메뉴 건너뛰기




Volumn 128, Issue 6, 2015, Pages 1071-1081

Role of cholesterol in SNARE-mediated trafficking on intracellular membranes

Author keywords

Cell migration; Cholesterol; Integrin trafficking; Recycling endosome; SNARE protein; Trans Golgi network

Indexed keywords

CELLUBREVIN; CHOLESTEROL; INTEGRIN; LIPID; PROTEIN; SNARE PROTEIN; SYNTAXIN; SYNTAXIN 6; UNCLASSIFIED DRUG;

EID: 84925436894     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.164459     Document Type: Note
Times cited : (64)

References (117)
  • 1
    • 84883487873 scopus 로고    scopus 로고
    • Structural basis for the interaction of the Golgi-associated retrograde protein complex with the t-SNARE Syntaxin 6
    • Abascal-Palacios, G., Schindler, C., Rojas, A. L., Bonifacino, J. S. and Hierro, A. (2013). Structural basis for the interaction of the Golgi-associated retrograde protein complex with the t-SNARE Syntaxin 6. Structure 21, 1698-1706.
    • (2013) Structure , vol.21 , pp. 1698-1706
    • Abascal-Palacios, G.1    Schindler, C.2    Rojas, A.L.3    Bonifacino, J.S.4    Hierro, A.5
  • 3
    • 0033787382 scopus 로고    scopus 로고
    • The RSNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes
    • Antonin, W., Holroyd, C., Tikkanen, R., Höning, S. and Jahn, R. (2000). The RSNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes. Mol. Biol. Cell 11, 3289-3298.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3289-3298
    • Antonin, W.1    Holroyd, C.2    Tikkanen, R.3    Höning, S.4    Jahn, R.5
  • 4
    • 84860158205 scopus 로고    scopus 로고
    • Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
    • Baier, C. J., Fantini, J. and Barrantes, F. J. (2011). Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor. Sci. Rep. 1, 69.
    • (2011) Sci. Rep. , vol.1 , pp. 69
    • Baier, C.J.1    Fantini, J.2    Barrantes, F.J.3
  • 5
    • 0030797279 scopus 로고    scopus 로고
    • Syntaxin 6 functions in trans-Golgi network vesicle trafficking
    • Bock, J. B., Klumperman, J., Davanger, S. and Scheller, R. H. (1997). Syntaxin 6 functions in trans-Golgi network vesicle trafficking. Mol. Biol. Cell 8, 1261- 1271.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1261-1271
    • Bock, J.B.1    Klumperman, J.2    Davanger, S.3    Scheller, R.H.4
  • 6
    • 79952103459 scopus 로고    scopus 로고
    • Transport according to GARP: receiving retrograde cargo at the trans-Golgi network
    • Bonifacino, J. S. and Hierro, A. (2011). Transport according to GARP: receiving retrograde cargo at the trans-Golgi network. Trends Cell Biol. 21, 159-167.
    • (2011) Trends Cell Biol. , vol.21 , pp. 159-167
    • Bonifacino, J.S.1    Hierro, A.2
  • 7
    • 75449112263 scopus 로고    scopus 로고
    • Aiming for invadopodia: organizing polarized delivery at sites of invasion
    • Caldieri, G. and Buccione, R. (2010). Aiming for invadopodia: organizing polarized delivery at sites of invasion. Trends Cell Biol. 20, 64-70.
    • (2010) Trends Cell Biol. , vol.20 , pp. 64-70
    • Caldieri, G.1    Buccione, R.2
  • 8
    • 44649198353 scopus 로고    scopus 로고
    • Endocytic transport of integrins during cell migration and invasion
    • Caswell, P. and Norman, J. (2008). Endocytic transport of integrins during cell migration and invasion. Trends Cell Biol. 18, 257-263.
    • (2008) Trends Cell Biol. , vol.18 , pp. 257-263
    • Caswell, P.1    Norman, J.2
  • 9
    • 0037147217 scopus 로고    scopus 로고
    • The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent-insoluble lipid rafts present on distinct intracellular membranes
    • Chamberlain, L. H. and Gould, G. W. (2002). The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent-insoluble lipid rafts present on distinct intracellular membranes. J. Biol. Chem. 277, 49750-49754.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49750-49754
    • Chamberlain, L.H.1    Gould, G.W.2
  • 10
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis
    • Chamberlain, L. H., Burgoyne, R. D. and Gould, G. W. (2001). SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. Proc. Natl. Acad. Sci. USA 98, 5619-5624.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 11
    • 2342544065 scopus 로고    scopus 로고
    • Snorkeling preferences foster an amino acid composition bias in transmembrane helices
    • Chamberlain, A. K., Lee, Y., Kim, S. and Bowie, J. U. (2004). Snorkeling preferences foster an amino acid composition bias in transmembrane helices. J. Mol. Biol. 339, 471-479.
    • (2004) J. Mol. Biol. , vol.339 , pp. 471-479
    • Chamberlain, A.K.1    Lee, Y.2    Kim, S.3    Bowie, J.U.4
  • 13
    • 33646786476 scopus 로고    scopus 로고
    • The N-terminal 12 residue long peptide of HIV gp41 is the minimal peptide sufficient to induce significant T-cell-like membrane destabilization in vitro
    • Charloteaux, B., Lorin, A., Crowet, J. M., Stroobant, V., Lins, L., Thomas, A. and Brasseur, R. (2006). The N-terminal 12 residue long peptide of HIV gp41 is the minimal peptide sufficient to induce significant T-cell-like membrane destabilization in vitro. J. Mol. Biol. 359, 597-609.
    • (2006) J. Mol. Biol. , vol.359 , pp. 597-609
    • Charloteaux, B.1    Lorin, A.2    Crowet, J.M.3    Stroobant, V.4    Lins, L.5    Thomas, A.6    Brasseur, R.7
  • 14
    • 77951087930 scopus 로고    scopus 로고
    • MLN64 mediates egress of cholesterol from endosomes to mitochondria in the absence of functional Niemann-Pick type C1 protein
    • Charman, M., Kennedy, B. E., Osborne, N. and Karten, B. (2010). MLN64 mediates egress of cholesterol from endosomes to mitochondria in the absence of functional Niemann-Pick type C1 protein. J. Lipid Res., 51, 1023-1034.
    • (2010) J. Lipid Res. , vol.51 , pp. 1023-1034
    • Charman, M.1    Kennedy, B.E.2    Osborne, N.3    Karten, B.4
  • 16
    • 33645713636 scopus 로고    scopus 로고
    • Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface
    • Choudhury, A., Marks, D. L., Proctor, K. M., Gould, G. W. and Pagano, R. E. (2006). Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface. Nat. Cell Biol. 8, 317-328.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 317-328
    • Choudhury, A.1    Marks, D.L.2    Proctor, K.M.3    Gould, G.W.4    Pagano, R.E.5
  • 20
    • 44349160147 scopus 로고    scopus 로고
    • Annexin A6-induced inhibition of cytoplasmic phospholipase A2 is linked to caveolin-1 export from the Golgi
    • Cubells, L., Vilà de Muga, S., Tebar, F., Bonventre, J. V., Balsinde, J., Pol, A., Grewal, T. and Enrich, C. (2008). Annexin A6-induced inhibition of cytoplasmic phospholipase A2 is linked to caveolin-1 export from the Golgi. J. Biol. Chem. 283, 10174-10183.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10174-10183
    • Cubells, L.1    Vilà de Muga, S.2    Tebar, F.3    Bonventre, J.V.4    Balsinde, J.5    Pol, A.6    Grewal, T.7    Enrich, C.8
  • 21
    • 80052592689 scopus 로고    scopus 로고
    • Mendelian disorders of membrane trafficking
    • De Matteis, M. A. and Luini, A. (2011). Mendelian disorders of membrane trafficking. N. Engl. J. Med. 365, 927-938.
    • (2011) N. Engl. J. Med. , vol.365 , pp. 927-938
    • De Matteis, M.A.1    Luini, A.2
  • 23
    • 84861148125 scopus 로고    scopus 로고
    • An essential role of Hrs/ Vps27 in endosomal cholesterol trafficking
    • Du, X., Kazim, A. S., Brown, A. J. and Yang, H. (2012). An essential role of Hrs/ Vps27 in endosomal cholesterol trafficking. Cell Rep., 1, 29-35.
    • (2012) Cell Rep. , vol.1 , pp. 29-35
    • Du, X.1    Kazim, A.S.2    Brown, A.J.3    Yang, H.4
  • 24
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • Epand, R. M. (2006). Cholesterol and the interaction of proteins with membrane domains. Prog. Lipid Res. 45, 279-294.
    • (2006) Prog. Lipid Res. , vol.45 , pp. 279-294
    • Epand, R.M.1
  • 25
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains: an overview
    • Epand, R. M., Thomas, A., Brasseur, R. and Epand, R. F. (2010). Cholesterol interaction with proteins that partition into membrane domains: an overview. Subcell. Biochem. 51, 253-278.
    • (2010) Subcell. Biochem. , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 26
    • 84883556425 scopus 로고    scopus 로고
    • How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
    • Fantini, J. and Barrantes, F. J. (2013). How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains. Front. Physiol. 4, 31.
    • (2013) Front. Physiol. , vol.4 , pp. 31
    • Fantini, J.1    Barrantes, F.J.2
  • 27
    • 0030482560 scopus 로고    scopus 로고
    • Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins
    • Fincham, V. J., Unlu, M., Brunton, V. G., Pitts, J. D., Wyke, J. A. and Frame, M. C. (1996). Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J. Cell Biol. 135, 1551-1564.
    • (1996) J. Cell Biol. , vol.135 , pp. 1551-1564
    • Fincham, V.J.1    Unlu, M.2    Brunton, V.G.3    Pitts, J.D.4    Wyke, J.A.5    Frame, M.C.6
  • 30
    • 38349014268 scopus 로고    scopus 로고
    • A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
    • Ganley, I. G., Espinosa, E. and Pfeffer, S. R. (2008). A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells. J. Cell Biol. 180, 159-172.
    • (2008) J. Cell Biol. , vol.180 , pp. 159-172
    • Ganley, I.G.1    Espinosa, E.2    Pfeffer, S.R.3
  • 31
    • 0033538832 scopus 로고    scopus 로고
    • Role of cholesterol in formation and function of a signaling complex involving alphavbeta3, integrin-associated protein (CD47), and heterotrimeric G proteins
    • Green, J. M., Zhelesnyak, A., Chung, J., Lindberg, F. P., Sarfati, M., Frazier, W. A. and Brown, E. J. (1999). Role of cholesterol in formation and function of a signaling complex involving alphavbeta3, integrin-associated protein (CD47), and heterotrimeric G proteins. J. Cell Biol. 146, 673-682.
    • (1999) J. Cell Biol. , vol.146 , pp. 673-682
    • Green, J.M.1    Zhelesnyak, A.2    Chung, J.3    Lindberg, F.P.4    Sarfati, M.5    Frazier, W.A.6    Brown, E.J.7
  • 32
    • 12744273521 scopus 로고    scopus 로고
    • Golgi vesiculation induced by cholesterol occurs by a dynamin- and cPLA2- dependent mechanism
    • Grimmer, S., Ying, M., Wälchli, S., van Deurs, B. and Sandvig, K. (2005). Golgi vesiculation induced by cholesterol occurs by a dynamin- and cPLA2- dependent mechanism. Traffic 6, 144-156.
    • (2005) Traffic , vol.6 , pp. 144-156
    • Grimmer, S.1    Ying, M.2    Wälchli, S.3    van Deurs, B.4    Sandvig, K.5
  • 34
    • 0037016677 scopus 로고    scopus 로고
    • Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle
    • Hao, M., Lin, S. X., Karylowski, O. J., Wüstner, D., McGraw, T. E. and Maxfield, F. R. (2002). Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle. J. Biol. Chem. 277, 609-617.
    • (2002) J. Biol. Chem. , vol.277 , pp. 609-617
    • Hao, M.1    Lin, S.X.2    Karylowski, O.J.3    Wüstner, D.4    McGraw, T.E.5    Maxfield, F.R.6
  • 35
    • 33646544088 scopus 로고    scopus 로고
    • Apolipoprotein E recycling: implications for dyslipidemia and atherosclerosis
    • Heeren, J., Beisiegel, U. and Grewal, T. (2006). Apolipoprotein E recycling: implications for dyslipidemia and atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 26, 442-448.
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 442-448
    • Heeren, J.1    Beisiegel, U.2    Grewal, T.3
  • 37
    • 20444407298 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
  • 38
    • 84890884015 scopus 로고    scopus 로고
    • Tethering the assembly of SNARE complexes
    • Hong, W. and Lev, S. (2014). Tethering the assembly of SNARE complexes. Trends Cell Biol. 24, 35-43.
    • (2014) Trends Cell Biol. , vol.24 , pp. 35-43
    • Hong, W.1    Lev, S.2
  • 39
    • 77955051719 scopus 로고    scopus 로고
    • Transport at the recycling endosome
    • Hsu, V. W. and Prekeris, R. (2010). Transport at the recycling endosome. Curr. Opin. Cell Biol. 22, 528-534.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 528-534
    • Hsu, V.W.1    Prekeris, R.2
  • 40
    • 84874644958 scopus 로고    scopus 로고
    • Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells
    • Hulce, J. J., Cognetta, A. B., Niphakis, M. J., Tully, S. E. and Cravatt, B. F. (2013). Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat. Methods 10, 259-264.
    • (2013) Nat. Methods , vol.10 , pp. 259-264
    • Hulce, J.J.1    Cognetta, A.B.2    Niphakis, M.J.3    Tully, S.E.4    Cravatt, B.F.5
  • 42
    • 33749464296 scopus 로고    scopus 로고
    • Mechanisms for cellular cholesterol transport: defects and human disease
    • Ikonen, E. (2006). Mechanisms for cellular cholesterol transport: defects and human disease. Physiol. Rev. 86, 1237-1261.
    • (2006) Physiol. Rev. , vol.86 , pp. 1237-1261
    • Ikonen, E.1
  • 43
    • 38549141572 scopus 로고    scopus 로고
    • Cellular cholesterol trafficking and compartmentalization
    • Ikonen, E. (2008). Cellular cholesterol trafficking and compartmentalization. Nat. Rev. Mol. Cell Biol. 9, 125-138.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 125-138
    • Ikonen, E.1
  • 44
    • 2942665893 scopus 로고    scopus 로고
    • Cellular pathology of Niemann-Pick type C disease
    • Ikonen, E. and Hölttä-Vuori, M. (2004). Cellular pathology of Niemann-Pick type C disease. Semin. Cell Dev. Biol. 15, 445-454.
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 445-454
    • Ikonen, E.1    Hölttä-Vuori, M.2
  • 45
    • 47149103256 scopus 로고    scopus 로고
    • Cellular sterol trafficking and metabolism: spotlight on structure
    • Ikonen, E. and Jansen, M. (2008). Cellular sterol trafficking and metabolism: spotlight on structure. Curr. Opin. Cell Biol. 20, 371-377.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 371-377
    • Ikonen, E.1    Jansen, M.2
  • 46
    • 55749083068 scopus 로고    scopus 로고
    • NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes
    • Infante, R. E., Wang, M. L., Radhakrishnan, A., Kwon, H. J., Brown, M. S. and Goldstein, J. L. (2008). NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes. Proc. Natl. Acad. Sci. USA 105, 15287-15292.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15287-15292
    • Infante, R.E.1    Wang, M.L.2    Radhakrishnan, A.3    Kwon, H.J.4    Brown, M.S.5    Goldstein, J.L.6
  • 48
    • 33748466150 scopus 로고    scopus 로고
    • Endocytic recycling pathways: emerging regulators of cell migration
    • Jones, M. C., Caswell, P. T. and Norman, J. C. (2006). Endocytic recycling pathways: emerging regulators of cell migration. Curr. Opin. Cell Biol. 18, 549- 557.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 549-557
    • Jones, M.C.1    Caswell, P.T.2    Norman, J.C.3
  • 49
    • 84863705415 scopus 로고    scopus 로고
    • Regulation of intracellular membrane trafficking and cell dynamics by syntaxin-6
    • Jung, J. J., Inamdar, S. M., Tiwari, A. and Choudhury, A. (2012). Regulation of intracellular membrane trafficking and cell dynamics by syntaxin-6. Biosci. Rep. 32, 383-391.
    • (2012) Biosci. Rep. , vol.32 , pp. 383-391
    • Jung, J.J.1    Inamdar, S.M.2    Tiwari, A.3    Choudhury, A.4
  • 50
    • 84887615640 scopus 로고    scopus 로고
    • LDL cholesterol recycles to the plasma membrane via a Rab8a-Myosin5b-actin-dependent membrane transport route
    • Kanerva, K., Uronen, R. L., Blom, T., Li, S., Bittman, R., Lappalainen, P., Peränen, J., Raposo, G. and Ikonen, E. (2013). LDL cholesterol recycles to the plasma membrane via a Rab8a-Myosin5b-actin-dependent membrane transport route. Dev. Cell 27, 249-262.
    • (2013) Dev. Cell , vol.27 , pp. 249-262
    • Kanerva, K.1    Uronen, R.L.2    Blom, T.3    Li, S.4    Bittman, R.5    Lappalainen, P.6    Peränen, J.7    Raposo, G.8    Ikonen, E.9
  • 52
    • 33644814231 scopus 로고    scopus 로고
    • NPC2 is expressed in human and murine liver and secreted into bile: potential implications for body cholesterol homeostasis
    • Klein, A., Amigo, L., Retamal, M. J., Morales, M. G., Miquel, J. F., Rigotti, A. and Zanlungo, S. (2006). NPC2 is expressed in human and murine liver and secreted into bile: potential implications for body cholesterol homeostasis. Hepatology 43, 126-133.
    • (2006) Hepatology , vol.43 , pp. 126-133
    • Klein, A.1    Amigo, L.2    Retamal, M.J.3    Morales, M.G.4    Miquel, J.F.5    Rigotti, A.6    Zanlungo, S.7
  • 53
    • 0036534286 scopus 로고    scopus 로고
    • The sterol-sensing domain: multiple families a unique role?
    • Kuwabara, P. E. and Labouesse, M. (2002). The sterol-sensing domain: multiple families, a unique role? Trends Genet. 18, 193-201.
    • (2002) Trends Genet , vol.18 , pp. 193-201
    • Kuwabara, P.E.1    Labouesse, M.2
  • 54
    • 0033616708 scopus 로고    scopus 로고
    • Raft association of SNAP receptors acting in apical trafficking in Madin- Darby canine kidney cells
    • Lafont, F., Verkade, P., Galli, T., Wimmer, C., Louvard, D. and Simons, K. (1999). Raft association of SNAP receptors acting in apical trafficking in Madin- Darby canine kidney cells. Proc. Natl. Acad. Sci. USA 96, 3734-3738.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3734-3738
    • Lafont, F.1    Verkade, P.2    Galli, T.3    Wimmer, C.4    Louvard, D.5    Simons, K.6
  • 55
    • 37249068200 scopus 로고    scopus 로고
    • SNARE proteins and 'membrane rafts'
    • Lang, T. (2007). SNARE proteins and 'membrane rafts'. J. Physiol. 585, 693-698.
    • (2007) J. Physiol. , vol.585 , pp. 693-698
    • Lang, T.1
  • 56
    • 80052572363 scopus 로고    scopus 로고
    • The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport
    • Laufman, O., Hong, W. and Lev, S. (2011). The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport. J. Cell Biol. 194, 459-472.
    • (2011) J. Cell Biol. , vol.194 , pp. 459-472
    • Laufman, O.1    Hong, W.2    Lev, S.3
  • 57
    • 79960698521 scopus 로고    scopus 로고
    • Mechanisms regulating hepatic SR-BI expression and their impact on HDL metabolism
    • Leiva, A., Verdejo, H., Benítez, M. L., Martínez, A., Busso, D. and Rigotti, A. (2011). Mechanisms regulating hepatic SR-BI expression and their impact on HDL metabolism. Atherosclerosis 217, 299-307.
    • (2011) Atherosclerosis , vol.217 , pp. 299-307
    • Leiva, A.1    Verdejo, H.2    Benítez, M.L.3    Martínez, A.4    Busso, D.5    Rigotti, A.6
  • 58
    • 0032504156 scopus 로고    scopus 로고
    • SNAP-23 requirement for transferrin recycling in Streptolysin-Opermeabilized Madin-Darby canine kidney cells
    • Leung, S. M., Chen, D., DasGupta, B. R., Whiteheart, S. W. and Apodaca, G. (1998). SNAP-23 requirement for transferrin recycling in Streptolysin-Opermeabilized Madin-Darby canine kidney cells. J. Biol. Chem. 273, 17732- 17741.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17732-17741
    • Leung, S.M.1    Chen, D.2    DasGupta, B.R.3    Whiteheart, S.W.4    Apodaca, G.5
  • 59
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li, H. and Papadopoulos, V. (1998). Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 139, 4991-4997.
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 60
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. and Simons, K. (2010). Lipid rafts as a membrane-organizing principle. Science 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 61
    • 31944450533 scopus 로고    scopus 로고
    • Syntaxins 3 and 4 are concentrated in separate clusters on the plasma membrane before the establishment of cell polarity
    • Low, S. H., Vasanji, A., Nanduri, J., He, M., Sharma, N., Koo, M., Drazba, J. and Weimbs, T. (2006). Syntaxins 3 and 4 are concentrated in separate clusters on the plasma membrane before the establishment of cell polarity. Mol. Biol. Cell 17, 977-989.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 977-989
    • Low, S.H.1    Vasanji, A.2    Nanduri, J.3    He, M.4    Sharma, N.5    Koo, M.6    Drazba, J.7    Weimbs, T.8
  • 66
    • 28444479505 scopus 로고    scopus 로고
    • Role of cholesterol and lipid organization in disease
    • Maxfield, F. R. and Tabas, I. (2005). Role of cholesterol and lipid organization in disease. Nature 438, 612-621.
    • (2005) Nature , vol.438 , pp. 612-621
    • Maxfield, F.R.1    Tabas, I.2
  • 67
    • 77955053533 scopus 로고    scopus 로고
    • Cholesterol, the central lipid of mammalian cells
    • Maxfield, F. R. and van Meer, G. (2010). Cholesterol, the central lipid of mammalian cells. Curr. Opin. Cell Biol. 22, 422-429.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 422-429
    • Maxfield, F.R.1    van Meer, G.2
  • 68
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
    • McMahon, H. T., Ushkaryov, Y. A., Edelmann, L., Link, E., Binz, T., Niemann, H., Jahn, R. and Südhof, T. C. (1993). Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature 364, 346-349.
    • (1993) Nature , vol.364 , pp. 346-349
    • McMahon, H.T.1    Ushkaryov, Y.A.2    Edelmann, L.3    Link, E.4    Binz, T.5    Niemann, H.6    Jahn, R.7    Südhof, T.C.8
  • 73
    • 80055016099 scopus 로고    scopus 로고
    • Molecular mechanism of cholesterol- and polyphosphoinositide-mediated syntaxin clustering
    • Murray, D. H. and Tamm, L. K. (2011). Molecular mechanism of cholesterol- and polyphosphoinositide-mediated syntaxin clustering. Biochemistry 50, 9014- 9022.
    • (2011) Biochemistry , vol.50 , pp. 9014-9022
    • Murray, D.H.1    Tamm, L.K.2
  • 74
    • 84872959202 scopus 로고    scopus 로고
    • Caveolae as plasma membrane sensors, protectors and organizers
    • Parton, R. G. and del Pozo, M. A. (2013). Caveolae as plasma membrane sensors, protectors and organizers. Nat. Rev. Mol. Cell Biol. 14, 98-112.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 98-112
    • Parton, R.G.1    del Pozo, M.A.2
  • 75
    • 0035966098 scopus 로고    scopus 로고
    • The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding
    • Peden, A. A., Park, G. Y. and Scheller, R. H. (2001). The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding. J. Biol. Chem. 276, 49183-49187.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49183-49187
    • Peden, A.A.1    Park, G.Y.2    Scheller, R.H.3
  • 76
    • 33750339742 scopus 로고    scopus 로고
    • Integrin traffic
    • Pellinen, T. and Ivaska, J. (2006). Integrin traffic. J. Cell Sci. 119, 3723-3731.
    • (2006) J. Cell Sci. , vol.119 , pp. 3723-3731
    • Pellinen, T.1    Ivaska, J.2
  • 78
    • 84871960929 scopus 로고    scopus 로고
    • The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction
    • Platt, F. M., Boland, B. and van der Spoel, A. C. (2012). The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction. J. Cell Biol. 199, 723-734.
    • (2012) J. Cell Biol. , vol.199 , pp. 723-734
    • Platt, F.M.1    Boland, B.2    van der Spoel, A.C.3
  • 79
    • 0742306892 scopus 로고    scopus 로고
    • Stimulation-dependent recycling of integrin beta1 regulated by ARF6 and Rab11
    • Powelka, A. M., Sun, J., Li, J., Gao, M., Shaw, L. M., Sonnenberg, A. and Hsu, V. W. (2004). Stimulation-dependent recycling of integrin beta1 regulated by ARF6 and Rab11. Traffic 5, 20-36.
    • (2004) Traffic , vol.5 , pp. 20-36
    • Powelka, A.M.1    Sun, J.2    Li, J.3    Gao, M.4    Shaw, L.M.5    Sonnenberg, A.6    Hsu, V.W.7
  • 80
    • 27744528461 scopus 로고    scopus 로고
    • Cholesterol-dependent syntaxin-4 and SNAP-23 clustering regulates caveolar fusion with the endothelial plasma membrane
    • Predescu, S. A., Predescu, D. N., Shimizu, K., Klein, I. K. and Malik, A. B. (2005). Cholesterol-dependent syntaxin-4 and SNAP-23 clustering regulates caveolar fusion with the endothelial plasma membrane. J. Biol. Chem. 280, 37130-37138.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37130-37138
    • Predescu, S.A.1    Predescu, D.N.2    Shimizu, K.3    Klein, I.K.4    Malik, A.B.5
  • 81
    • 0032538835 scopus 로고    scopus 로고
    • Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes
    • Prekeris, R., Klumperman, J., Chen, Y. A. and Scheller, R. H. (1998). Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. J. Cell Biol. 143, 957-971.
    • (1998) J. Cell Biol. , vol.143 , pp. 957-971
    • Prekeris, R.1    Klumperman, J.2    Chen, Y.A.3    Scheller, R.H.4
  • 83
    • 33749529365 scopus 로고    scopus 로고
    • Ternary SNARE complexes are enriched in lipid rafts during mast cell exocytosis
    • Puri, N. and Roche, P. A. (2006). Ternary SNARE complexes are enriched in lipid rafts during mast cell exocytosis. Traffic 7, 1482-1494.
    • (2006) Traffic , vol.7 , pp. 1482-1494
    • Puri, N.1    Roche, P.A.2
  • 84
    • 84877923307 scopus 로고    scopus 로고
    • Late endosomal and lysosomal trafficking during integrin-mediated cell migration and invasion: cell matrix receptors are trafficked through the late endosomal pathway in a way that dictates how cells migrate
    • Rainero, E. and Norman, J. C. (2013). Late endosomal and lysosomal trafficking during integrin-mediated cell migration and invasion: cell matrix receptors are trafficked through the late endosomal pathway in a way that dictates how cells migrate. BioEssays 35, 523-532.
    • (2013) BioEssays , vol.35 , pp. 523-532
    • Rainero, E.1    Norman, J.C.2
  • 85
    • 33847190728 scopus 로고    scopus 로고
    • Changes in cholesterol levels in the plasma membrane modulate cell signaling and regulate cell adhesion and migration on fibronectin
    • Ramprasad, O. G., Srinivas, G., Rao, K. S., Joshi, P., Thiery, J. P., Dufour, S. and Pande, G. (2007). Changes in cholesterol levels in the plasma membrane modulate cell signaling and regulate cell adhesion and migration on fibronectin. Cell Motil. Cytoskeleton 64, 199-216.
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 199-216
    • Ramprasad, O.G.1    Srinivas, G.2    Rao, K.S.3    Joshi, P.4    Thiery, J.P.5    Dufour, S.6    Pande, G.7
  • 88
    • 19544382047 scopus 로고    scopus 로고
    • Arachidonic acid allows SNARE complex formation in the presence of Munc18
    • Rickman, C. and Davletov, B. (2005). Arachidonic acid allows SNARE complex formation in the presence of Munc18. Chem. Biol. 12, 545-553.
    • (2005) Chem. Biol. , vol.12 , pp. 545-553
    • Rickman, C.1    Davletov, B.2
  • 89
    • 84869110440 scopus 로고    scopus 로고
    • Regulation of integrin endocytic recycling and chemotactic cell migration by syntaxin 6 and VAMP3 interaction
    • Riggs, K. A., Hasan, N., Humphrey, D., Raleigh, C., Nevitt, C., Corbin, D. and Hu, C. (2012). Regulation of integrin endocytic recycling and chemotactic cell migration by syntaxin 6 and VAMP3 interaction. J. Cell Sci. 125, 3827-3839.
    • (2012) J. Cell Sci. , vol.125 , pp. 3827-3839
    • Riggs, K.A.1    Hasan, N.2    Humphrey, D.3    Raleigh, C.4    Nevitt, C.5    Corbin, D.6    Hu, C.7
  • 90
    • 84911472010 scopus 로고    scopus 로고
    • ER contact sites define the position and timing of endosome fission
    • Rowland, A. A., Chitwood, P. J., Phillips, M. J. and Voeltz, G. K. (2014). ER contact sites define the position and timing of endosome fission. Cell 159, 1027-1041.
    • (2014) Cell , vol.159 , pp. 1027-1041
    • Rowland, A.A.1    Chitwood, P.J.2    Phillips, M.J.3    Voeltz, G.K.4
  • 91
    • 12544252686 scopus 로고    scopus 로고
    • The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells. Regulation by distinct cysteine-rich domains
    • Salaün, C., Gould, G. W. and Chamberlain, L. H. (2005). The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells. Regulation by distinct cysteine-rich domains. J. Biol. Chem. 280, 1236-1240.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1236-1240
    • Salaün, C.1    Gould, G.W.2    Chamberlain, L.H.3
  • 92
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe, H. J., Stevens, T. J. and Munro, S. (2010). A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 142, 158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 93
    • 33646202286 scopus 로고    scopus 로고
    • The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane
    • Sieber, J. J., Willig, K. I., Heintzmann, R., Hell, S. W. and Lang, T. (2006). The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane. Biophys. J. 90, 2843-2851.
    • (2006) Biophys. J. , vol.90 , pp. 2843-2851
    • Sieber, J.J.1    Willig, K.I.2    Heintzmann, R.3    Hell, S.W.4    Lang, T.5
  • 95
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons, K. and Ikonen, E. (2000). How cells handle cholesterol. Science 290, 1721-1726.
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 96
    • 0033559983 scopus 로고    scopus 로고
    • SNAP-23 participates in SNARE complex assembly in rat adipose cells
    • St-Denis, J. F., Cabaniols, J. P., Cushman, S. W. and Roche, P. A. (1999). SNAP-23 participates in SNARE complex assembly in rat adipose cells. Biochem. J. 338, 709-715.
    • (1999) Biochem. J. , vol.338 , pp. 709-715
    • St-Denis, J.F.1    Cabaniols, J.P.2    Cushman, S.W.3    Roche, P.A.4
  • 98
    • 0038694994 scopus 로고    scopus 로고
    • Snorkeling of lysine side chains in transmembrane helices: how easy can it get?
    • Strandberg, E. and Killian, J. A. (2003). Snorkeling of lysine side chains in transmembrane helices: how easy can it get? FEBS Lett. 544, 69-73.
    • (2003) FEBS Lett. , vol.544 , pp. 69-73
    • Strandberg, E.1    Killian, J.A.2
  • 100
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: grappling with SNARE and SM proteins
    • Südhof, T. C. and Rothman, J. E. (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
  • 101
    • 80054683948 scopus 로고    scopus 로고
    • Endothelial cell migration on fibronectin is regulated by syntaxin 6-mediated alpha5beta1 integrin recycling
    • Tiwari, A., Jung, J. J., Inamdar, S. M., Brown, C. O., Goel, A. and Choudhury, A. (2011). Endothelial cell migration on fibronectin is regulated by syntaxin 6-mediated alpha5beta1 integrin recycling. J. Biol. Chem. 286, 36749- 36761.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36749-36761
    • Tiwari, A.1    Jung, J.J.2    Inamdar, S.M.3    Brown, C.O.4    Goel, A.5    Choudhury, A.6
  • 102
    • 65249144553 scopus 로고    scopus 로고
    • A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol
    • Tong, J., Borbat, P. P., Freed, J. H. and Shin, Y. K. (2009). A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol. Proc. Natl. Acad. Sci. USA 106, 5141-5146.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5141-5146
    • Tong, J.1    Borbat, P.P.2    Freed, J.H.3    Shin, Y.K.4
  • 104
    • 77958020672 scopus 로고    scopus 로고
    • Endosomalsorting complexes required for transport (ESCRT) pathway-dependent endosomal traffic regulates the localization of active Src at focal adhesions
    • Tu, C., Ortega-Cava, C. F., Winograd, P., Stanton, M. J., Reddi, A. L., Dodge, I., Arya, R., Dimri, M., Clubb, R. J., Naramura, M. et al. (2010). Endosomalsorting complexes required for transport (ESCRT) pathway-dependent endosomal traffic regulates the localization of active Src at focal adhesions. Proc. Natl. Acad. Sci. USA 107, 16107-16112.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16107-16112
    • Tu, C.1    Ortega-Cava, C.F.2    Winograd, P.3    Stanton, M.J.4    Reddi, A.L.5    Dodge, I.6    Arya, R.7    Dimri, M.8    Clubb, R.J.9    Naramura, M.10
  • 105
    • 55949126769 scopus 로고    scopus 로고
    • Transport of LDL-derived cholesterol from the NPC1 compartment to the ER involves the trans-Golgi network and the SNARE protein complex
    • Urano, Y., Watanabe, H., Murphy, S. R., Shibuya, Y., Geng, Y., Peden, A. A., Chang, C. C. and Chang, T. Y. (2008). Transport of LDL-derived cholesterol from the NPC1 compartment to the ER involves the trans-Golgi network and the SNARE protein complex. Proc. Natl. Acad. Sci. USA 105, 16513-16518.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16513-16518
    • Urano, Y.1    Watanabe, H.2    Murphy, S.R.3    Shibuya, Y.4    Geng, Y.5    Peden, A.A.6    Chang, C.C.7    Chang, T.Y.8
  • 106
    • 84887169831 scopus 로고    scopus 로고
    • Microdomains of SNARE proteins in the plasma membrane
    • van den Bogaart, G., Lang, T. and Jahn, R. (2013). Microdomains of SNARE proteins in the plasma membrane. Curr. Top Membr. 72, 193-230.
    • (2013) Curr. Top Membr. , vol.72 , pp. 193-230
    • van den Bogaart, G.1    Lang, T.2    Jahn, R.3
  • 107
    • 84896819965 scopus 로고    scopus 로고
    • Small regulators, major consequences - Ca2+ and cholesterol at the endosome-ER interface
    • van der Kant, R. and Neefjes, J. (2014). Small regulators, major consequences - Ca2+ and cholesterol at the endosome-ER interface. J. Cell Sci. 127, 929- 938.
    • (2014) J. Cell Sci. , vol.127 , pp. 929-938
    • van der Kant, R.1    Neefjes, J.2
  • 108
    • 84905033032 scopus 로고    scopus 로고
    • Niemann-Pick C Disease and mobilization of lysosomal cholesterol by cyclodextrin
    • Vance, J. E. and Karten, B. (2014). Niemann-Pick C Disease and mobilization of lysosomal cholesterol by cyclodextrin. J. Lipid Res. 55, 1609-1621.
    • (2014) J. Lipid Res. , vol.55 , pp. 1609-1621
    • Vance, J.E.1    Karten, B.2
  • 109
    • 0034577510 scopus 로고    scopus 로고
    • Cholesterol is required for the formation of regulated and constitutive secretory vesicles from the trans-Golgi network
    • Wang, Y., Thiele, C. and Huttner, W. B. (2000). Cholesterol is required for the formation of regulated and constitutive secretory vesicles from the trans-Golgi network. Traffic 1, 952-962.
    • (2000) Traffic , vol.1 , pp. 952-962
    • Wang, Y.1    Thiele, C.2    Huttner, W.B.3
  • 110
    • 78649916808 scopus 로고    scopus 로고
    • Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes
    • Wang, M. L., Motamed, M., Infante, R. E., Abi-Mosleh, L., Kwon, H. J., Brown, M. S. and Goldstein, J. L. (2010). Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes. Cell Metab. 12, 166-173.
    • (2010) Cell Metab. , vol.12 , pp. 166-173
    • Wang, M.L.1    Motamed, M.2    Infante, R.E.3    Abi-Mosleh, L.4    Kwon, H.J.5    Brown, M.S.6    Goldstein, J.L.7
  • 111
    • 0033963378 scopus 로고    scopus 로고
    • Functional cooperation of two independent targeting domains in syntaxin 6 is required for its efficient localization in the trans-golgi network of 3T3L1 adipocytes
    • Watson, R. T. and Pessin, J. E. (2000). Functional cooperation of two independent targeting domains in syntaxin 6 is required for its efficient localization in the trans-golgi network of 3T3L1 adipocytes. J. Biol. Chem. 275, 1261-1268.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1261-1268
    • Watson, R.T.1    Pessin, J.E.2
  • 112
    • 0034839484 scopus 로고    scopus 로고
    • Syntaxin 6: the promiscuous behaviour of a SNARE protein
    • Wendler, F. and Tooze, S. (2001). Syntaxin 6: the promiscuous behaviour of a SNARE protein. Traffic 2, 606-611.
    • (2001) Traffic , vol.2 , pp. 606-611
    • Wendler, F.1    Tooze, S.2
  • 113
    • 84898847399 scopus 로고    scopus 로고
    • SNARE-dependent interaction of Src, EGFR and b1 integrin regulates invadopodia formation and tumor cell invasion
    • Williams, K. C. and Coppolino, M. G. (2014). SNARE-dependent interaction of Src, EGFR and b1 integrin regulates invadopodia formation and tumor cell invasion. J. Cell Sci. 127, 1712-1725.
    • (2014) J. Cell Sci. , vol.127 , pp. 1712-1725
    • Williams, K.C.1    Coppolino, M.G.2
  • 114
    • 84903537714 scopus 로고    scopus 로고
    • SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) mediate trafficking of membrane type 1-matrix metalloproteinase (MT1-MMP) during invadopodium formation and tumor cell invasion
    • Williams, K. C., McNeilly, R. E. and Coppolino, M. G. (2014). SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) mediate trafficking of membrane type 1-matrix metalloproteinase (MT1-MMP) during invadopodium formation and tumor cell invasion. Mol. Biol. Cell 25, 2061-2070.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 2061-2070
    • Williams, K.C.1    McNeilly, R.E.2    Coppolino, M.G.3
  • 115
    • 33744949741 scopus 로고    scopus 로고
    • Domain requirement for the membrane trafficking and targeting of syntaxin 1A
    • Yang, X., Xu, P., Xiao, Y., Xiong, X. and Xu, T. (2006). Domain requirement for the membrane trafficking and targeting of syntaxin 1A. J. Biol. Chem. 281, 15457-15463.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15457-15463
    • Yang, X.1    Xu, P.2    Xiao, Y.3    Xiong, X.4    Xu, T.5
  • 117
    • 79953802832 scopus 로고    scopus 로고
    • Ca2+ induces clustering of membrane proteins in the plasma membrane via electrostatic interactions
    • Zilly, F. E., Halemani, N. D., Walrafen, D., Spitta, L., Schreiber, A., Jahn, R. and Lang, T. (2011). Ca2+ induces clustering of membrane proteins in the plasma membrane via electrostatic interactions. EMBO J. 30, 1209-1220.
    • (2011) EMBO J. , vol.30 , pp. 1209-1220
    • Zilly, F.E.1    Halemani, N.D.2    Walrafen, D.3    Spitta, L.4    Schreiber, A.5    Jahn, R.6    Lang, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.