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Volumn 56, Issue 4, 2012, Pages 245-253

Specificity of botulinum protease for human VAMP family proteins

Author keywords

Botulinum neurotoxin light chain; Proteolysis; Substrate specificity; VAMP proteins

Indexed keywords

BACTERIAL TOXIN; BOTULINUM NEUROTOXIN LIGHT CHAIN; BOTULINUM NEUROTOXIN LIGHT CHAIN B; BOTULINUM NEUROTOXIN LIGHT CHAIN F; BOTULINUM TOXIN; CELLUBREVIN; COMPLEMENTARY DNA; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOBREVIN 1; SYNAPTOBREVIN 2; UNCLASSIFIED DRUG;

EID: 84859844136     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2012.00434.x     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco C., Schiavo G. (1994) Mechanism of action of tetanus and botulinum neurotoxins. Mol Microbiol 13: 1-8.
    • (1994) Mol Microbiol , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 4
    • 0036840945 scopus 로고    scopus 로고
    • Review of the use of botulinum toxin for hyperhidrosis and cosmetic purposes
    • Glogau R.G. (2002) Review of the use of botulinum toxin for hyperhidrosis and cosmetic purposes. Clin J Pain 18: S191-7.
    • (2002) Clin J Pain , vol.18
    • Glogau, R.G.1
  • 5
    • 2442458014 scopus 로고    scopus 로고
    • Botulinum toxins in neurological disease
    • Comella C.L., Pullman S.L. (2004) Botulinum toxins in neurological disease. Muscle Nerve 29: 628-44.
    • (2004) Muscle Nerve , vol.29 , pp. 628-644
    • Comella, C.L.1    Pullman, S.L.2
  • 6
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock J.B., Matern H.T., Peden A.A., Scheller R.H. (2001) A genomic perspective on membrane compartment organization. Nature 409: 839-41.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 7
    • 23844556932 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong W. (2005) SNAREs and traffic. Biochim Biophys Acta 1744: 493-517.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 493-517
    • Hong, W.1
  • 8
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs-engines for membrane fusion
    • Jahn R., Scheller R.H. (2006) SNAREs-engines for membrane fusion. Nat Rev Mol Cell Biol 7: 631-43.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 9
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R., Sudhof T.C. (1999) Membrane fusion and exocytosis. Annu Rev Biochem 68: 863-911.
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 10
    • 0034523701 scopus 로고    scopus 로고
    • Mechanisms of synaptic vesicle exocytosis
    • Lin R.C., Scheller R.H. (2000) Mechanisms of synaptic vesicle exocytosis. Annu Rev Cell Dev Biol 16: 19-49.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 19-49
    • Lin, R.C.1    Scheller, R.H.2
  • 11
    • 0036624735 scopus 로고    scopus 로고
    • Subcellular distribution of 3 functional platelet SNARE proteins: human cellubrevin, SNAP-23, and syntaxin 2
    • Feng D., Crane K., Rozenvayn N., Dvorak A.M., Flaumenhaft R. (2002) Subcellular distribution of 3 functional platelet SNARE proteins: human cellubrevin, SNAP-23, and syntaxin 2. Blood 99: 4006-14.
    • (2002) Blood , vol.99 , pp. 4006-4014
    • Feng, D.1    Crane, K.2    Rozenvayn, N.3    Dvorak, A.M.4    Flaumenhaft, R.5
  • 12
    • 0036683001 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion
    • Polgar J., Chung S.H., Reed G.L. (2002) Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion. Blood 100: 1081-3.
    • (2002) Blood , vol.100 , pp. 1081-1083
    • Polgar, J.1    Chung, S.H.2    Reed, G.L.3
  • 13
    • 0028291894 scopus 로고
    • Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells
    • Galli T., Chilcote T., Mundigl O., Binz T., Niemann H., De Camilli P. (1994) Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells. J Cell Biol 125: 1015-24.
    • (1994) J Cell Biol , vol.125 , pp. 1015-1024
    • Galli, T.1    Chilcote, T.2    Mundigl, O.3    Binz, T.4    Niemann, H.5    De Camilli, P.6
  • 14
    • 18144400440 scopus 로고    scopus 로고
    • Tetanus neurotoxin-mediated cleavage of cellubrevin impairs epithelial cell migration and integrin-dependent cell adhesion
    • Proux-Gillardeaux V., Gavard J., Irinopoulou T., Mege R.M., Galli T. (2005) Tetanus neurotoxin-mediated cleavage of cellubrevin impairs epithelial cell migration and integrin-dependent cell adhesion. Proc Natl Acad Sci USA 102: 6362-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6362-6367
    • Proux-Gillardeaux, V.1    Gavard, J.2    Irinopoulou, T.3    Mege, R.M.4    Galli, T.5
  • 15
    • 59649096973 scopus 로고    scopus 로고
    • Silencing of VAMP3 inhibits cell migration and integrin-mediated adhesion
    • Luftman K., Hasan N., Day P., Hardee D., Hu C. (2009) Silencing of VAMP3 inhibits cell migration and integrin-mediated adhesion. Biochem Biophys Res Commun 380: 65-70.
    • (2009) Biochem Biophys Res Commun , vol.380 , pp. 65-70
    • Luftman, K.1    Hasan, N.2    Day, P.3    Hardee, D.4    Hu, C.5
  • 16
    • 0032978225 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking
    • Steegmaier M., Klumperman J., Foletti D.L., Yoo J.S., Scheller R.H. (1999) Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking. Mol Biol Cell 10: 1957-72.
    • (1999) Mol Biol Cell , vol.10 , pp. 1957-1972
    • Steegmaier, M.1    Klumperman, J.2    Foletti, D.L.3    Yoo, J.S.4    Scheller, R.H.5
  • 18
    • 0031697114 scopus 로고    scopus 로고
    • A novel synaptobrevin/VAMP homologous protein (VAMP5) is increased during in vitro myogenesis and present in the plasma membrane
    • Zeng Q., Subramaniam V.N., Wong S.H., Tang B.L., Parton R.G., Rea S., James D.E., Hong W. (1998) A novel synaptobrevin/VAMP homologous protein (VAMP5) is increased during in vitro myogenesis and present in the plasma membrane. Mol Biol Cell 9: 2423-37.
    • (1998) Mol Biol Cell , vol.9 , pp. 2423-2437
    • Zeng, Q.1    Subramaniam, V.N.2    Wong, S.H.3    Tang, B.L.4    Parton, R.G.5    Rea, S.6    James, D.E.7    Hong, W.8
  • 20
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • Galli T., Zahraoui A., Vaidyanathan V.V., Raposo G., Tian J.M., Karin M., Niemann H., Louvard D. (1998) A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol Biol Cell 9: 1437-48.
    • (1998) Mol Biol Cell , vol.9 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3    Raposo, G.4    Tian, J.M.5    Karin, M.6    Niemann, H.7    Louvard, D.8
  • 21
    • 35548970161 scopus 로고    scopus 로고
    • Distinct v-SNAREs regulate direct and indirect apical delivery in polarized epithelial cells
    • Pocard T., Le Bivic A., Galli T., Zurzolo C. (2007) Distinct v-SNAREs regulate direct and indirect apical delivery in polarized epithelial cells. J Cell Sci 120: 3309-20.
    • (2007) J Cell Sci , vol.120 , pp. 3309-3320
    • Pocard, T.1    Le Bivic, A.2    Galli, T.3    Zurzolo, C.4
  • 22
    • 0000926518 scopus 로고    scopus 로고
    • Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome
    • Wong S.H., Zhang T., Xu Y., Subramaniam V.N., Griffiths G., Hong W. (1998) Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome. Mol Biol Cell 9: 1549-63.
    • (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
  • 23
    • 0033787382 scopus 로고    scopus 로고
    • The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes
    • Antonin W., Holroyd C., Tikkanen R., Honing S., Jahn R. (2000) The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes. Mol Biol Cell 11: 3289-98.
    • (2000) Mol Biol Cell , vol.11 , pp. 3289-3298
    • Antonin, W.1    Holroyd, C.2    Tikkanen, R.3    Honing, S.4    Jahn, R.5
  • 24
    • 4544227227 scopus 로고    scopus 로고
    • A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells
    • Wang C.C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.F., Hong W. (2004) A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells. Dev Cell 7: 359-71.
    • (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
  • 25
    • 0344178042 scopus 로고    scopus 로고
    • Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment
    • Zhang T., Wong S.H., Tang B.L., Xu Y., Hong W. (1999) Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment. Mol Biol Cell 10: 435-53.
    • (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
  • 26
    • 0034607967 scopus 로고    scopus 로고
    • Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking
    • Hatsuzawa K., Hirose H., Tani K., Yamamoto A., Scheller R.H., Tagaya M. (2000) Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking. J Biol Chem 275: 13713-20.
    • (2000) J Biol Chem , vol.275 , pp. 13713-13720
    • Hatsuzawa, K.1    Hirose, H.2    Tani, K.3    Yamamoto, A.4    Scheller, R.H.5    Tagaya, M.6
  • 27
    • 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
    • Zhang T., Hong W. (2001) 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: 27480-7.
    • (2001) J Biol Chem , vol.276 , pp. 27480-27487
    • Zhang, T.1    Hong, W.2
  • 28
    • 1842636943 scopus 로고    scopus 로고
    • Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation
    • Fukasawa M., Varlamov O., Eng W.S., Sollner T.H., Rothman J.E. (2004) Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation. Proc Natl Acad Sci USA 101: 4815-20.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4815-4820
    • Fukasawa, M.1    Varlamov, O.2    Eng, W.S.3    Sollner, T.H.4    Rothman, J.E.5
  • 29
    • 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
    • Tai G., Lu L., Wang T.L., Tang B.L., Goud B., Johannes L., Hong W. (2004) 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: 4011-22.
    • (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
  • 31
    • 51049112074 scopus 로고    scopus 로고
    • Substrate recognition of VAMP-2 by botulinum neurotoxin B and tetanus neurotoxin
    • Chen S., Hall C., Barbieri J.T. (2008) Substrate recognition of VAMP-2 by botulinum neurotoxin B and tetanus neurotoxin. J Biol Chem 283: 21153-9.
    • (2008) J Biol Chem , vol.283 , pp. 21153-21159
    • Chen, S.1    Hall, C.2    Barbieri, J.T.3
  • 32
    • 33644859288 scopus 로고    scopus 로고
    • Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity
    • Arndt J.W., Chai Q., Christian T., Stevens R.C. (2006) Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity. Biochemistry 45: 3255-62.
    • (2006) Biochemistry , vol.45 , pp. 3255-3262
    • Arndt, J.W.1    Chai, Q.2    Christian, T.3    Stevens, R.C.4
  • 33
    • 24344470084 scopus 로고    scopus 로고
    • Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design
    • Agarwal R., Binz T., Swaminathan S. (2005) Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design. Biochemistry 44: 11758-65.
    • (2005) Biochemistry , vol.44 , pp. 11758-11765
    • Agarwal, R.1    Binz, T.2    Swaminathan, S.3
  • 34
    • 0034121745 scopus 로고    scopus 로고
    • How botulinum and tetanus neurotoxins block neurotransmitter release
    • Humeau Y., Doussau F., Grant N.J., Poulain B. (2000) How botulinum and tetanus neurotoxins block neurotransmitter release. Biochimie 82: 427-46.
    • (2000) Biochimie , vol.82 , pp. 427-446
    • Humeau, Y.1    Doussau, F.2    Grant, N.J.3    Poulain, B.4
  • 36
    • 0030787389 scopus 로고    scopus 로고
    • The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F
    • Pellizzari R., Mason S., Shone C.C., Montecucco C. (1997) The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F. FEBS Lett 409: 339-42.
    • (1997) FEBS Lett , vol.409 , pp. 339-342
    • Pellizzari, R.1    Mason, S.2    Shone, C.C.3    Montecucco, C.4
  • 37
    • 51049104533 scopus 로고    scopus 로고
    • Substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins
    • Sikorra S., Henke T., Galli T., Binz T. (2008) Substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins. J Biol Chem 283: 21145-52.
    • (2008) J Biol Chem , vol.283 , pp. 21145-21152
    • Sikorra, S.1    Henke, T.2    Galli, T.3    Binz, T.4
  • 38
    • 0000080858 scopus 로고
    • Clostridium botulinum type F with recent observations on other types
    • Dolman C.E., L. Murakami (1961) Clostridium botulinum type F with recent observations on other types. J Infect Dis 109: 107-28.
    • (1961) J Infect Dis , vol.109 , pp. 107-128
    • Dolman, C.E.1    Murakami, L.2
  • 39
    • 28544452195 scopus 로고    scopus 로고
    • A role for the phagosome in cytokine secretion
    • Murray R.Z., Kay J.G., Sangermani D.G., Stow J.L. (2005) A role for the phagosome in cytokine secretion. Science 310: 1492-5.
    • (2005) Science , vol.310 , pp. 1492-1495
    • Murray, R.Z.1    Kay, J.G.2    Sangermani, D.G.3    Stow, J.L.4
  • 40
    • 0029811998 scopus 로고    scopus 로고
    • Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins
    • Pellizzari R., Rossetto O., Lozzi L., Giovedi S., Johnson E., Shone C.C., Montecucco C. (1996) Structural determinants of the specificity for synaptic vesicle-associated membrane protein/synaptobrevin of tetanus and botulinum type B and G neurotoxins. J Biol Chem 271: 20353-8.
    • (1996) J Biol Chem , vol.271 , pp. 20353-20358
    • Pellizzari, R.1    Rossetto, O.2    Lozzi, L.3    Giovedi, S.4    Johnson, E.5    Shone, C.C.6    Montecucco, C.7


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