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Volumn 108, Issue 42, 2011, Pages 17325-17330

A lipid-anchored SNARE supports membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; LIPID; LIPID LINKED PROTEIN; Q SNARE PROTEIN; SNARE PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL A1;

EID: 80054811004     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1113888108     Document Type: Article
Times cited : (43)

References (39)
  • 2
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs - Engines for membrane fusion
    • DOI 10.1038/nrm2002, PII NRM2002
    • Jahn R, Scheller RH (2006) SNAREs - Engines for membrane fusion. Nat Rev Mol Cell Biol 7:631-643. (Pubitemid 44268209)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.9 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 3
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • Südhof TC, Rothman JE (2009) Membrane fusion: Grappling with SNARE and SM proteins. Science 323:474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 5
    • 44849125083 scopus 로고    scopus 로고
    • Regulation of SNARE-mediated membrane fusion during exocytosis
    • McNew JA (2008) Regulation of SNARE-mediated membrane fusion during exocytosis. Chem Rev 108:1669-1686.
    • (2008) Chem Rev , vol.108 , pp. 1669-1686
    • McNew, J.A.1
  • 6
    • 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
    • Wickner W (2010) 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 26:115-136.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 115-136
    • Wickner, W.1
  • 7
    • 0033197735 scopus 로고    scopus 로고
    • The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion
    • DOI 10.1016/S1097-2765(00)80343-3
    • McNew JA, Weber T, Engelman DM, Söllner TH, Rothman JE (1999) The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion. Mol Cell 4:415-421. (Pubitemid 29499794)
    • (1999) Molecular Cell , vol.4 , Issue.3 , pp. 415-421
    • McNew, J.A.1    Weber, T.2    Engelman, D.M.3    Sollner, T.H.4    Rothman, J.E.5
  • 9
    • 0034675978 scopus 로고    scopus 로고
    • Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion
    • Grote E, Baba M, Ohsumi Y, Novick PJ (2000) Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion. J Cell Biol 151:453-466.
    • (2000) J Cell Biol , vol.151 , pp. 453-466
    • Grote, E.1    Baba, M.2    Ohsumi, Y.3    Novick, P.J.4
  • 10
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • DOI 10.1016/S0092-8674(00)80512-7
    • Hanson PI, Roth R, Morisaki H, Jahn R, Heuser JE (1997) Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90:523-535. (Pubitemid 27347242)
    • (1997) Cell , vol.90 , Issue.3 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 11
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • Stein A, Weber G, Wahl MC, Jahn R (2009) Helical extension of the neuronal SNARE complex into the membrane. Nature 460:525-528.
    • (2009) Nature , vol.460 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 16
    • 0034648836 scopus 로고    scopus 로고
    • Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
    • McNew JA, et al. (2000) Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature 407:153-159.
    • (2000) Nature , vol.407 , pp. 153-159
    • McNew, J.A.1
  • 17
    • 0037086618 scopus 로고    scopus 로고
    • Yeast vacuoles and membrane fusion pathways
    • Wickner W (2002) Yeast vacuoles and membrane fusion pathways. EMBO J 21:1241-1247.
    • (2002) EMBO J , vol.21 , pp. 1241-1247
    • Wickner, W.1
  • 19
    • 33646128965 scopus 로고    scopus 로고
    • Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
    • Stroupe C, Collins KM, Fratti RA, Wickner W (2006) Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J 25:1579-1589.
    • (2006) EMBO J , vol.25 , pp. 1579-1589
    • Stroupe, C.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4
  • 20
    • 0035126830 scopus 로고    scopus 로고
    • Vam3p structure reveals conserved and divergent properties of syntaxins
    • DOI 10.1038/85012
    • Dulubova I, Yamaguchi T, Wang Y, Südhof TC, Rizo J (2001) Vam3p structure reveals conserved and divergent properties of syntaxins. Nat Struct Biol 8:258-264. (Pubitemid 32180054)
    • (2001) Nature Structural Biology , vol.8 , Issue.3 , pp. 258-264
    • Dulubova, I.1    Yamaguchi, T.2    Wang, Y.3    Sudhof, T.C.4    Rizo, J.5
  • 21
    • 79960303122 scopus 로고    scopus 로고
    • HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites
    • Kramer L, Ungermann C (2011) HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell 22:2601-2611.
    • (2011) Mol Biol Cell , vol.22 , pp. 2601-2611
    • Kramer, L.1    Ungermann, C.2
  • 22
    • 37149039641 scopus 로고    scopus 로고
    • Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion
    • DOI 10.1038/sj.emboj.7601915, PII 7601915
    • Jun Y, Xu H, Thorngren N, Wickner W (2007) Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. EMBO J 26:4935-4945. (Pubitemid 350261278)
    • (2007) EMBO Journal , vol.26 , Issue.24 , pp. 4935-4945
    • Jun, Y.1    Xu, H.2    Thorngren, N.3    Wickner, W.4
  • 23
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck DK, Hoekstra D, Pagano RE (1981) Use of resonance energy transfer to monitor membrane fusion. Biochemistry 20:4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 24
    • 65649153795 scopus 로고    scopus 로고
    • Capture and release of partially zipped trans-SNARE complexes on intact organelles
    • Schwartz ML, Merz AJ (2009) Capture and release of partially zipped trans-SNARE complexes on intact organelles. J Cell Biol 185:535-549.
    • (2009) J Cell Biol , vol.185 , pp. 535-549
    • Schwartz, M.L.1    Merz, A.J.2
  • 25
    • 77953608974 scopus 로고    scopus 로고
    • HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion
    • Xu H, Jun Y, Thompson J, Yates J, Wickner W (2010) HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion. EMBO J 29:1948-1960.
    • (2010) EMBO J , vol.29 , pp. 1948-1960
    • Xu, H.1    Jun, Y.2    Thompson, J.3    Yates, J.4    Wickner, W.5
  • 26
    • 78649821097 scopus 로고    scopus 로고
    • Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly
    • Xu H, Wickner W (2010) Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly. J Biol Chem 285:39359-39365.
    • (2010) J Biol Chem , vol.285 , pp. 39359-39365
    • Xu, H.1    Wickner, W.2
  • 27
    • 0037449809 scopus 로고    scopus 로고
    • The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes to promote homotypic vacuole fusion
    • DOI 10.1074/jbc.M209522200
    • Rohde J, Dietrich L, Langosch D, Ungermann C (2003) The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes to promote homotypic vacuole fusion. J Biol Chem 278:1656-1662. (Pubitemid 36801397)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.3 , pp. 1656-1662
    • Rohde, J.1    Dietrich, L.2    Langosch, D.3    Ungermann, C.4
  • 29
    • 33646151867 scopus 로고    scopus 로고
    • Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion
    • Dennison SM, Bowen ME, Brunger AT, Lentz BR (2006) Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion. Biophys J 90:1661-1675.
    • (2006) Biophys J , vol.90 , pp. 1661-1675
    • Dennison, S.M.1    Bowen, M.E.2    Brunger, A.T.3    Lentz, B.R.4
  • 30
    • 80054793989 scopus 로고    scopus 로고
    • Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to smal molecules and by lysis
    • in press
    • Zucchi PC, Zick M (2011) Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to smal molecules and by lysis. Mol Biol Cell, in press.
    • (2011) Mol Biol Cell
    • Zucchi, P.C.1    Zick, M.2
  • 31
    • 33745938170 scopus 로고    scopus 로고
    • Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release
    • DOI 10.1016/j.tcb.2006.04.006, PII S0962892406001206
    • Rizo J, Chen X, Araç D (2006) Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release. Trends Cell Biol 16:339-350. (Pubitemid 44062312)
    • (2006) Trends in Cell Biology , vol.16 , Issue.7 , pp. 339-350
    • Rizo, J.1    Chen, X.2    Arac, D.3
  • 32
    • 11244258475 scopus 로고    scopus 로고
    • Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
    • DOI 10.1083/jcb.200409068
    • Fratti RA, Jun Y, Merz AJ, Margolis N, Wickner W (2004) Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles. J Cell Biol 167:1087-1098. (Pubitemid 40066624)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1087-1098
    • Fratti, R.A.1    Jun, Y.2    Merz, A.J.3    Margolis, N.4    Wickner, W.5    Wickner, B.6
  • 35
    • 77954194779 scopus 로고    scopus 로고
    • HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly
    • Hickey CM, Wickner W (2010) HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Mol Biol Cell 21:2297-2305.
    • (2010) Mol Biol Cell , vol.21 , pp. 2297-2305
    • Hickey, C.M.1    Wickner, W.2
  • 36
    • 3542999933 scopus 로고    scopus 로고
    • A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion
    • DOI 10.1038/sj.emboj.7600286
    • Thorngren N, Collins KM, Fratti RA, Wickner W, Merz AJ (2004) A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. EMBO J 23:2765-2776. (Pubitemid 39013549)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2765-2776
    • Thorngren, N.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4    Merz, A.J.5
  • 37
    • 48749099702 scopus 로고    scopus 로고
    • HOPS proofreads the trans-SNARE complex for yeast vacuole fusion
    • Starai VJ, Hickey CM, Wickner W (2008) HOPS proofreads the trans-SNARE complex for yeast vacuole fusion. Mol Biol Cell 19:2500-2508.
    • (2008) Mol Biol Cell , vol.19 , pp. 2500-2508
    • Starai, V.J.1    Hickey, C.M.2    Wickner, W.3
  • 38
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of 'parallel' expression vectors
    • DOI 10.1006/prep.1998.1003
    • Sheffield P, Garrard S, Derewenda Z (1999) Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expr Purif 15:34-39. (Pubitemid 29321466)
    • (1999) Protein Expression and Purification , vol.15 , Issue.1 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 39
    • 49149131497 scopus 로고    scopus 로고
    • Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones
    • Mima J, Hickey CM, Xu H, Jun Y, Wickner W (2008) Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones. EMBO J 27:2031-2042.
    • (2008) EMBO J , vol.27 , pp. 2031-2042
    • Mima, J.1    Hickey, C.M.2    Xu, H.3    Jun, Y.4    Wickner, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.