 로고
    • Munc13-1 acts as a priming factor for large dense-core vesicles in bovine chromaffin cells
    • doi:10.1093/emboj/19.14.3586
    • Ashery U, Varoqueaux F, Voets T, Betz A, Thakur P, Koch H, et al. Munc13-1 acts as a priming factor for large dense-core vesicles in bovine chromaffin cells. EMBO J (2000) 19:3586-96. doi:10.1093/emboj/19.14.3586.
    • (2000) EMBO J , vol.19 , pp. 3586-3596
    • Ashery, U.1    Varoqueaux, F.2    Voets, T.3    Betz, A.4    Thakur, P.5    Koch, H.6
  • 82
    • 4143099206 scopus 로고    scopus 로고
    • CAPS acts at a prefusion step in dense-core vesicle exocytosis as a PIP2 binding protein
    • doi:10.1016/j.neuron.2004.07.028
    • Grishanin RN, Kowalchyk JA, Klenchin VA, Ann K, Earles CA, Chapman ER, et al. CAPS acts at a prefusion step in dense-core vesicle exocytosis as a PIP2 binding protein. Neuron (2004) 43:551-62. doi:10.1016/j.neuron.2004.07.028.
    • (2004) Neuron , vol.43 , pp. 551-562
    • Grishanin, R.N.1    Kowalchyk, J.A.2    Klenchin, V.A.3    Ann, K.4    Earles, C.A.5    Chapman, E.R.6
  • 83
    • 45849136363 scopus 로고    scopus 로고
    • CAPS facilitates filling of the rapidly releasable pool of large dense-core vesicles
    • doi:10.1523/JNEUROSCI.5672-07.2008
    • Liu Y, Schirra C, Stevens DR, Matti U, Speidel D, Hof D, et al. CAPS facilitates filling of the rapidly releasable pool of large dense-core vesicles. J Neurosci (2008) 28:5594-601. doi:10.1523/JNEUROSCI.5672-07.2008.
    • (2008) J Neurosci , vol.28 , pp. 5594-5601
    • Liu, Y.1    Schirra, C.2    Stevens, D.R.3    Matti, U.4    Speidel, D.5    Hof, D.6
  • 84
    • 0035974886 scopus 로고    scopus 로고
    • Munc18-1 promotes large dense-core vesicle docking
    • doi:10.1016/S0896-6273(01)00391-9
    • Voets T, Toonen RF, Brian EC, de Wit H, Moser T, Rettig J, et al. Munc18-1 promotes large dense-core vesicle docking. Neuron (2001) 31:581-91. doi:10.1016/S0896-6273(01)00391-9.
    • (2001) Neuron , vol.31 , pp. 581-591
    • Voets, T.1    Toonen, R.F.2    Brian, E.C.3    de Wit, H.4    Moser, T.5    Rettig, J.6
  • 85
    • 0034235922 scopus 로고    scopus 로고
    • Definition of Munc13-homology-domains and characterization of a novel ubiquitously expressed Munc13 isoform
    • doi:10.1042/0264-6021:3490247
    • Koch H, Hofmann K, Brose N. Definition of Munc13-homology-domains and characterization of a novel ubiquitously expressed Munc13 isoform. Biochem J (2000) 349:247-53. doi:10.1042/0264-6021:3490247.
    • (2000) Biochem J , vol.349 , pp. 247-253
    • Koch, H.1    Hofmann, K.2    Brose, N.3
  • 86
    • 0026722645 scopus 로고
    • A novel 145 kd brain cytosolic protein reconstitutes Ca(2+)-regulated secretion in permeable neuroendocrine cells
    • doi:10.1016/0092-8674(92)90310-9
    • Walent JH, Porter BW, Martin TF. A novel 145 kd brain cytosolic protein reconstitutes Ca(2+)-regulated secretion in permeable neuroendocrine cells. Cell (1992) 70:765-75. doi:10.1016/0092-8674(92)90310-9.
    • (1992) Cell , vol.70 , pp. 765-775
    • Walent, J.H.1    Porter, B.W.2    Martin, T.F.3
  • 87
    • 0030611081 scopus 로고    scopus 로고
    • Novel Ca2+-binding protein (CAPS) related to UNC-31 required for Ca2+-activated exocytosis
    • doi:10.1074/jbc.272.32.19637
    • Ann K, Kowalchyk JA, Loyet KM, Martin TF. Novel Ca2+-binding protein (CAPS) related to UNC-31 required for Ca2+-activated exocytosis. J Biol Chem (1997) 272:19637-40. doi:10.1074/jbc.272.32.19637.
    • (1997) J Biol Chem , vol.272 , pp. 19637-19640
    • Ann, K.1    Kowalchyk, J.A.2    Loyet, K.M.3    Martin, T.F.4
  • 88
    • 39049104478 scopus 로고    scopus 로고
    • CAPS and syntaxin dock dense core vesicles to the plasma membrane in neurons
    • doi:10.1083/jcb.200708018
    • Hammarlund M, Watanabe S, Schuske K, Jorgensen EM. CAPS and syntaxin dock dense core vesicles to the plasma membrane in neurons. J Cell Biol (2008) 180:483-91. doi:10.1083/jcb.200708018.
    • (2008) J Cell Biol , vol.180 , pp. 483-491
    • Hammarlund, M.1    Watanabe, S.2    Schuske, K.3    Jorgensen, E.M.4
  • 89
    • 34250020729 scopus 로고    scopus 로고
    • UNC-31 (CAPS) is required for dense-core vesicle but not synaptic vesicle exocytosis in Caenorhabditis elegans
    • doi:10.1523/JNEUROSCI.1466-07.2007
    • Speese S, Petrie M, Schuske K, Ailion M, Ann K, Iwasaki K, et al. UNC-31 (CAPS) is required for dense-core vesicle but not synaptic vesicle exocytosis in Caenorhabditis elegans. J Neurosci (2007) 27:6150-62. doi:10.1523/JNEUROSCI.1466-07.2007.
    • (2007) J Neurosci , vol.27 , pp. 6150-6162
    • Speese, S.1    Petrie, M.2    Schuske, K.3    Ailion, M.4    Ann, K.5    Iwasaki, K.6
  • 90
    • 36148956730 scopus 로고    scopus 로고
    • PKA activation bypasses the requirement for UNC-31 in the docking of dense core vesicles from C
    • doi:10.1016/j.neuron.2007.09.015
    • Zhou KM, Dong YM, Ge Q, Zhu D, Zhou W, Lin XG, et al. PKA activation bypasses the requirement for UNC-31 in the docking of dense core vesicles from C. elegans neurons. Neuron (2007) 56:657-69. doi:10.1016/j.neuron.2007.09.015.
    • (2007) elegans neurons. Neuron , vol.56 , pp. 657-669
    • Zhou, K.M.1    Dong, Y.M.2    Ge, Q.3    Zhu, D.4    Zhou, W.5    Lin, X.G.6
  • 91
    • 33644785908 scopus 로고    scopus 로고
    • Presynaptic UNC-31 (CAPS) is required to activate the G alpha(s) pathway of the Caenorhabditis elegans synaptic signaling network
    • doi:10.1534/genetics.105.049577
    • Charlie NK, Schade MA, Thomure AM, Miller KG. Presynaptic UNC-31 (CAPS) is required to activate the G alpha(s) pathway of the Caenorhabditis elegans synaptic signaling network. Genetics (2006) 172:943-61. doi:10.1534/genetics.105.049577.
    • (2006) Genetics , vol.172 , pp. 943-961
    • Charlie, N.K.1    Schade, M.A.2    Thomure, A.M.3    Miller, K.G.4
  • 92
    • 34548842752 scopus 로고    scopus 로고
    • Tomosyn negatively regulates CAPS-dependent peptide release at Caenorhabditis elegans synapses
    • doi:10.1523/JNEUROSCI.2339-07.2007
    • Gracheva EO, Burdina AO, Touroutine D, Berthelot-Grosjean M, Parekh H, Richmond JE. Tomosyn negatively regulates CAPS-dependent peptide release at Caenorhabditis elegans synapses. J Neurosci (2007) 27:10176-84. doi:10.1523/JNEUROSCI.2339-07.2007.
    • (2007) J Neurosci , vol.27 , pp. 10176-10184
    • Gracheva, E.O.1    Burdina, A.O.2    Touroutine, D.3    Berthelot-Grosjean, M.4    Parekh, H.5    Richmond, J.E.6
  • 93
    • 0033349884 scopus 로고    scopus 로고
    • UNC-13 is required for synaptic vesicle fusion in C
    • doi:10.1038/12160
    • Richmond JE, Davis WS, Jorgensen EM. UNC-13 is required for synaptic vesicle fusion in C. elegans. Nat Neurosci (1999) 2:959-64. doi:10.1038/12160.
    • (1999) elegans. Nat Neurosci , vol.2 , pp. 959-964
    • Richmond, J.E.1    Davis, W.S.2    Jorgensen, E.M.3
  • 94
    • 33845881679 scopus 로고    scopus 로고
    • PKC-1 regulates secretion of neuropeptides
    • doi:10.1038/nn1810
    • Sieburth D, Madison JM, Kaplan JM. PKC-1 regulates secretion of neuropeptides. Nat Neurosci (2007) 10:49-57. doi:10.1038/nn1810.
    • (2007) Nat Neurosci , vol.10 , pp. 49-57
    • Sieburth, D.1    Madison, J.M.2    Kaplan, J.M.3
  • 95
    • 34547105832 scopus 로고    scopus 로고
    • Ca2+-dependent activator protein for secretion 1 is critical for constitutive and regulated exocytosis but not for loading of transmitters into dense core vesicles
    • doi:10.1074/jbc.M703699200
    • Fujita Y, Xu A, Xie L, Arunachalam L, Chou TC, Jiang T, et al. Ca2+-dependent activator protein for secretion 1 is critical for constitutive and regulated exocytosis but not for loading of transmitters into dense core vesicles. J Biol Chem (2007) 282:21392-403. doi:10.1074/jbc.M703699200.
    • (2007) J Biol Chem , vol.282 , pp. 21392-21403
    • Fujita, Y.1    Xu, A.2    Xie, L.3    Arunachalam, L.4    Chou, T.C.5    Jiang, T.6
  • 96
    • 67650514336 scopus 로고    scopus 로고
    • CAPS activity in priming vesicle exocytosis requires CK2 phosphorylation
    • doi:10.1074/jbc.M109.017483
    • Nojiri M, Loyet KM, Klenchin VA, Kabachinski G, Martin TF. CAPS activity in priming vesicle exocytosis requires CK2 phosphorylation. J Biol Chem (2009) 284:18707-14. doi:10.1074/jbc.M109.017483.
    • (2009) J Biol Chem , vol.284 , pp. 18707-18714
    • Nojiri, M.1    Loyet, K.M.2    Klenchin, V.A.3    Kabachinski, G.4    Martin, T.F.5
  • 97
    • 0038303159 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase serves as a metabolic sensor and regulates priming of secretory granules in pancreatic beta cells
    • doi:10.1073/pnas.0931282100
    • Olsen HL, Hoy M, Zhang W, Bertorello AM, Bokvist K, Capito K, et al. Phosphatidylinositol 4-kinase serves as a metabolic sensor and regulates priming of secretory granules in pancreatic beta cells. Proc Natl Acad Sci U S A (2003) 100:5187-92. doi:10.1073/pnas.0931282100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5187-5192
    • Olsen, H.L.1    Hoy, M.2    Zhang, W.3    Bertorello, A.M.4    Bokvist, K.5    Capito, K.6
  • 98
    • 0842344424 scopus 로고    scopus 로고
    • The secretory granule-associated protein CAPS2 regulates neurotrophin release and cell survival
    • doi:10.1523/JNEUROSCI.2528-03.2004
    • Sadakata T, Mizoguchi A, Sato Y, Katoh-Semba R, Fukuda M, Mikoshiba K, et al. The secretory granule-associated protein CAPS2 regulates neurotrophin release and cell survival. J Neurosci (2004) 24:43-52. doi:10.1523/JNEUROSCI.2528-03.2004.
    • (2004) J Neurosci , vol.24 , pp. 43-52
    • Sadakata, T.1    Mizoguchi, A.2    Sato, Y.3    Katoh-Semba, R.4    Fukuda, M.5    Mikoshiba, K.6
  • 99
    • 37449005991 scopus 로고    scopus 로고
    • CAPS1 and CAPS2 regulate stability and recruitment of insulin granules in mouse pancreatic beta cells
    • doi:10.1016/j.cmet.2007.11.009
    • Speidel D, Salehi A, Obermueller S, Lundquist I, Brose N, Renstrom E, et al. CAPS1 and CAPS2 regulate stability and recruitment of insulin granules in mouse pancreatic beta cells. Cell Metab (2008) 7:57-67. doi:10.1016/j.cmet.2007.11.009.
    • (2008) Cell Metab , vol.7 , pp. 57-67
    • Speidel, D.1    Salehi, A.2    Obermueller, S.3    Lundquist, I.4    Brose, N.5    Renstrom, E.6
  • 100
    • 28144450659 scopus 로고    scopus 로고
    • Role of phosphoinositide signaling in the control of insulin exocytosis
    • doi:10.1210/me.2004-0530
    • Waselle L, Gerona RR, Vitale N, Martin TF, Bader MF, Regazzi R. Role of phosphoinositide signaling in the control of insulin exocytosis. Mol Endocrinol (2005) 19:3097-106. doi:10.1210/me.2004-0530.
    • (2005) Mol Endocrinol , vol.19 , pp. 3097-3106
    • Waselle, L.1    Gerona, R.R.2    Vitale, N.3    Martin, T.F.4    Bader, M.F.5    Regazzi, R.6
  • 101
    • 33744504875 scopus 로고    scopus 로고
    • Munc13-1 is required for the sustained release of insulin from pancreatic beta cells
    • doi:10.1016/j.cmet.2006.04.012
    • Kang L, He Z, Xu P, Fan J, Betz A, Brose N, et al. Munc13-1 is required for the sustained release of insulin from pancreatic beta cells. Cell Metab (2006) 3:463-8. doi:10.1016/j.cmet.2006.04.012.
    • (2006) Cell Metab , vol.3 , pp. 463-468
    • Kang, L.1    He, Z.2    Xu, P.3    Fan, J.4    Betz, A.5    Brose, N.6
  • 102
    • 33745291822 scopus 로고    scopus 로고
    • Munc13-1 deficiency reduces insulin secretion and causes abnormal glucose tolerance
    • doi:10.2337/db05-1263
    • Kwan EP, Xie L, Sheu L, Nolan CJ, Prentki M, Betz A, et al. Munc13-1 deficiency reduces insulin secretion and causes abnormal glucose tolerance. Diabetes (2006) 55:1421-9. doi:10.2337/db05-1263.
    • (2006) Diabetes , vol.55 , pp. 1421-1429
    • Kwan, E.P.1    Xie, L.2    Sheu, L.3    Nolan, C.J.4    Prentki, M.5    Betz, A.6
  • 103
    • 0032126752 scopus 로고    scopus 로고
    • CAPS (mammalian UNC-31) protein localizes to membranes involved in dense-core vesicle exocytosis
    • doi:10.1016/S0896-6273(00)80521-8
    • Berwin B, Floor E, Martin TF. CAPS (mammalian UNC-31) protein localizes to membranes involved in dense-core vesicle exocytosis. Neuron (1998) 21:137-45. doi:10.1016/S0896-6273(00)80521-8.
    • (1998) Neuron , vol.21 , pp. 137-145
    • Berwin, B.1    Floor, E.2    Martin, T.F.3
  • 104
    • 78149244169 scopus 로고    scopus 로고
    • Novel interactions of CAPS (Ca2+-dependent activator protein for secretion) with the three neuronal SNARE proteins required for vesicle fusion
    • doi:10.1074/jbc.M110.145169
    • Daily NJ, Boswell KL, James DJ, Martin TF. Novel interactions of CAPS (Ca2+-dependent activator protein for secretion) with the three neuronal SNARE proteins required for vesicle fusion. J Biol Chem (2010) 285:35320-9. doi:10.1074/jbc.M110.145169.
    • (2010) J Biol Chem , vol.285 , pp. 35320-35329
    • Daily, N.J.1    Boswell, K.L.2    James, D.J.3    Martin, T.F.4
  • 105
    • 77955283450 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulation of SNARE function in membrane fusion mediated by CAPS
    • doi:10.1016/j.advenzreg.2009.10.012
    • James DJ, Khodthong C, Kowalchyk JA, Martin TF. Phosphatidylinositol 4,5-bisphosphate regulation of SNARE function in membrane fusion mediated by CAPS. Adv Enzyme Regul (2010) 50:62-70. doi:10.1016/j.advenzreg.2009.10.012.
    • (2010) Adv Enzyme Regul , vol.50 , pp. 62-70
    • James, D.J.1    Khodthong, C.2    Kowalchyk, J.A.3    Martin, T.F.4
  • 106
    • 70350436474 scopus 로고    scopus 로고
    • CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactions
    • doi:10.1073/pnas.0900755106
    • James DJ, Kowalchyk J, Daily N, Petrie M, Martin TF. CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactions. Proc Natl Acad Sci U S A (2009) 106:17308-13. doi:10.1073/pnas.0900755106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 17308-17313
    • James, D.J.1    Kowalchyk, J.2    Daily, N.3    Petrie, M.4    Martin, T.F.5
  • 107
    • 79960937914 scopus 로고    scopus 로고
    • Munc13 homology domain-1 in CAPS/UNC31 mediates SNARE binding required for priming vesicle exocytosis
    • doi:10.1016/j.cmet.2011.07.002
    • Khodthong C, Kabachinski G, James DJ, Martin TF. Munc13 homology domain-1 in CAPS/UNC31 mediates SNARE binding required for priming vesicle exocytosis. Cell Metab (2011) 14:254-63. doi:10.1016/j.cmet.2011.07.002.
    • (2011) Cell Metab , vol.14 , pp. 254-263
    • Khodthong, C.1    Kabachinski, G.2    James, D.J.3    Martin, T.F.4
  • 109
    • 84881407314 scopus 로고    scopus 로고
    • Calcium-dependent activator protein for secretion 1 (CAPS1) binds to syntaxin-1 in a distinct mode from Munc13-1
    • doi:10.1074/jbc.M113.494088
    • Parsaud L, Li L, Jung CH, Park S, Saw NM, Park S, et al. Calcium-dependent activator protein for secretion 1 (CAPS1) binds to syntaxin-1 in a distinct mode from Munc13-1. J Biol Chem (2013) 288(32):23050-63. doi:10.1074/jbc.M113.494088.
    • (2013) J Biol Chem , vol.288 , Issue.32 , pp. 23050-23063
    • Parsaud, L.1    Li, L.2    Jung, C.H.3    Park, S.4    Saw, N.M.5    Park, S.6
  • 110
    • 35948934236 scopus 로고    scopus 로고
    • Regulation of atrial natriuretic peptide secretion by a novel Ras-like protein
    • doi:10.1083/jcb.200707101
    • Rybkin II, Kim MS, Bezprozvannaya S, Qi X, Richardson JA, Plato CF, et al. Regulation of atrial natriuretic peptide secretion by a novel Ras-like protein. J Cell Biol (2007) 179:527-37. doi:10.1083/jcb.200707101.
    • (2007) J Cell Biol , vol.179 , pp. 527-537
    • Rybkin, I.I.1    Kim, M.S.2    Bezprozvannaya, S.3    Qi, X.4    Richardson, J.A.5    Plato, C.F.6
  • 111
    • 0032478796 scopus 로고    scopus 로고
    • Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis
    • doi:10.1074/jbc.273.14.8337
    • Loyet KM, Kowalchyk JA, Chaudhary A, Chen J, Prestwich GD, Martin TF. Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis. J Biol Chem (1998) 273:8337-43. doi:10.1074/jbc.273.14.8337.
    • (1998) J Biol Chem , vol.273 , pp. 8337-8343
    • Loyet, K.M.1    Kowalchyk, J.A.2    Chaudhary, A.3    Chen, J.4    Prestwich, G.D.5    Martin, T.F.6
  • 112
    • 0037077255 scopus 로고    scopus 로고
    • Membrane association domains in Ca2+-dependent activator protein for secretion mediate plasma membrane and dense-core vesicle binding required for Ca2+-dependent exocytosis
    • doi:10.1074/jbc.M201614200
    • Grishanin RN, Klenchin VA, Loyet KM, Kowalchyk JA, Ann K, Martin TF. Membrane association domains in Ca2+-dependent activator protein for secretion mediate plasma membrane and dense-core vesicle binding required for Ca2+-dependent exocytosis. J Biol Chem (2002) 277:22025-34. doi:10.1074/jbc.M201614200.
    • (2002) J Biol Chem , vol.277 , pp. 22025-22034
    • Grishanin, R.N.1    Klenchin, V.A.2    Loyet, K.M.3    Kowalchyk, J.A.4    Ann, K.5    Martin, T.F.6
  • 113
    • 1642546578 scopus 로고    scopus 로고
    • Insulinoma-associated protein IA-2, a vesicle transmembrane protein, genetically interacts with UNC-31/CAPS and affects neurosecretion in Caenorhabditis elegans
    • doi:10.1523/JNEUROSCI.0101-04.2004
    • Cai T, Fukushige T, Notkins AL, Krause M. Insulinoma-associated protein IA-2, a vesicle transmembrane protein, genetically interacts with UNC-31/CAPS and affects neurosecretion in Caenorhabditis elegans. J Neurosci (2004) 24:3115-24. doi:10.1523/JNEUROSCI.0101-04.2004.
    • (2004) J Neurosci , vol.24 , pp. 3115-3124
    • Cai, T.1    Fukushige, T.2    Notkins, A.L.3    Krause, M.4
  • 114
    • 59449096121 scopus 로고    scopus 로고
    • Ca2+-dependent activator proteins of secretion promote vesicular monoamine uptake
    • doi:10.1074/jbc.M805328200
    • Brunk I, Blex C, Speidel D, Brose N, Ahnert-Hilger G. Ca2+-dependent activator proteins of secretion promote vesicular monoamine uptake. J Biol Chem (2009) 284:1050-6. doi:10.1074/jbc.M805328200.
    • (2009) J Biol Chem , vol.284 , pp. 1050-1056
    • Brunk, I.1    Blex, C.2    Speidel, D.3    Brose, N.4    Ahnert-Hilger, G.5
  • 115
    • 84856086841 scopus 로고    scopus 로고
    • Calcium-dependent activator protein for secretion 2 interacts with the class II ARF small GTPases and regulates dense-core vesicle trafficking
    • doi:10.1111/j.1742-4658.2011.08431.x
    • Sadakata T, Sekine Y, Oka M, Itakura M, Takahashi M, Furuichi T. Calcium-dependent activator protein for secretion 2 interacts with the class II ARF small GTPases and regulates dense-core vesicle trafficking. FEBS J (2012) 279:384-94. doi:10.1111/j.1742-4658.2011.08431.x.
    • (2012) FEBS J , vol.279 , pp. 384-394
    • Sadakata, T.1    Sekine, Y.2    Oka, M.3    Itakura, M.4    Takahashi, M.5    Furuichi, T.6
  • 116
    • 78649681291 scopus 로고    scopus 로고
    • Interaction of calcium-dependent activator protein for secretion 1 (CAPS1) with the class II ADP-ribosylation factor small GTPases is required for dense-core vesicle trafficking in the trans-Golgi network
    • doi:10.1074/jbc.M110.137414
    • Sadakata T, Shinoda Y, Sekine Y, Saruta C, Itakura M, Takahashi M, et al. Interaction of calcium-dependent activator protein for secretion 1 (CAPS1) with the class II ADP-ribosylation factor small GTPases is required for dense-core vesicle trafficking in the trans-Golgi network. J Biol Chem (2010) 285:38710-9. doi:10.1074/jbc.M110.137414.
    • (2010) J Biol Chem , vol.285 , pp. 38710-38719
    • Sadakata, T.1    Shinoda, Y.2    Sekine, Y.3    Saruta, C.4    Itakura, M.5    Takahashi, M.6
  • 117
    • 10744224641 scopus 로고    scopus 로고
    • Munc13-4 is essential for cytolytic granules fusion and is mutated in a form of familial hemophagocytic lymphohistiocytosis (FHL3)
    • doi:10.1016/S0092-8674(03)00855-9
    • Feldmann J, Callebaut I, Raposo G, Certain S, Bacq D, Dumont C, et al. Munc13-4 is essential for cytolytic granules fusion and is mutated in a form of familial hemophagocytic lymphohistiocytosis (FHL3). Cell (2003) 115:461-73. doi:10.1016/S0092-8674(03)00855-9.
    • (2003) Cell , vol.115 , pp. 461-473
    • Feldmann, J.1    Callebaut, I.2    Raposo, G.3    Certain, S.4    Bacq, D.5    Dumont, C.6
  • 118
    • 80051639052 scopus 로고    scopus 로고
    • The munc13-4-rab27 complex is specifically required for tethering secretory lysosomes at the plasma membrane
    • doi:10.1182/blood-2011-02-339523
    • Elstak ED, Neeft M, Nehme NT, Voortman J, Cheung M, Goodarzifard M, et al. The munc13-4-rab27 complex is specifically required for tethering secretory lysosomes at the plasma membrane. Blood (2011) 118:1570-8. doi:10.1182/blood-2011-02-339523.
    • (2011) Blood , vol.118 , pp. 1570-1578
    • Elstak, E.D.1    Neeft, M.2    Nehme, N.T.3    Voortman, J.4    Cheung, M.5    Goodarzifard, M.6
  • 119
    • 19944430653 scopus 로고    scopus 로고
    • Munc13-4 is an effector of rab27a and controls secretion of lysosomes in hematopoietic cells
    • doi:10.1091/mbc.E04-10-0923
    • Neeft M, Wieffer M, de Jong AS, Negroiu G, Metz CH, van Loon A, et al. Munc13-4 is an effector of rab27a and controls secretion of lysosomes in hematopoietic cells. Mol Biol Cell (2005) 16:731-41. doi:10.1091/mbc.E04-10-0923.
    • (2005) Mol Biol Cell , vol.16 , pp. 731-741
    • Neeft, M.1    Wieffer, M.2    de Jong, A.S.3    Negroiu, G.4    Metz, C.H.5    van Loon, A.6
  • 120
    • 84861922902 scopus 로고    scopus 로고
    • Munc13-4 reconstitutes calcium-dependent SNARE-mediated membrane fusion
    • doi:10.1083/jcb.201109132
    • Boswell KL, James DJ, Esquibel JM, Bruinsma S, Shirakawa R, Horiuchi H, et al. Munc13-4 reconstitutes calcium-dependent SNARE-mediated membrane fusion. J Cell Biol (2012) 197:301-12. doi:10.1083/jcb.201109132.
    • (2012) J Cell Biol , vol.197 , pp. 301-312
    • Boswell, K.L.1    James, D.J.2    Esquibel, J.M.3    Bruinsma, S.4    Shirakawa, R.5    Horiuchi, H.6
  • 121
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin
    • doi:10.1074/jbc.272.4.2520
    • Betz A, Okamoto M, Benseler F, Brose N. Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. J Biol Chem (1997) 272:2520-6. doi:10.1074/jbc.272.4.2520.
    • (1997) J Biol Chem , vol.272 , pp. 2520-2526
    • Betz, A.1    Okamoto, M.2    Benseler, F.3    Brose, N.4
  • 122
    • 29044435309 scopus 로고    scopus 로고
    • Identification of the minimal protein domain required for priming activity of Munc13-1
    • doi:10.1016/j.cub.2005.10.055
    • Stevens DR, Wu ZX, Matti U, Junge HJ, Schirra C, Becherer U, et al. Identification of the minimal protein domain required for priming activity of Munc13-1. Curr Biol (2005) 15:2243-8. doi:10.1016/j.cub.2005.10.055.
    • (2005) Curr Biol , vol.15 , pp. 2243-2248
    • Stevens, D.R.1    Wu, Z.X.2    Matti, U.3    Junge, H.J.4    Schirra, C.5    Becherer, U.6
  • 123
    • 38949089701 scopus 로고    scopus 로고
    • Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes
    • doi:10.1021/bi702345m
    • Guan R, Dai H, Rizo J. Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes. Biochemistry (2008) 47:1474-81. doi:10.1021/bi702345m.
    • (2008) Biochemistry , vol.47 , pp. 1474-1481
    • Guan, R.1    Dai, H.2    Rizo, J.3
  • 124
    • 38949211822 scopus 로고    scopus 로고
    • Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex
    • doi:10.1016/j.str.2007.12.010
    • Weninger K, Bowen ME, Choi UB, Chu S, Brunger AT. Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin/SNAP-25 complex. Structure (2008) 16:308-20. doi:10.1016/j.str.2007.12.010.
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3    Chu, S.4    Brunger, A.T.5
  • 125
    • 85027945821 scopus 로고    scopus 로고
    • Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex
    • doi:10.1038/nsmb.2047
    • Ma C, Li W, Xu Y, Rizo J. Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex. Nat Struct Mol Biol (2011) 18:542-9. doi:10.1038/nsmb.2047.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 542-549
    • Ma, C.1    Li, W.2    Xu, Y.3    Rizo, J.4
  • 126
    • 84872802734 scopus 로고    scopus 로고
    • Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release
    • doi:10.1126/science.1230473
    • Ma C, Su L, Seven AB, Xu Y, Rizo J. Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release. Science (2013) 339:421-5. doi:10.1126/science.1230473.
    • (2013) Science , vol.339 , pp. 421-425
    • Ma, C.1    Su, L.2    Seven, A.B.3    Xu, Y.4    Rizo, J.5
  • 128
    • 77949266565 scopus 로고    scopus 로고
    • Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis
    • doi:10.1038/nsmb.1758
    • Shin OH, Lu J, Rhee JS, Tomchick DR, Pang ZP, Wojcik SM, et al. Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis. Nat Struct Mol Biol (2010) 17:280-8. doi:10.1038/nsmb.1758.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 280-288
    • Shin, O.H.1    Lu, J.2    Rhee, J.S.3    Tomchick, D.R.4    Pang, Z.P.5    Wojcik, S.M.6
  • 129
    • 33846144743 scopus 로고    scopus 로고
    • Potentiation of exocytosis by phospholipase C-coupled G-protein-coupled receptors requires the priming protein Munc13-1
    • doi:10.1523/JNEUROSCI.4201-06.2007
    • Bauer CS, Woolley RJ, Teschemacher AG, Seward EP. Potentiation of exocytosis by phospholipase C-coupled G-protein-coupled receptors requires the priming protein Munc13-1. J Neurosci (2007) 27:212-9. doi:10.1523/JNEUROSCI.4201-06.2007.
    • (2007) J Neurosci , vol.27 , pp. 212-219
    • Bauer, C.S.1    Woolley, R.J.2    Teschemacher, A.G.3    Seward, E.P.4
  • 130
    • 70349876488 scopus 로고    scopus 로고
    • A protein interaction node at the neurotransmitter release site: domains of Aczonin/Piccolo, Bassoon, CAST, and rim converge on the N-terminal domain of Munc13-1
    • doi:10.1523/JNEUROSCI.1255-09.2009
    • Wang X, Hu B, Zieba A, Neumann NG, Kasper-Sonnenberg M, Honsbein A, et al. A protein interaction node at the neurotransmitter release site: domains of Aczonin/Piccolo, Bassoon, CAST, and rim converge on the N-terminal domain of Munc13-1. J Neurosci (2009) 29:12584-96. doi:10.1523/JNEUROSCI.1255-09.2009.
    • (2009) J Neurosci , vol.29 , pp. 12584-12596
    • Wang, X.1    Hu, B.2    Zieba, A.3    Neumann, N.G.4    Kasper-Sonnenberg, M.5    Honsbein, A.6
  • 131
    • 28844449520 scopus 로고    scopus 로고
    • A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?
    • doi:10.1038/sj.emboj.7600753
    • Dulubova I, Lou X, Lu J, Huryeva I, Alam A, Schneggenburger R, et al. A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity? EMBO J (2005) 24:2839-50. doi:10.1038/sj.emboj.7600753.
    • (2005) EMBO J , vol.24 , pp. 2839-2850
    • Dulubova, I.1    Lou, X.2    Lu, J.3    Huryeva, I.4    Alam, A.5    Schneggenburger, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.