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Volumn 1744, Issue 2, 2005, Pages 120-144

Erratum: SNAREs and traffic (Biochimica et Biophysica Acta (2005) 1744 (120-144) PII: S0167488905000571 and DOI: 10.1016/j.bbamcr.2005.03.014);SNAREs and traffic

Author keywords

Endocytosis; Exocytosis; Membrane traffic; Soluble N ethylmaleimide sensitive factor attachment protein receptor; Synaptic transmission; Vesicle fusion

Indexed keywords

PROTEIN SM; SNARE PROTEIN; SYNAPTOPHYSIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNAPTOTAGMIN;

EID: 20444407298     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2005.06.006     Document Type: Erratum
Times cited : (385)

References (166)
  • 1
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • J.S. Bonifacino, and B.S. Glick The mechanisms of vesicle budding and fusion Cell 116 2004 153 166
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 7
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 a resolution
    • R.B. Sutton, D. Fasshauer, R. Jahn, and A.T. Brunger Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution Nature 395 1998 347 353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 8
    • 0036166318 scopus 로고    scopus 로고
    • Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
    • W. Antonin, D. Fasshauer, S. Becker, R. Jahn, and T.R. Schneider Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs Nat. Struct. Biol. 9 2002 107 111
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 107-111
    • Antonin, W.1    Fasshauer, D.2    Becker, S.3    Jahn, R.4    Schneider, T.R.5
  • 9
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • E. Mossessova, L.C. Bickford, and J. Goldberg SNARE selectivity of the COPII coat Cell 114 2003 483 495
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 10
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • E.A. Miller, T.H. Beilharz, P.N. Malkus, M.C. Lee, S. Hamamoto, L. Orci, and R. Schekman Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles Cell 114 2003 497 509
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 11
    • 0037193471 scopus 로고    scopus 로고
    • ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • U. Rein, U. Andag, R. Duden, H.D. Schmitt, and A. Spang ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat J. Cell Biol. 157 2002 395 404
    • (2002) J. Cell Biol. , vol.157 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 13
    • 7944229497 scopus 로고    scopus 로고
    • Synaptobrevin is essential for fast synaptic-vesicle endocytosis
    • F. Deak, S. Schoch, X. Liu, T.C. Sudhof, and E.T. Kavalali Synaptobrevin is essential for fast synaptic-vesicle endocytosis Nat. Cell Biol. 6 2004 1102 1108
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1102-1108
    • Deak, F.1    Schoch, S.2    Liu, X.3    Sudhof, T.C.4    Kavalali, E.T.5
  • 14
    • 0043162027 scopus 로고    scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • A.K. Gillingham, and S. Munro Long coiled-coil proteins and membrane traffic Biochim. Biophys. Acta 1641 2003 71 85
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 15
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • J.R. Whyte, and S. Munro Vesicle tethering complexes in membrane traffic J. Cell Sci. 115 2002 2627 2637
    • (2002) J. Cell Sci. , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 16
    • 0036544571 scopus 로고    scopus 로고
    • Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115
    • J. Shorter, M.B. Beard, J. Seemann, A.B. Dirac-Svejstrup, and G. Warren Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115 J. Cell Biol. 157 2002 45 62
    • (2002) J. Cell Biol. , vol.157 , pp. 45-62
    • Shorter, J.1    Beard, M.B.2    Seemann, J.3    Dirac-Svejstrup, A.B.4    Warren, G.5
  • 18
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • R. Jahn, T. Lang, and T.C. Sudhof Membrane fusion Cell 112 2003 519 533
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 19
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • T.C. Sudhof The synaptic vesicle cycle Annu. Rev. Neurosci. 27 2004 509 547
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 20
    • 0036780223 scopus 로고    scopus 로고
    • Lasker basic medical research award. the machinery and principles of vesicle transport in the cell
    • J.E. Rothman Lasker basic medical research award. The machinery and principles of vesicle transport in the cell Nat. Med. 8 2002 1059 1062
    • (2002) Nat. Med. , vol.8 , pp. 1059-1062
    • Rothman, J.E.1
  • 21
    • 0032214690 scopus 로고    scopus 로고
    • Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes
    • T.M. Hohl, F. Parlati, C. Wimmer, J.E. Rothman, T.H. Sollner, and H. Engelhardt Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes Mol. Cell 2 1998 539 548
    • (1998) Mol. Cell , vol.2 , pp. 539-548
    • Hohl, T.M.1    Parlati, F.2    Wimmer, C.3    Rothman, J.E.4    Sollner, T.H.5    Engelhardt, H.6
  • 23
    • 0041736713 scopus 로고    scopus 로고
    • Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 a resolution
    • J. Furst, R.B. Sutton, J. Chen, A.T. Brunger, and N. Grigorieff Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 A resolution EMBO J. 22 2003 4365 4374
    • (2003) EMBO J. , vol.22 , pp. 4365-4374
    • Furst, J.1    Sutton, R.B.2    Chen, J.3    Brunger, A.T.4    Grigorieff, N.5
  • 24
    • 0242573090 scopus 로고    scopus 로고
    • NSF and p97/VCP: Similar at first, different at last
    • A.T. Brunger, and B. DeLaBarre NSF and p97/VCP: Similar at first, different at last FEBS Lett. 555 2003 126 133
    • (2003) FEBS Lett. , vol.555 , pp. 126-133
    • Brunger, A.T.1    Delabarre, B.2
  • 25
    • 12644298688 scopus 로고    scopus 로고
    • A conserved domain is present in different families of vesicular fusion proteins: A new superfamily
    • T. Weimbs, S.H. Low, S.J. Chapin, K.E. Mostov, P. Bucher, and K. Hofmann A conserved domain is present in different families of vesicular fusion proteins: a new superfamily Proc. Natl. Acad. Sci. 94 1997 3046 3051
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 3046-3051
    • Weimbs, T.1    Low, S.H.2    Chapin, S.J.3    Mostov, K.E.4    Bucher, P.5    Hofmann, K.6
  • 26
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • D. Fasshauer, R.B. Sutton, A.T. Brunger, and R. Jahn Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs Proc. Natl. Acad. Sci. 95 1998 15781 15786
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 27
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • R. Jahn, and T.C. Sudhof Membrane fusion and exocytosis Annu. Rev. Biochem. 68 1999 863 911
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 28
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • J.B. Bock, H.T. Matern, A.A. Peden, and R.H. Scheller A genomic perspective on membrane compartment organization Nature 409 2001 839 841
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 29
    • 1842636943 scopus 로고    scopus 로고
    • Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation
    • M. Fukasawa, O. Varlamov, W.S. Eng, T.H. Sollner, and J.E. Rothman Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation Proc. Natl. Acad. Sci. 101 2004 4815 4820
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 4815-4820
    • Fukasawa, M.1    Varlamov, O.2    Eng, W.S.3    Sollner, T.H.4    Rothman, J.E.5
  • 30
    • 18244432240 scopus 로고    scopus 로고
    • Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25
    • M. Veit, T.H. Sollner, and J.E. Rothman Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25 FEBS Lett. 385 1996 119 123
    • (1996) FEBS Lett. , vol.385 , pp. 119-123
    • Veit, M.1    Sollner, T.H.2    Rothman, J.E.3
  • 31
    • 0033659365 scopus 로고    scopus 로고
    • Syntaxin 11 is an atypical SNARE abundant in the immune system
    • R. Prekeris, J. Klumperman, and R.H. Scheller Syntaxin 11 is an atypical SNARE abundant in the immune system Eur. J. Cell Biol. 79 2000 771 780
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 771-780
    • Prekeris, R.1    Klumperman, J.2    Scheller, R.H.3
  • 32
    • 0034723194 scopus 로고    scopus 로고
    • Targeting of SNAP-25 to membranes is mediated by its association with the target SNARE syntaxin
    • K. Vogel, J.P. Cabaniols, and P.A. Roche Targeting of SNAP-25 to membranes is mediated by its association with the target SNARE syntaxin J. Biol. Chem. 275 2000 2959 2965
    • (2000) J. Biol. Chem. , vol.275 , pp. 2959-2965
    • Vogel, K.1    Cabaniols, J.P.2    Roche, P.A.3
  • 33
    • 0041659220 scopus 로고    scopus 로고
    • Structural insights into the SNARE mechanism
    • D. Fasshauer Structural insights into the SNARE mechanism Biochim. Biophys. Acta 1641 2003 87 97
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 87-97
    • Fasshauer, D.1
  • 37
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • K.M. Misura, R.H. Scheller, and W.I. Weis Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex Nature 404 2000 355 362
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.1    Scheller, R.H.2    Weis, W.I.3
  • 38
    • 0037184043 scopus 로고    scopus 로고
    • The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly
    • W. Antonin, I. Dulubova, D. Arac, S. Pabst, J. Plitzner, J. Rizo, and R. Jahn The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly J. Biol. Chem. 277 2002 36449 36456
    • (2002) J. Biol. Chem. , vol.277 , pp. 36449-36456
    • Antonin, W.1    Dulubova, I.2    Arac, D.3    Pabst, S.4    Plitzner, J.5    Rizo, J.6    Jahn, R.7
  • 40
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • T. Yamaguchi, I. Dulubova, S.W. Min, X. Chen, J. Rizo, and T.C. Sudhof Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif Dev. Cell 2 2002 295 305
    • (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
  • 41
    • 0037112932 scopus 로고    scopus 로고
    • Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p
    • A. Bracher, and W. Weissenhorn Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p EMBO J. 21 2002 6114 6124
    • (2002) EMBO J. , vol.21 , pp. 6114-6124
    • Bracher, A.1    Weissenhorn, W.2
  • 43
  • 46
    • 0035958644 scopus 로고    scopus 로고
    • An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p
    • H. Tochio, M.M. Tsui, D.K. Banfield, and M. Zhang An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p Science 293 2001 698 702
    • (2001) Science , vol.293 , pp. 698-702
    • Tochio, H.1    Tsui, M.M.2    Banfield, D.K.3    Zhang, M.4
  • 47
    • 0035968198 scopus 로고    scopus 로고
    • A novel snare N-terminal domain revealed by the crystal structure of Sec22b
    • L.C. Gonzalez Jr., W.I. Weis, and R.H. Scheller A novel snare N-terminal domain revealed by the crystal structure of Sec22b J. Biol. Chem. 276 2001 24203 24211
    • (2001) J. Biol. Chem. , vol.276 , pp. 24203-24211
    • Gonzalez Jr., L.C.1    Weis, W.I.2    Scheller, R.H.3
  • 48
    • 0037147148 scopus 로고    scopus 로고
    • Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda
    • S.B. Jang, Y.G. Kim, Y.S. Cho, P.G. Suh, K.H. Kim, and B.H. Oh Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda J. Biol. Chem. 277 2002 49863 49869
    • (2002) J. Biol. Chem. , vol.277 , pp. 49863-49869
    • Jang, S.B.1    Kim, Y.G.2    Cho, Y.S.3    Suh, P.G.4    Kim, K.H.5    Oh, B.H.6
  • 49
    • 0842285407 scopus 로고    scopus 로고
    • The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion
    • L.E. Dietrich, R. Gurezka, M. Veit, and C. Ungermann The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion EMBO J. 23 2004 45 53
    • (2004) EMBO J. , vol.23 , pp. 45-53
    • Dietrich, L.E.1    Gurezka, R.2    Veit, M.3    Ungermann, C.4
  • 50
    • 10644285634 scopus 로고    scopus 로고
    • The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal cysteine residues
    • M. Veit The human SNARE protein Ykt6 mediates its own palmitoylation at C-terminal cysteine residues Biochem. J. 384 2004 233 237
    • (2004) Biochem. J. , vol.384 , pp. 233-237
    • Veit, M.1
  • 51
    • 0035966098 scopus 로고    scopus 로고
    • The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding
    • A.A. Peden, G.Y. Park, and R.H. Scheller The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding J. Biol. Chem. 276 2001 49183 49187
    • (2001) J. Biol. Chem. , vol.276 , pp. 49183-49187
    • Peden, A.A.1    Park, G.Y.2    Scheller, R.H.3
  • 52
    • 0038264998 scopus 로고    scopus 로고
    • The cytoplasmic domain of Vamp4 and Vamp5 is responsible for their correct subcellular targeting: The N-terminal extenSion of VAMP4 contains a dominant autonomous targeting signal for the trans-Golgi network
    • Q. Zeng, T.T. Tran, H.X. Tan, and W. Hong The cytoplasmic domain of Vamp4 and Vamp5 is responsible for their correct subcellular targeting: the N-terminal extenSion of VAMP4 contains a dominant autonomous targeting signal for the trans-Golgi network J. Biol. Chem. 278 2003 23046 23054
    • (2003) J. Biol. Chem. , vol.278 , pp. 23046-23054
    • Zeng, Q.1    Tran, T.T.2    Tan, H.X.3    Hong, W.4
  • 53
    • 0347093454 scopus 로고    scopus 로고
    • AP-1 recruitment to VAMP4 is modulated by phosphorylation-dependent binding of PACS-1
    • I. Hinners, F. Wendler, H. Fei, L. Thomas, G. Thomas, and S.A. Tooze AP-1 recruitment to VAMP4 is modulated by phosphorylation-dependent binding of PACS-1 EMBO Rep. 4 2003 1182 1189
    • (2003) EMBO Rep. , vol.4 , pp. 1182-1189
    • Hinners, I.1    Wendler, F.2    Fei, H.3    Thomas, L.4    Thomas, G.5    Tooze, S.A.6
  • 57
    • 0035920124 scopus 로고    scopus 로고
    • Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport
    • T. Zhang, and W. Hong Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport J. Biol. Chem. 276 2001 27480 27487
    • (2001) J. Biol. Chem. , vol.276 , pp. 27480-27487
    • Zhang, T.1    Hong, W.2
  • 58
    • 0036800355 scopus 로고    scopus 로고
    • GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus
    • Y. Xu, S. Martin, D.E. James, and W. Hong GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is implicated in traffic in the early cisternae of the Golgi apparatus Mol. Biol. Cell 13 2002 3493 3507
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3493-3507
    • Xu, Y.1    Martin, S.2    James, D.E.3    Hong, W.4
  • 60
    • 0033593207 scopus 로고    scopus 로고
    • Proteins of the exocytotic core complex mediate platelet alpha-granule secretion. Roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4
    • R. Flaumenhaft, K. Croce, E. Chen, B. Furie, and B.C. Furie Proteins of the exocytotic core complex mediate platelet alpha-granule secretion. Roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4 J. Biol. Chem. 274 1999 2492 2501
    • (1999) J. Biol. Chem. , vol.274 , pp. 2492-2501
    • Flaumenhaft, R.1    Croce, K.2    Chen, E.3    Furie, B.4    Furie, B.C.5
  • 61
    • 2442584514 scopus 로고    scopus 로고
    • Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis
    • S.K. Rao, C. Huynh, V. Proux-Gillardeaux, T. Galli, and N.W. Andrews Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis J. Biol. Chem. 279 2004 20471 20479
    • (2004) J. Biol. Chem. , vol.279 , pp. 20471-20479
    • Rao, S.K.1    Huynh, C.2    Proux-Gillardeaux, V.3    Galli, T.4    Andrews, N.W.5
  • 62
    • 4544227227 scopus 로고    scopus 로고
    • A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells
    • C.C. Wang, C.P. Ng, L. Lu, V. Atlashkin, W. Zhang, L.F. Seet, and W. Hong A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells Dev. Cell 7 2004 359 371
    • (2004) Dev. Cell , vol.7 , pp. 359-371
    • Wang, C.C.1    Ng, C.P.2    Lu, L.3    Atlashkin, V.4    Zhang, W.5    Seet, L.F.6    Hong, W.7
  • 63
    • 0034407116 scopus 로고    scopus 로고
    • A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function
    • W. Antonin, C. Holroyd, D. Fasshauer, S. Pabst, G.F. Von Mollard, and R. Jahn A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function EMBO J. 19 2000 6453 6464
    • (2000) EMBO J. , vol.19 , pp. 6453-6464
    • Antonin, W.1    Holroyd, C.2    Fasshauer, D.3    Pabst, S.4    Von Mollard, G.F.5    Jahn, R.6
  • 66
    • 1842335138 scopus 로고    scopus 로고
    • The mammalian protein (rbet1) homologous to yeast Bet1p is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus
    • T. Zhang, S.H. Wong, B.L. Tang, Y. Xu, F. Peter, V.N. Subramaniam, and W. Hong The mammalian protein (rbet1) homologous to yeast Bet1p is primarily associated with the pre-Golgi intermediate compartment and is involved in vesicular transport from the endoplasmic reticulum to the Golgi apparatus J. Cell Biol. 139 1997 1157 1168
    • (1997) J. Cell Biol. , vol.139 , pp. 1157-1168
    • Zhang, T.1    Wong, S.H.2    Tang, B.L.3    Xu, Y.4    Peter, F.5    Subramaniam, V.N.6    Hong, W.7
  • 67
    • 0344178042 scopus 로고    scopus 로고
    • Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment
    • T. Zhang, S.H. Wong, B.L. Tang, Y. Xu, and W. Hong Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment Mol. Biol. Cell 10 1999 435 453
    • (1999) Mol. Biol. Cell , vol.10 , pp. 435-453
    • Zhang, T.1    Wong, S.H.2    Tang, B.L.3    Xu, Y.4    Hong, W.5
  • 68
    • 0037113095 scopus 로고    scopus 로고
    • Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC)
    • H. Horstmann, C.P. Ng, B.L. Tang, and W. Hong Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC) J. Cell Sci. 115 2002 4263 4273
    • (2002) J. Cell Sci. , vol.115 , pp. 4263-4273
    • Horstmann, H.1    Ng, C.P.2    Tang, B.L.3    Hong, W.4
  • 70
    • 0027294075 scopus 로고
    • The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p
    • D.J. Sweet, and H.R. Pelham The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p EMBO J. 12 1993 2831 2840
    • (1993) EMBO J. , vol.12 , pp. 2831-2840
    • Sweet, D.J.1    Pelham, H.R.2
  • 71
    • 4344599512 scopus 로고    scopus 로고
    • Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network
    • G. Tai, L. Lu, T.L. Wang, B.L. Tang, B. Goud, L. Johannes, and W. Hong Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network Mol. Biol. Cell 15 2004 4011 4022
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4011-4022
    • Tai, G.1    Lu, L.2    Wang, T.L.3    Tang, B.L.4    Goud, B.5    Johannes, L.6    Hong, W.7
  • 72
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • H.M. McBride, V. Rybin, C. Murphy, A. Giner, R. Teasdale, and M. Zerial Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13 Cell 98 1999 377 3786
    • (1999) Cell , vol.98 , pp. 377-3786
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 73
    • 0038825173 scopus 로고    scopus 로고
    • Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
    • W. Sun, Q. Yan, T.A. Vida, and A.J. Bean Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex J. Cell Biol. 162 2003 125 137
    • (2003) J. Cell Biol. , vol.162 , pp. 125-137
    • Sun, W.1    Yan, Q.2    Vida, T.A.3    Bean, A.J.4
  • 74
    • 0029847075 scopus 로고    scopus 로고
    • Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells
    • S.H. Low, S.J. Chapin, T. Weimbs, L.G. Komuves, M.K. Bennett, and K.E. Mostov Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells Mol. Biol. Cell 7 1996 2007 2018
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2007-2018
    • Low, S.H.1    Chapin, S.J.2    Weimbs, T.3    Komuves, L.G.4    Bennett, M.K.5    Mostov, K.E.6
  • 75
    • 0032007835 scopus 로고    scopus 로고
    • Endogenous syntaxins 2, 3 and 4 exhibit distinct but overlapping patterns of expression at the hepatocyte plasma membrane
    • H. Fujita, P.L. Tuma, C.M. Finnegan, L. Locco, and A.L. Hubbard Endogenous syntaxins 2, 3 and 4 exhibit distinct but overlapping patterns of expression at the hepatocyte plasma membrane Biochem. J. 329 1998 527 538
    • (1998) Biochem. J. , vol.329 , pp. 527-538
    • Fujita, H.1    Tuma, P.L.2    Finnegan, C.M.3    Locco, L.4    Hubbard, A.L.5
  • 76
    • 0033616708 scopus 로고    scopus 로고
    • Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells
    • F. Lafont, P. Verkade, T. Galli, C. Wimmer, D. Louvard, and K. Simons Raft association of SNAP receptors acting in apical trafficking in Madin-Darby canine kidney cells Proc. Natl. Acad. Sci. 96 1999 3734 3738
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 3734-3738
    • Lafont, F.1    Verkade, P.2    Galli, T.3    Wimmer, C.4    Louvard, D.5    Simons, K.6
  • 77
    • 4644321100 scopus 로고    scopus 로고
    • Inhibition of SNAP-25 phosphorylation at Ser187 is involved in chronic morphine-induced down-regulation of SNARE complex formation
    • N.J. Xu, Y.X. Yu, J.M. Zhu, H. Liu, L. Shen, R. Zeng, X. Zhang, and G. Pei Inhibition of SNAP-25 phosphorylation at Ser187 is involved in chronic morphine-induced down-regulation of SNARE complex formation J. Biol. Chem. 279 2004 40601 40608
    • (2004) J. Biol. Chem. , vol.279 , pp. 40601-40608
    • Xu, N.J.1    Yu, Y.X.2    Zhu, J.M.3    Liu, H.4    Shen, L.5    Zeng, R.6    Zhang, X.7    Pei, G.8
  • 78
    • 1242306711 scopus 로고    scopus 로고
    • Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25
    • G. Nagy, K. Reim, U. Matti, N. Brose, T. Binz, J. Rettig, E. Neher, and J.B. Sorensen Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25 Neuron 41 2004 417 429
    • (2004) Neuron , vol.41 , pp. 417-429
    • Nagy, G.1    Reim, K.2    Matti, U.3    Brose, N.4    Binz, T.5    Rettig, J.6    Neher, E.7    Sorensen, J.B.8
  • 80
    • 5444272879 scopus 로고    scopus 로고
    • Intramolecular protein-protein and protein-lipid interactions control the conformation and subcellular targeting of neuronal Ykt6
    • H. Hasegawa, Z. Yang, L. Oltedal, S. Davanger, and J.C. Hay Intramolecular protein-protein and protein-lipid interactions control the conformation and subcellular targeting of neuronal Ykt6 J. Cell Sci. 117 2004 4495 4508
    • (2004) J. Cell Sci. , vol.117 , pp. 4495-4508
    • Hasegawa, H.1    Yang, Z.2    Oltedal, L.3    Davanger, S.4    Hay, J.C.5
  • 81
    • 0037697285 scopus 로고    scopus 로고
    • Defining the SNARE complex binding surface of alpha-SNAP: Implications for SNARE complex disassembly
    • K.E. Marz, J.M. Lauer, and P.I. Hanson Defining the SNARE complex binding surface of alpha-SNAP: implications for SNARE complex disassembly J. Biol. Chem. 278 2003 27000 27008
    • (2003) J. Biol. Chem. , vol.278 , pp. 27000-27008
    • Marz, K.E.1    Lauer, J.M.2    Hanson, P.I.3
  • 82
    • 1442360430 scopus 로고    scopus 로고
    • The hyh mutation uncovers roles for alpha Snap in apical protein localization and control of neural cell fate
    • T.H. Chae, S. Kim, K.E. Marz, P.I. Hanson, and C.A. Walsh The hyh mutation uncovers roles for alpha Snap in apical protein localization and control of neural cell fate Nat. Genet. 36 2004 264 270
    • (2004) Nat. Genet. , vol.36 , pp. 264-270
    • Chae, T.H.1    Kim, S.2    Marz, K.E.3    Hanson, P.I.4    Walsh, C.A.5
  • 87
    • 0031710883 scopus 로고    scopus 로고
    • Alpha-SNAP but not gamma-SNAP is required for ER-Golgi transport after vesicle budding and the Rab1-requiring step but before the EGTA-sensitive step
    • F. Peter, S.H. Wong, V.N. Subramaniam, B.L. Tang, and W. Hong Alpha-SNAP but not gamma-SNAP is required for ER-Golgi transport after vesicle budding and the Rab1-requiring step but before the EGTA-sensitive step J. Cell Sci. 111 1998 2625 2633
    • (1998) J. Cell Sci. , vol.111 , pp. 2625-2633
    • Peter, F.1    Wong, S.H.2    Subramaniam, V.N.3    Tang, B.L.4    Hong, W.5
  • 88
    • 0036673069 scopus 로고    scopus 로고
    • Snares and Munc18 in synaptic vesicle fusion
    • J. Rizo, and T.C. Sudhof Snares and Munc18 in synaptic vesicle fusion Nat. Rev., Neurosci. 3 2002 641 653
    • (2002) Nat. Rev., Neurosci. , vol.3 , pp. 641-653
    • Rizo, J.1    Sudhof, T.C.2
  • 89
    • 0037334373 scopus 로고    scopus 로고
    • The riddle of the Sec1/Munc-18 proteins-New twists added to their interactions with SNAREs
    • D. Gallwitz, and R. Jahn The riddle of the Sec1/Munc-18 proteins-New twists added to their interactions with SNAREs Trends Biochem. Sci. 28 2003 113 116
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 113-116
    • Gallwitz, D.1    Jahn, R.2
  • 90
    • 0028998826 scopus 로고
    • A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic
    • Y. Hata, and T.C. Sudhof A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic J. Biol. Chem. 270 1995 13022 13028
    • (1995) J. Biol. Chem. , vol.270 , pp. 13022-13028
    • Hata, Y.1    Sudhof, T.C.2
  • 91
    • 0347091328 scopus 로고    scopus 로고
    • Analysis of the Munc18b-syntaxin binding interface. Use of a mutant Munc18b to dissect the functions of syntaxins 2 and 3
    • M. Kauppi, G. Wohlfahrt, and V.M. Olkkonen Analysis of the Munc18b-syntaxin binding interface. Use of a mutant Munc18b to dissect the functions of syntaxins 2 and 3 J. Biol. Chem. 277 2002 43973 43979
    • (2002) J. Biol. Chem. , vol.277 , pp. 43973-43979
    • Kauppi, M.1    Wohlfahrt, G.2    Olkkonen, V.M.3
  • 92
    • 10344236432 scopus 로고    scopus 로고
    • Regulated membrane trafficking of the insulin-responsive glucose transporter 4 in adipocytes
    • R.T. Watson, M. Kanzaki, and J.E. Pessin Regulated membrane trafficking of the insulin-responsive glucose transporter 4 in adipocytes Endocr. Rev. 25 2004 177 204
    • (2004) Endocr. Rev. , vol.25 , pp. 177-204
    • Watson, R.T.1    Kanzaki, M.2    Pessin, J.E.3
  • 95
    • 0028791349 scopus 로고
    • Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins
    • N. Brose, K. Hofmann, Y. Hata, and T.C. Sudhof Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins J. Biol. Chem. 270 1995 25273 25280
    • (1995) J. Biol. Chem. , vol.270 , pp. 25273-25280
    • Brose, N.1    Hofmann, K.2    Hata, Y.3    Sudhof, T.C.4
  • 96
    • 0034235922 scopus 로고    scopus 로고
    • Definition of Munc13-homology-domains and characterization of a novel ubiquitously expressed Munc13 isoform
    • H. Koch, K. Hofmann, and N. Brose Definition of Munc13-homology-domains and characterization of a novel ubiquitously expressed Munc13 isoform Biochem. J. 349 2000 247 253
    • (2000) Biochem. J. , vol.349 , pp. 247-253
    • Koch, H.1    Hofmann, K.2    Brose, N.3
  • 98
    • 0037172972 scopus 로고    scopus 로고
    • Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming
    • F. Varoqueaux, A. Sigler, J.S. Rhee, N. Brose, C. Enk, K. Reim, and C. Rosenmund Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming Proc. Natl. Acad. Sci. 99 2002 9037 9042
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 9037-9042
    • Varoqueaux, F.1    Sigler, A.2    Rhee, J.S.3    Brose, N.4    Enk, C.5    Reim, K.6    Rosenmund, C.7
  • 99
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin
    • A. Betz, M. Okamoto, F. Benseler, and N. Brose Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin J. Biol. Chem. 272 1997 2520 2526
    • (1997) J. Biol. Chem. , vol.272 , pp. 2520-2526
    • Betz, A.1    Okamoto, M.2    Benseler, F.3    Brose, N.4
  • 100
    • 0030877243 scopus 로고    scopus 로고
    • Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
    • Y. Wang, M. Okamoto, F. Schmitz, K. Hofmann, and T.C. Sudhof Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion Nature 388 1997 593 598
    • (1997) Nature , vol.388 , pp. 593-598
    • Wang, Y.1    Okamoto, M.2    Schmitz, F.3    Hofmann, K.4    Sudhof, T.C.5
  • 103
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • H.T. McMahon, M. Missler, C. Li, and T.C. Sudhof Complexins: cytosolic proteins that regulate SNAP receptor function Cell 83 1995 111 119
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Sudhof, T.C.4
  • 104
    • 0036680512 scopus 로고    scopus 로고
    • Sealed with a twist: Complexin and the synaptic SNARE complex
    • K.E. Marz, and P.I. Hanson Sealed with a twist: complexin and the synaptic SNARE complex Trends Neurosci. 25 2002 381 383
    • (2002) Trends Neurosci. , vol.25 , pp. 381-383
    • Marz, K.E.1    Hanson, P.I.2
  • 109
    • 0037040890 scopus 로고    scopus 로고
    • Synaptotagmins: Why so many?
    • T.C. Sudhof Synaptotagmins: why so many? J. Biol. Chem. 277 2002 7629 7632
    • (2002) J. Biol. Chem. , vol.277 , pp. 7629-7632
    • Sudhof, T.C.1
  • 110
    • 0028061861 scopus 로고
    • Synaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse
    • M. Geppert, Y. Goda, R.E. Hammer, C. Li, T.W. Rosahl, C.F. Stevens, and T.C. Sudhof Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse Cell 79 1994 717 727
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1    Goda, Y.2    Hammer, R.E.3    Li, C.4    Rosahl, T.W.5    Stevens, C.F.6    Sudhof, T.C.7
  • 112
    • 1542286172 scopus 로고    scopus 로고
    • The C2 domains of synaptotagmin-Partners in exocytosis
    • J. Bai, and E.R. Chapman The C2 domains of synaptotagmin-Partners in exocytosis Trends Biochem. Sci. 29 2004 143 151
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 143-151
    • Bai, J.1    Chapman, E.R.2
  • 113
    • 0842291506 scopus 로고    scopus 로고
    • PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • J. Bai, W.C. Tucker, and E.R. Chapman PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane Nat. Struct. Mol. Biol. 11 2004 36 44
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 114
    • 0037117938 scopus 로고    scopus 로고
    • Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis
    • X. Zhang, M.J. Kim-Miller, M. Fukuda, J.A. Kowalchyk, and T.F. Martin Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis Neuron 34 2002 599 611
    • (2002) Neuron , vol.34 , pp. 599-611
    • Zhang, X.1    Kim-Miller, M.J.2    Fukuda, M.3    Kowalchyk, J.A.4    Martin, T.F.5
  • 115
    • 1942520207 scopus 로고    scopus 로고
    • Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs
    • W.C. Tucker, T. Weber, and E.R. Chapman Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs Science 304 2004 435 438
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 116
    • 0042733066 scopus 로고    scopus 로고
    • The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis
    • K. Hatsuzawa, T. Lang, D. Fasshauer, D. Bruns, and R. Jahn The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis J. Biol. Chem. 278 2003 31159 31166
    • (2003) J. Biol. Chem. , vol.278 , pp. 31159-31166
    • Hatsuzawa, K.1    Lang, T.2    Fasshauer, D.3    Bruns, D.4    Jahn, R.5
  • 118
    • 0037008753 scopus 로고    scopus 로고
    • Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly
    • S.J. Scales, B.A. Hesser, E.S. Masuda, and R.H. Scheller Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly J. Biol. Chem. 277 2002 28271 28279
    • (2002) J. Biol. Chem. , vol.277 , pp. 28271-28279
    • Scales, S.J.1    Hesser, B.A.2    Masuda, E.S.3    Scheller, R.H.4
  • 119
    • 1842714295 scopus 로고    scopus 로고
    • Synaptophysin: Leading actor or walk-on role in synaptic vesicle exocytosis?
    • F. Valtorta, M. Pennuto, D. Bonanomi, and F. Benfenati Synaptophysin: leading actor or walk-on role in synaptic vesicle exocytosis? BioEssays 26 2004 445 453
    • (2004) BioEssays , vol.26 , pp. 445-453
    • Valtorta, F.1    Pennuto, M.2    Bonanomi, D.3    Benfenati, F.4
  • 120
    • 9744270641 scopus 로고    scopus 로고
    • Stimulus-dependent dynamic homo- and heteromultimerization of synaptobrevin/VAMP and synaptophysin
    • M.V. Khvotchev, and T.C. Sudhof Stimulus-dependent dynamic homo- and heteromultimerization of synaptobrevin/VAMP and synaptophysin Biochemistry 43 2004 15037 15043
    • (2004) Biochemistry , vol.43 , pp. 15037-15043
    • Khvotchev, M.V.1    Sudhof, T.C.2
  • 121
    • 0344875499 scopus 로고    scopus 로고
    • Synaptophysin I controls the targeting of VAMP2/synaptobrevin II to synaptic vesicles
    • M. Pennuto, D. Bonanomi, F. Benfenati, and F. Valtorta Synaptophysin I controls the targeting of VAMP2/synaptobrevin II to synaptic vesicles Mol. Biol. Cell 14 2003 4909 4919
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4909-4919
    • Pennuto, M.1    Bonanomi, D.2    Benfenati, F.3    Valtorta, F.4
  • 123
  • 125
    • 0842277809 scopus 로고    scopus 로고
    • Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis
    • M.A. Puthenveedu, and A.D. Linstedt Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis Proc. Natl. Acad. Sci. 101 2004 1253 1256
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 1253-1256
    • Puthenveedu, M.A.1    Linstedt, A.D.2
  • 127
    • 0242643727 scopus 로고    scopus 로고
    • Hrs function: Viruses provide the clue
    • M.J. Clague, and S. Urbe Hrs function: viruses provide the clue Trends Cell Biol. 13 2003 603 606
    • (2003) Trends Cell Biol. , vol.13 , pp. 603-606
    • Clague, M.J.1    Urbe, S.2
  • 129
    • 0032879685 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 interacts directly with syntaxin-6
    • A. Simonsen, J.M. Gaullier, A. D'Arrigo, and H. Stenmark The Rab5 effector EEA1 interacts directly with syntaxin-6 J. Biol. Chem. 274 1999 28857 28860
    • (1999) J. Biol. Chem. , vol.274 , pp. 28857-28860
    • Simonsen, A.1    Gaullier, J.M.2    D'Arrigo, A.3    Stenmark, H.4
  • 130
    • 0035800743 scopus 로고    scopus 로고
    • Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6
    • A. Charest, K. Lane, K. McMahon, and D.E. Housman Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6 J. Biol. Chem. 276 2001 29456 29465
    • (2001) J. Biol. Chem. , vol.276 , pp. 29456-29465
    • Charest, A.1    Lane, K.2    McMahon, K.3    Housman, D.E.4
  • 132
    • 0001417555 scopus 로고    scopus 로고
    • GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28
    • Y. Sagiv, A. Legesse-Miller, A. Porat, and Z. Elazar GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28 EMBO J. 19 2000 1494 1504
    • (2000) EMBO J. , vol.19 , pp. 1494-1504
    • Sagiv, Y.1    Legesse-Miller, A.2    Porat, A.3    Elazar, Z.4
  • 133
    • 0037166941 scopus 로고    scopus 로고
    • Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion
    • J.M. Muller, J. Shorter, R. Newman, K. Deinhardt, Y. Sagiv, Z. Elazar, G. Warren, and D.T. Shima Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion J. Cell Biol. 157 2002 1161 1173
    • (2002) J. Cell Biol. , vol.157 , pp. 1161-1173
    • Muller, J.M.1    Shorter, J.2    Newman, R.3    Deinhardt, K.4    Sagiv, Y.5    Elazar, Z.6    Warren, G.7    Shima, D.T.8
  • 134
    • 0347695019 scopus 로고    scopus 로고
    • A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L
    • J. Hemelaar, V.S. Lelyveld, B.M. Kessler, and H.L. Ploegh A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L J. Biol. Chem. 278 2003 51841 61850
    • (2003) J. Biol. Chem. , vol.278 , pp. 51841-61850
    • Hemelaar, J.1    Lelyveld, V.S.2    Kessler, B.M.3    Ploegh, H.L.4
  • 137
    • 12544259110 scopus 로고    scopus 로고
    • A direct interaction between Cdc42 and VAMP2 regulates SNARE-dependent insulin exocytosis
    • A.K. Nevins, and D.C. Thurmond A direct interaction between Cdc42 and VAMP2 regulates SNARE-dependent insulin exocytosis J. Biol. Chem. 280 3 2005 1944 1952
    • (2005) J. Biol. Chem. , vol.280 , Issue.3 , pp. 1944-1952
    • Nevins, A.K.1    Thurmond, D.C.2
  • 138
    • 0035134281 scopus 로고    scopus 로고
    • VAMP3 null mice display normal constitutive, insulin- and exercise-regulated vesicle trafficking
    • C. Yang, S. Mora, J.W. Ryder, K.J. Coker, P. Hansen, L.A. Allen, and J.E. Pessin VAMP3 null mice display normal constitutive, insulin- and exercise-regulated vesicle trafficking Mol. Cell. Biol. 2001 1573 1580
    • (2001) Mol. Cell. Biol. , pp. 1573-1580
    • Yang, C.1    Mora, S.2    Ryder, J.W.3    Coker, K.J.4    Hansen, P.5    Allen, L.A.6    Pessin, J.E.7
  • 139
    • 0000926518 scopus 로고    scopus 로고
    • Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome
    • S.H. Wong, T. Zhang, Y. Xu, V.N. Subramaniam, G. Griffiths, and W. Hong Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome Mol. Biol. Cell 9 1998 1549 1563
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1549-1563
    • Wong, S.H.1    Zhang, T.2    Xu, Y.3    Subramaniam, V.N.4    Griffiths, G.5    Hong, W.6
  • 140
  • 141
    • 0033787382 scopus 로고    scopus 로고
    • The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes
    • W. Antonin, C. Holroyd, R. Tikkanen, S. Honing, and R. Jahn The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes Mol. Biol. Cell 11 2000 3289 3298
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3289-3298
    • Antonin, W.1    Holroyd, C.2    Tikkanen, R.3    Honing, S.4    Jahn, R.5
  • 143
    • 0347786911 scopus 로고    scopus 로고
    • The t-SNARE syntaxin 4 is regulated during macrophage activation to function in membrane traffic and cytokine secretion
    • J.K. Pagan, F.G. Wylie, S. Joseph, C. Widberg, N.J. Bryant, D.E. James, and J.L. Stow The t-SNARE syntaxin 4 is regulated during macrophage activation to function in membrane traffic and cytokine secretion Curr. Biol. 13 2003 156 160
    • (2003) Curr. Biol. , vol.13 , pp. 156-160
    • Pagan, J.K.1    Wylie, F.G.2    Joseph, S.3    Widberg, C.4    Bryant, N.J.5    James, D.E.6    Stow, J.L.7
  • 147
    • 0030863058 scopus 로고    scopus 로고
    • An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal
    • N. Hui, N. Nakamura, B. Sonnichsen, D.T. Shima, T. Nilsson, and G. Warren An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal Mol. Biol. Cell 8 1997 1777 1787
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1777-1787
    • Hui, N.1    Nakamura, N.2    Sonnichsen, B.3    Shima, D.T.4    Nilsson, T.5    Warren, G.6
  • 148
    • 0032544441 scopus 로고    scopus 로고
    • Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A
    • I. Fernandez, J. Ubach, I. Dulubova, X. Zhang, T.C. Sudhof, and J. Rizo Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A Cell 94 1998 841 849
    • (1998) Cell , vol.94 , pp. 841-849
    • Fernandez, I.1    Ubach, J.2    Dulubova, I.3    Zhang, X.4    Sudhof, T.C.5    Rizo, J.6
  • 149
    • 0032743997 scopus 로고    scopus 로고
    • The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency
    • L. Huang, Y.M. Kuo, and J. Gitschier The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency Nat. Genet. 23 1999 329 332
    • (1999) Nat. Genet. , vol.23 , pp. 329-332
    • Huang, L.1    Kuo, Y.M.2    Gitschier, J.3
  • 150
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • J.M. Ilardi, S. Mochida, and Z.H. Sheng Snapin: a SNARE-associated protein implicated in synaptic transmission Nat. Neurosci. 2 1999 119 124
    • (1999) Nat. Neurosci. , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 151
    • 0141814988 scopus 로고    scopus 로고
    • Syntaxin 4 and Synip (syntaxin 4 interacting protein) regulate insulin secretion in the pancreatic beta HC-9 cell
    • T. Saito, S. Okada, E. Yamada, K. Ohshima, H. Shimizu, K. Shimomura, M. Sato, J.E. Pessin, and M. Mori Syntaxin 4 and Synip (syntaxin 4 interacting protein) regulate insulin secretion in the pancreatic beta HC-9 cell J. Biol. Chem. 278 2003 36718 36725
    • (2003) J. Biol. Chem. , vol.278 , pp. 36718-36725
    • Saito, T.1    Okada, S.2    Yamada, E.3    Ohshima, K.4    Shimizu, H.5    Shimomura, K.6    Sato, M.7    Pessin, J.E.8    Mori, M.9
  • 153
    • 0033363646 scopus 로고    scopus 로고
    • The septin CDCrel-1 binds syntaxin and inhibits exocytosis
    • C.L. Beites, H. Xie, R. Bowser, and W.S. Trimble The septin CDCrel-1 binds syntaxin and inhibits exocytosis Nat. Neurosci. 2 1999 434 439
    • (1999) Nat. Neurosci. , vol.2 , pp. 434-439
    • Beites, C.L.1    Xie, H.2    Bowser, R.3    Trimble, W.S.4
  • 154
    • 2542463861 scopus 로고    scopus 로고
    • Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a
    • S. Torii, T. Takeuchi, S. Nagamatsu, and T. Izumi Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a J. Biol. Chem. 279 2004 22532 22538
    • (2004) J. Biol. Chem. , vol.279 , pp. 22532-22538
    • Torii, S.1    Takeuchi, T.2    Nagamatsu, S.3    Izumi, T.4
  • 155
    • 2442492169 scopus 로고    scopus 로고
    • Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes
    • Q. Yan, W. Sun, J.A. McNew, T.A. Vida, and A.J. Bean Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes J. Biol. Chem. 279 2004 18270 18276
    • (2004) J. Biol. Chem. , vol.279 , pp. 18270-18276
    • Yan, Q.1    Sun, W.2    McNew, J.A.3    Vida, T.A.4    Bean, A.J.5
  • 157
    • 5444235717 scopus 로고    scopus 로고
    • Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons
    • Q. Su, Q. Cai, C. Gerwin, C.L. Smith, and Z.H. Sheng Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons Nat. Cell Biol. 6 2004 941 953
    • (2004) Nat. Cell Biol. , vol.6 , pp. 941-953
    • Su, Q.1    Cai, Q.2    Gerwin, C.3    Smith, C.L.4    Sheng, Z.H.5
  • 158
    • 0036312094 scopus 로고    scopus 로고
    • Identification of a novel SNAP25 interacting protein (SIP30)
    • H.K. Lee, S. Safieddine, R.S. Petralia, and R.J. Wenthold Identification of a novel SNAP25 interacting protein (SIP30) J. Neurochem. 81 2002 1338 1347
    • (2002) J. Neurochem. , vol.81 , pp. 1338-1347
    • Lee, H.K.1    Safieddine, S.2    Petralia, R.S.3    Wenthold, R.J.4
  • 159
  • 160
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • I. Augustin, C. Rosenmund, T.C. Südhof, and N. Brose Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles Nature 400 1999 457 461
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Südhof, T.C.3    Brose, N.4
  • 161
    • 0035141520 scopus 로고    scopus 로고
    • The cerebellum-specific Munc13 isoform Munc13-3 regulates cerebellar synaptic transmission and motor learning in mice
    • I. Augustin, S. Korte, M. Rickmann, H.A. Kretzschmar, T.C. Sudhof, J.W. Herms, and N. Brose The cerebellum-specific Munc13 isoform Munc13-3 regulates cerebellar synaptic transmission and motor learning in mice J. Neurosci. 21 2001 10 17
    • (2001) J. Neurosci. , vol.21 , pp. 10-17
    • Augustin, I.1    Korte, S.2    Rickmann, M.3    Kretzschmar, H.A.4    Sudhof, T.C.5    Herms, J.W.6    Brose, N.7
  • 163
    • 0141618325 scopus 로고    scopus 로고
    • Complexin II is essential for normal neurological function in mice
    • D. Glynn, R.A. Bortnick, and A.J. Morton Complexin II is essential for normal neurological function in mice Hum. Mol. Genet. 12 2003 2431 2448
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2431-2448
    • Glynn, D.1    Bortnick, R.A.2    Morton, A.J.3
  • 164
    • 0033151614 scopus 로고    scopus 로고
    • Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis
    • M. Komada, and P. Soriano Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis Genes Dev. 13 1999 1475 1485
    • (1999) Genes Dev. , vol.13 , pp. 1475-1485
    • Komada, M.1    Soriano, P.2
  • 165
    • 0036132908 scopus 로고    scopus 로고
    • The septin CDCrel-1 is dispensable for normal development and neurotransmitter release
    • X.R. Peng, Z. Jia, Y. Zhang, J. Ware, and W.S. Trimble The septin CDCrel-1 is dispensable for normal development and neurotransmitter release Mol. Cell. Biol. 22 2002 378 387
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 378-387
    • Peng, X.R.1    Jia, Z.2    Zhang, Y.3    Ware, J.4    Trimble, W.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.