메뉴 건너뛰기




Volumn 38, Issue 2, 2013, Pages 57-63

Connections between SNAREs and autophagy

Author keywords

Autophagy; Lysosome; SNARE

Indexed keywords

HYDROLASE; LYSOSOME ENZYME; MICROTUBULE ASSOCIATED PROTEIN 1; PROTEIN BCL 2; PROTEIN BCL XL; SNARE PROTEIN; SOLUBLE N ETHYLMALEIMIDE SENSITIVE FACTOR ATTACHMENT PROTEIN; SYNAPTOBREVIN;

EID: 84872793852     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2012.11.004     Document Type: Review
Times cited : (123)

References (52)
  • 1
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B., Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008, 132:27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 2
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein D.C., et al. Autophagy modulation as a potential therapeutic target for diverse diseases. Nat. Rev. Drug Discov. 2012, 11:709-730.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1
  • 3
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., et al. Autophagy fights disease through cellular self-digestion. Nature 2008, 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1
  • 4
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: renovation of cells and tissues
    • Mizushima N., Komatsu M. Autophagy: renovation of cells and tissues. Cell 2011, 147:728-741.
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 5
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie Z., Klionsky D.J. Autophagosome formation: core machinery and adaptations. Nat. Cell Biol. 2007, 9:1102-1109.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 6
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: minimal machinery for membrane fusion
    • Weber T., et al. SNAREpins: minimal machinery for membrane fusion. Cell 1998, 92:759-772.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1
  • 8
    • 77952495224 scopus 로고    scopus 로고
    • Mitochondria supply membranes for autophagosome biogenesis during starvation
    • Hailey D.W., et al. Mitochondria supply membranes for autophagosome biogenesis during starvation. Cell 2010, 141:656-667.
    • (2010) Cell , vol.141 , pp. 656-667
    • Hailey, D.W.1
  • 9
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • Hayashi-Nishino M., et al. A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat. Cell Biol. 2009, 11:1433-1437.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1433-1437
    • Hayashi-Nishino, M.1
  • 10
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • Ravikumar B., et al. Plasma membrane contributes to the formation of pre-autophagosomal structures. Nat. Cell Biol. 2010, 12:747-757.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 747-757
    • Ravikumar, B.1
  • 11
    • 77954197767 scopus 로고    scopus 로고
    • Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae
    • van der Vaart A., et al. Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae. Mol. Biol. Cell 2010, 21:2270-2284.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2270-2284
    • van der Vaart, A.1
  • 12
    • 75749135725 scopus 로고    scopus 로고
    • The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy
    • Yen W.L., et al. The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy. J. Cell Biol. 2010, 188:101-114.
    • (2010) J. Cell Biol. , vol.188 , pp. 101-114
    • Yen, W.L.1
  • 13
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • Yla-Anttila P., et al. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 2009, 5:1180-1185.
    • (2009) Autophagy , vol.5 , pp. 1180-1185
    • Yla-Anttila, P.1
  • 14
    • 84859965801 scopus 로고    scopus 로고
    • Arf6 promotes autophagosome formation via effects on phosphatidylinositol 4,5-bisphosphate and phospholipase D
    • Moreau K., et al. Arf6 promotes autophagosome formation via effects on phosphatidylinositol 4,5-bisphosphate and phospholipase D. J. Cell Biol. 2012, 196:483-496.
    • (2012) J. Cell Biol. , vol.196 , pp. 483-496
    • Moreau, K.1
  • 15
    • 79960774898 scopus 로고    scopus 로고
    • Autophagosome precursor maturation requires homotypic fusion
    • Moreau K., et al. Autophagosome precursor maturation requires homotypic fusion. Cell 2011, 146:303-317.
    • (2011) Cell , vol.146 , pp. 303-317
    • Moreau, K.1
  • 16
    • 79960798816 scopus 로고    scopus 로고
    • SNARE proteins are required for macroautophagy
    • Nair U., et al. SNARE proteins are required for macroautophagy. Cell 2011, 146:290-302.
    • (2011) Cell , vol.146 , pp. 290-302
    • Nair, U.1
  • 17
    • 84862626146 scopus 로고    scopus 로고
    • The plasma membrane as a control center for autophagy
    • Moreau K., Rubinsztein D.C. The plasma membrane as a control center for autophagy. Autophagy 2012, 8:861-863.
    • (2012) Autophagy , vol.8 , pp. 861-863
    • Moreau, K.1    Rubinsztein, D.C.2
  • 18
    • 72049088519 scopus 로고    scopus 로고
    • TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways
    • Fader C.M., et al. TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways. Biochim. Biophys. Acta 2009, 1793:1901-1916.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1901-1916
    • Fader, C.M.1
  • 19
    • 77949448601 scopus 로고    scopus 로고
    • Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes
    • Furuta N., et al. Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes. Mol. Biol. Cell 2010, 21:1001-1010.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1001-1010
    • Furuta, N.1
  • 20
    • 70350395467 scopus 로고    scopus 로고
    • Endosomal fusion upon SNARE knockdown is maintained by residual SNARE activity and enhanced docking
    • Bethani I., et al. Endosomal fusion upon SNARE knockdown is maintained by residual SNARE activity and enhanced docking. Traffic 2009, 10:1543-1559.
    • (2009) Traffic , vol.10 , pp. 1543-1559
    • Bethani, I.1
  • 21
    • 46449120732 scopus 로고    scopus 로고
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
    • Liang C., et al. Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat. Cell Biol. 2008, 10:776-787.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 776-787
    • Liang, C.1
  • 22
    • 64049086758 scopus 로고    scopus 로고
    • Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
    • Matsunaga K., et al. Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat. Cell Biol. 2009, 11:385-396.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 385-396
    • Matsunaga, K.1
  • 23
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations
    • Lee J.H., et al. Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell 2010, 141:1146-1158.
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1
  • 24
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse E., et al. VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 2010, 6:217-227.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1
  • 25
    • 7244255989 scopus 로고    scopus 로고
    • Role for Rab7 in maturation of late autophagic vacuoles
    • Jager S., et al. Role for Rab7 in maturation of late autophagic vacuoles. J. Cell Sci. 2004, 117:4837-4848.
    • (2004) J. Cell Sci. , vol.117 , pp. 4837-4848
    • Jager, S.1
  • 26
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • Zhong Y., et al. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat. Cell Biol. 2009, 11:468-476.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 468-476
    • Zhong, Y.1
  • 27
    • 35948983328 scopus 로고    scopus 로고
    • Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
    • Filimonenko M., et al. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J. Cell Biol. 2007, 179:485-500.
    • (2007) J. Cell Biol. , vol.179 , pp. 485-500
    • Filimonenko, M.1
  • 28
    • 35348869859 scopus 로고    scopus 로고
    • ESCRTs and Fab1 regulate distinct steps of autophagy
    • Rusten T.E., et al. ESCRTs and Fab1 regulate distinct steps of autophagy. Curr. Biol. 2007, 17:1817-1825.
    • (2007) Curr. Biol. , vol.17 , pp. 1817-1825
    • Rusten, T.E.1
  • 29
    • 0030807624 scopus 로고    scopus 로고
    • A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole
    • Darsow T., et al. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J. Cell Biol. 1997, 138:517-529.
    • (1997) J. Cell Biol. , vol.138 , pp. 517-529
    • Darsow, T.1
  • 30
    • 0031841313 scopus 로고    scopus 로고
    • Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking
    • Sato T.K., et al. Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. Mol. Cell. Biol. 1998, 18:5308-5319.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5308-5319
    • Sato, T.K.1
  • 31
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer A., Wickner W. Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol. 1997, 136:307-317.
    • (1997) J. Cell Biol. , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 32
    • 0035192612 scopus 로고    scopus 로고
    • Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion
    • Ishihara N., et al. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol. Biol. Cell 2001, 12:3690-3702.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3690-3702
    • Ishihara, N.1
  • 33
    • 78149282263 scopus 로고    scopus 로고
    • Lysosomal fusion and SNARE function are impaired by cholesterol accumulation in lysosomal storage disorders
    • Fraldi A., et al. Lysosomal fusion and SNARE function are impaired by cholesterol accumulation in lysosomal storage disorders. EMBO J. 2010, 29:3607-3620.
    • (2010) EMBO J. , vol.29 , pp. 3607-3620
    • Fraldi, A.1
  • 34
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A., et al. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct. Funct. 1998, 23:33-42.
    • (1998) Cell Struct. Funct. , vol.23 , pp. 33-42
    • Yamamoto, A.1
  • 35
    • 79551546749 scopus 로고    scopus 로고
    • Autophagic substrate clearance requires activity of the syntaxin-5 SNARE complex
    • Renna M., et al. Autophagic substrate clearance requires activity of the syntaxin-5 SNARE complex. J. Cell Sci. 2011, 124:469-482.
    • (2011) J. Cell Sci. , vol.124 , pp. 469-482
    • Renna, M.1
  • 36
    • 84864295258 scopus 로고    scopus 로고
    • Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation
    • Deretic V., et al. Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation. Trends Cell Biol. 2012, 22:397-406.
    • (2012) Trends Cell Biol. , vol.22 , pp. 397-406
    • Deretic, V.1
  • 37
    • 79956325949 scopus 로고    scopus 로고
    • Spatial coupling of mTOR and autophagy augments secretory phenotypes
    • Narita M., et al. Spatial coupling of mTOR and autophagy augments secretory phenotypes. Science 2011, 332:966-970.
    • (2011) Science , vol.332 , pp. 966-970
    • Narita, M.1
  • 38
    • 77149152566 scopus 로고    scopus 로고
    • Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation
    • Manjithaya R., et al. Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation. J. Cell Biol. 2010, 188:537-546.
    • (2010) J. Cell Biol. , vol.188 , pp. 537-546
    • Manjithaya, R.1
  • 39
    • 84855490021 scopus 로고    scopus 로고
    • Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion
    • Bruns C., et al. Biogenesis of a novel compartment for autophagosome-mediated unconventional protein secretion. J. Cell Biol. 2011, 195:979-992.
    • (2011) J. Cell Biol. , vol.195 , pp. 979-992
    • Bruns, C.1
  • 40
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta
    • Dupont N., et al. Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta. EMBO J. 2011, 30:4701-4711.
    • (2011) EMBO J. , vol.30 , pp. 4701-4711
    • Dupont, N.1
  • 41
    • 80052277733 scopus 로고    scopus 로고
    • Rescue of DeltaF508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway
    • Gee H.Y., et al. Rescue of DeltaF508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway. Cell 2011, 146:746-760.
    • (2011) Cell , vol.146 , pp. 746-760
    • Gee, H.Y.1
  • 42
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • Cadwell K., et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 2008, 456:259-263.
    • (2008) Nature , vol.456 , pp. 259-263
    • Cadwell, K.1
  • 43
    • 83455173649 scopus 로고    scopus 로고
    • Autophagy proteins regulate the secretory component of osteoclastic bone resorption
    • DeSelm C.J., et al. Autophagy proteins regulate the secretory component of osteoclastic bone resorption. Dev. Cell 2011, 21:966-974.
    • (2011) Dev. Cell , vol.21 , pp. 966-974
    • DeSelm, C.J.1
  • 44
    • 79955577268 scopus 로고    scopus 로고
    • Crucial role for autophagy in degranulation of mast cells
    • Ushio H., et al. Crucial role for autophagy in degranulation of mast cells. J. Allergy Clin. Immunol. 2011, 127:1267-1276.
    • (2011) J. Allergy Clin. Immunol. , vol.127 , pp. 1267-1276
    • Ushio, H.1
  • 45
    • 83755181759 scopus 로고    scopus 로고
    • Autophagy-dependent anticancer immune responses induced by chemotherapeutic agents in mice
    • Michaud M., et al. Autophagy-dependent anticancer immune responses induced by chemotherapeutic agents in mice. Science 2011, 334:1573-1577.
    • (2011) Science , vol.334 , pp. 1573-1577
    • Michaud, M.1
  • 46
    • 28244440230 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte exocytosis: bring on the SNAREs!
    • Hong W. Cytotoxic T lymphocyte exocytosis: bring on the SNAREs!. Trends Cell Biol. 2005, 15:644-650.
    • (2005) Trends Cell Biol. , vol.15 , pp. 644-650
    • Hong, W.1
  • 47
    • 34548814973 scopus 로고    scopus 로고
    • Defective cytotoxic lymphocyte degranulation in syntaxin-11 deficient familial hemophagocytic lymphohistiocytosis 4 (FHL4) patients
    • Bryceson Y.T., et al. Defective cytotoxic lymphocyte degranulation in syntaxin-11 deficient familial hemophagocytic lymphohistiocytosis 4 (FHL4) patients. Blood 2007, 110:1906-1915.
    • (2007) Blood , vol.110 , pp. 1906-1915
    • Bryceson, Y.T.1
  • 48
    • 77955507742 scopus 로고    scopus 로고
    • The exocytosis of lytic granules is impaired in Vti1b- or Vamp8-deficient CTL leading to a reduced cytotoxic activity following antigen-specific activation
    • Dressel R., et al. The exocytosis of lytic granules is impaired in Vti1b- or Vamp8-deficient CTL leading to a reduced cytotoxic activity following antigen-specific activation. J. Immunol. 2010, 185:1005-1014.
    • (2010) J. Immunol. , vol.185 , pp. 1005-1014
    • Dressel, R.1
  • 49
    • 67749122634 scopus 로고    scopus 로고
    • A gene network regulating lysosomal biogenesis and function
    • Sardiello M., et al. A gene network regulating lysosomal biogenesis and function. Science 2009, 325:473-477.
    • (2009) Science , vol.325 , pp. 473-477
    • Sardiello, M.1
  • 50
    • 80955177196 scopus 로고    scopus 로고
    • TFEB links autophagy to lysosomal biogenesis
    • Settembre C., et al. TFEB links autophagy to lysosomal biogenesis. Science 2011, 332:1429-1433.
    • (2011) Science , vol.332 , pp. 1429-1433
    • Settembre, C.1
  • 51
    • 80052729465 scopus 로고    scopus 로고
    • Transcriptional activation of lysosomal exocytosis promotes cellular clearance
    • Medina D.L., et al. Transcriptional activation of lysosomal exocytosis promotes cellular clearance. Dev. Cell 2011, 21:421-430.
    • (2011) Dev. Cell , vol.21 , pp. 421-430
    • Medina, D.L.1
  • 52
    • 84870880174 scopus 로고    scopus 로고
    • The Hairpin-type tail-anchored snare syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • Itakura E., et al. The Hairpin-type tail-anchored snare syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 2012, 151:1256-1269.
    • (2012) Cell , vol.151 , pp. 1256-1269
    • Itakura, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.