메뉴 건너뛰기




Volumn 429, Issue 2, 2010, Pages 391-401

The identification of the SNARE complex required for the fusion of VLDL-transport vesicle with hepatic cis-Golgi

Author keywords

Apolipoprotein B (apoB); Endoplasmic reticulum (ER); Sec22b; Triacylglycerol (TAG); Very low density lipoprotein transport vesicle (VTV)

Indexed keywords

APOLIPOPROTEIN B (APOB); BIOCHEMICAL COMPOSITION; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; IN-VITRO; LOW DENSITY LIPOPROTEINS; PRE-TREATMENT; PROTEIN RECEPTORS; SYNTAXIN; TARGETED DELIVERY; TRIACYLGLYCEROLS; TRITON X-100;

EID: 77954735698     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100336     Document Type: Article
Times cited : (36)

References (51)
  • 1
    • 0032927776 scopus 로고    scopus 로고
    • Apolipoprotein B in the rough endoplasmic reticulum: Translation, translocation and the initiation of lipoprotein assembly
    • Shelness, G. S., Ingram, M. F., Huang, X. F. and DeLozier, J. A. (1999) Apolipoprotein B in the rough endoplasmic reticulum: translation, translocation and the initiation of lipoprotein assembly. J. Nutr. 129, 456S-462S
    • (1999) J. Nutr. , vol.129
    • Shelness, G.S.1    Ingram, M.F.2    Huang, X.F.3    DeLozier, J.A.4
  • 3
    • 0034712665 scopus 로고    scopus 로고
    • Decreased secretion of ApoB follows inhibition of ApoB-MTP binding by a novel antagonist
    • Bakillah, A., Nayak, N., Saxena, U., Medford, R. M. and Hussain, M. M. (2000) Decreased secretion of ApoB follows inhibition of ApoB-MTP binding by a novel antagonist. Biochemistry 39, 4892-4899
    • (2000) Biochemistry , vol.39 , pp. 4892-4899
    • Bakillah, A.1    Nayak, N.2    Saxena, U.3    Medford, R.M.4    Hussain, M.M.5
  • 4
    • 20544462893 scopus 로고    scopus 로고
    • Evolution and mechanism of apolipoprotein B-containing lipoprotein assembly
    • Shelness, G. S. and Ledford, A. S. (2005) Evolution and mechanism of apolipoprotein B-containing lipoprotein assembly. Curr. Opin. Lipidol. 16, 325-332
    • (2005) Curr. Opin. Lipidol. , vol.16 , pp. 325-332
    • Shelness, G.S.1    Ledford, A.S.2
  • 5
    • 0032861798 scopus 로고    scopus 로고
    • The assembly and secretion of apolipoprotein B-containing lipoproteins
    • Olofsson, S. O., Asp, L. and Boren, J. (1999) The assembly and secretion of apolipoprotein B-containing lipoproteins. Curr. Opin. Lipidol. 10, 341-346
    • (1999) Curr. Opin. Lipidol. , vol.10 , pp. 341-346
    • Olofsson, S.O.1    Asp, L.2    Boren, J.3
  • 6
    • 0023646009 scopus 로고
    • Intrahepatic assembly of very low density lipoproteins: Rate of transport out of the endoplasmic reticulum determines rate of secretion
    • Borchardt, R. A. and Davis, R. A. (1987) Intrahepatic assembly of very low density lipoproteins: rate of transport out of the endoplasmic reticulum determines rate of secretion. J. Biol. Chem. 262, 16394-16402
    • (1987) J. Biol. Chem. , vol.262 , pp. 16394-16402
    • Borchardt, R.A.1    Davis, R.A.2
  • 7
    • 0027535128 scopus 로고
    • Assembly of rat hepatic very low density lipoproteins in the endoplasmic reticulum
    • Rusinol, A., Verkade, H. and Vance, J. E. (1993) Assembly of rat hepatic very low density lipoproteins in the endoplasmic reticulum. J. Biol. Chem. 268, 3555-3562
    • (1993) J. Biol. Chem. , vol.268 , pp. 3555-3562
    • Rusinol, A.1    Verkade, H.2    Vance, J.E.3
  • 8
    • 0037163096 scopus 로고    scopus 로고
    • Intracellular assembly of very low density lipoproteins containing apolipoprotein B100 in rat hepatoma McA-RH7777 cells
    • Tran, K., Thorne-Tjomsland, G., DeLong, C. J., Cui, Z., Shan, J., Burton, L., Jamieson, J. C. and Yao, Z. (2002) Intracellular assembly of very low density lipoproteins containing apolipoprotein B100 in rat hepatoma McA-RH7777 cells. J. Biol. Chem. 277, 31187-31200
    • (2002) J. Biol. Chem. , vol.277 , pp. 31187-31200
    • Tran, K.1    Thorne-Tjomsland, G.2    DeLong, C.J.3    Cui, Z.4    Shan, J.5    Burton, L.6    Jamieson, J.C.7    Yao, Z.8
  • 9
    • 0029033102 scopus 로고
    • Synthesis and secretion of apolipoprotein B from cultured liver cells
    • Ginsberg, H. N. (1995) Synthesis and secretion of apolipoprotein B from cultured liver cells. Curr. Opin. Lipidol. 6, 275-280
    • (1995) Curr. Opin. Lipidol. , vol.6 , pp. 275-280
    • Ginsberg, H.N.1
  • 10
    • 34547101495 scopus 로고    scopus 로고
    • Golgi-associated maturation of very low density lipoproteins involves conformational changes in apolipoprotein B, but is not dependent on apolipoprotein E
    • Gusarova, V., Seo, J., Sullivan, M. L., Watkins, S. C., Brodsky, J. L. and Fisher, E. A. (2007) Golgi-associated maturation of very low density lipoproteins involves conformational changes in apolipoprotein B, but is not dependent on apolipoprotein E. J. Biol. Chem. 282, 19453-19462
    • (2007) J. Biol. Chem. , vol.282 , pp. 19453-19462
    • Gusarova, V.1    Seo, J.2    Sullivan, M.L.3    Watkins, S.C.4    Brodsky, J.L.5    Fisher, E.A.6
  • 11
    • 0031443539 scopus 로고    scopus 로고
    • Conformational changes in apolipoprotein B modulate intracellular assembly and degradation of Apo B containing lipoprotein particles in HepG2 cells
    • Macri, J. and Adeli, K. (1997) Conformational changes in apolipoprotein B modulate intracellular assembly and degradation of Apo B containing lipoprotein particles in HepG2 cells. Arterioscler. Thromb. Vasc. Biol. 17, 2982-2994
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 2982-2994
    • Macri, J.1    Adeli, K.2
  • 12
    • 0025319210 scopus 로고
    • Possible role of the Golgi apparatus in the assembly of very low density lipoprotein
    • Bamberger, M. J. and Lane, M. D. (1990) Possible role of the Golgi apparatus in the assembly of very low density lipoprotein. Proc. Natl. Acad. Sci. U.S.A. 87, 2390-2394
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2390-2394
    • Bamberger, M.J.1    Lane, M.D.2
  • 13
    • 0024295210 scopus 로고
    • Evidence that during very low density lipoprotein assembly in rat hepatocytes most of the triacylglycerol and phospholipid are packaged with apolipoprotein B in the Golgi complex
    • Higgins, J. A. (1988) Evidence that during very low density lipoprotein assembly in rat hepatocytes most of the triacylglycerol and phospholipid are packaged with apolipoprotein B in the Golgi complex. FEBS Lett. 232, 405-408
    • (1988) FEBS Lett. , vol.232 , pp. 405-408
    • Higgins, J.A.1
  • 14
    • 0032516855 scopus 로고    scopus 로고
    • COPII and selective export from the endoplasmic reticulum
    • Barlowe, C. (1998) COPII and selective export from the endoplasmic reticulum. Biochim. Biophys. Acta 1404, 67-76
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 67-76
    • Barlowe, C.1
  • 16
    • 39149086740 scopus 로고    scopus 로고
    • Assembly, organization, and function of the COPII coat
    • Hughes, H. and and Stephens, D. J. (2008) Assembly, organization, and function of the COPII coat. Histochem. Cell Biol. 129, 129-151
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 129-151
    • Hughes, H.1    Stephens, D.J.2
  • 17
    • 20544451051 scopus 로고    scopus 로고
    • COPII and exit from the endoplasmic reticulum
    • Tang, B. L., Wang, Y., Ong, Y. S. and Hong, W. (2005) COPII and exit from the endoplasmic reticulum. Biochim. Biophys. Acta 1744, 293-303
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 293-303
    • Tang, B.L.1    Wang, Y.2    Ong, Y.S.3    Hong, W.4
  • 18
    • 34248176797 scopus 로고    scopus 로고
    • Mechanisms of COPII vesicle formation and protein sorting
    • Sato, K. and Nakano, A. (2007) Mechanisms of COPII vesicle formation and protein sorting. FEBS Lett. 581, 2076-2082
    • (2007) FEBS Lett. , vol.581 , pp. 2076-2082
    • Sato, K.1    Nakano, A.2
  • 20
    • 46049089793 scopus 로고    scopus 로고
    • Coordination of COPII vesicle trafficking by Sec23
    • Fromme, J. C., Orci, L. and Schekman, R. (2008) Coordination of COPII vesicle trafficking by Sec23. Trends Cell Biol. 18, 330-336
    • (2008) Trends Cell Biol. , vol.18 , pp. 330-336
    • Fromme, J.C.1    Orci, L.2    Schekman, R.3
  • 21
    • 48149087127 scopus 로고    scopus 로고
    • VLDL exits from the endoplasmic reticulum in a specialized vesicle, the VLDL transport vesicle, in rat primary hepatocytes
    • Siddiqi, S. A. (2008) VLDL exits from the endoplasmic reticulum in a specialized vesicle, the VLDL transport vesicle, in rat primary hepatocytes. Biochem. J. 413, 333-342
    • (2008) Biochem. J. , vol.413 , pp. 333-342
    • Siddiqi, S.A.1
  • 22
    • 0346220266 scopus 로고    scopus 로고
    • Apolipoprotein B100 exit from the endoplasmic reticulum (ER) is COPII-dependent, and its lipidation to very low density lipoprotein occurs post-ER
    • Gusarova, V., Brodsky, J. L. and Fisher, E. A. (2003) Apolipoprotein B100 exit from the endoplasmic reticulum (ER) is COPII-dependent, and its lipidation to very low density lipoprotein occurs post-ER. J. Biol. Chem. 278, 48051-48058
    • (2003) J. Biol. Chem. , vol.278 , pp. 48051-48058
    • Gusarova, V.1    Brodsky, J.L.2    Fisher, E.A.3
  • 24
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay, J. C. and Scheller, R. H. (1997) SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9, 505-512
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 26
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • Sudhof, 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
    • Sudhof, T.C.1    Rothman, J.E.2
  • 27
    • 34548515059 scopus 로고    scopus 로고
    • An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system
    • Kloepper, T. H., Kienle, C. N. and Fasshauer, D. (2007) An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system. Mol. Biol. Cell 18, 3463-3471
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3463-3471
    • Kloepper, T.H.1    Kienle, C.N.2    Fasshauer, D.3
  • 28
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T. and Jahn, R. (1998) Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. U.S.A. 95, 15781-15786
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 30
    • 33746363860 scopus 로고    scopus 로고
    • The identification of a novel endoplasmic reticulum to Golgi SNARE complex used by the prechylomicron transport vesicle
    • Siddiqi, S. A., Siddiqi, S., Mahan, J., Peggs, K., Gorelick, F. S. and Mansbach, II, C. M. (2006) The identification of a novel endoplasmic reticulum to Golgi SNARE complex used by the prechylomicron transport vesicle. J. Biol. Chem. 281, 20974-20982
    • (2006) J. Biol. Chem. , vol.281 , pp. 20974-20982
    • Siddiqi, S.A.1    Siddiqi, S.2    Mahan, J.3    Peggs, K.4    Gorelick, F.S.5    Mansbach II, C.M.6
  • 32
    • 0030857961 scopus 로고    scopus 로고
    • Determinants of triacylglycerol transport from the endoplasmic reticulum to the Golgi in intestine
    • Kumar, N. S. and Mansbach, II, C. M. (1997) Determinants of triacylglycerol transport from the endoplasmic reticulum to the Golgi in intestine. Am. J. Physiol. 273, G18-G30
    • (1997) Am. J. Physiol. , vol.273
    • Kumar, N.S.1    Mansbach II, C.M.2
  • 33
    • 0037439881 scopus 로고    scopus 로고
    • COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle
    • Siddiqi, S. A., Gorelick, F. S., Mahan, J. T. and Mansbach, II, C. M. (2003) COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle. J. Cell Sci. 116, 415-427
    • (2003) J. Cell Sci. , vol.116 , pp. 415-427
    • Siddiqi, S.A.1    Gorelick, F.S.2    Mahan, J.T.3    Mansbach II, C.M.4
  • 34
    • 68049114749 scopus 로고    scopus 로고
    • Proteomic profiling of the prechylomicron transport vesicle involved in the assembly and secretion of apoB-48 containing chylomicrons in the intestinal enterocytes
    • Wong, D. M., Webb, J. P., Malinowski, P. M., Macri, J. and Adeli, K. (2009) Proteomic profiling of the prechylomicron transport vesicle involved in the assembly and secretion of apoB-48 containing chylomicrons in the intestinal enterocytes. Proteomics 9, 3698-3711
    • (2009) Proteomics , vol.9 , pp. 3698-3711
    • Wong, D.M.1    Webb, J.P.2    Malinowski, P.M.3    Macri, J.4    Adeli, K.5
  • 35
    • 34547114033 scopus 로고    scopus 로고
    • Liver fatty acid-binding protein initiates budding of pre-chylomicron transport vesicles from intestinal endoplasmic reticulum
    • Neeli, I., Siddiqi, S. A., Siddiqi, S., Mahan, J., Lagakos, W. S., Binas, B., Gheyi, T., Storch, J. and Mansbach, II, C. M. (2007) Liver fatty acid-binding protein initiates budding of pre-chylomicron transport vesicles from intestinal endoplasmic reticulum. J. Biol. Chem. 282, 17974-17984
    • (2007) J. Biol. Chem. , vol.282 , pp. 17974-17984
    • Neeli, I.1    Siddiqi, S.A.2    Siddiqi, S.3    Mahan, J.4    Lagakos, W.S.5    Binas, B.6    Gheyi, T.7    Storch, J.8    Mansbach II, C.M.9
  • 36
    • 49649118045 scopus 로고    scopus 로고
    • PKCζ -mediated phosphorylation controls budding of the prechylomicron transport vesicle
    • Siddiqi, S. A. and Mansbach, II, C. M. (2008) PKCζ -mediated phosphorylation controls budding of the prechylomicron transport vesicle. J. Cell Sci. 121, 2327-2338
    • (2008) J. Cell Sci. , vol.121 , pp. 2327-2338
    • Siddiqi, S.A.1    Mansbach II, C.M.2
  • 37
    • 77951057045 scopus 로고    scopus 로고
    • Sec24C is required for the docking of the prechylomicron transport vesicle with the Golgi
    • Siddiqi, S., Siddiqi, S. A. and and Mansbach, II, C. M. (2009) Sec24C is required for the docking of the prechylomicron transport vesicle with the Golgi. J. Lipid Res. 51, 1093-1100
    • (2009) J. Lipid Res. , vol.51 , pp. 1093-1100
    • Siddiqi, S.1    Siddiqi, S.A.2    Mansbach II, C.M.3
  • 38
    • 0034695915 scopus 로고    scopus 로고
    • Live Salmonella recruits N-ethylmaleimide sensitive fusion protein on phagosomal membrane and promotes fusion with early endosome
    • Mukherjee, K., Siddiqi, S. A., Hashim, S., Raje, M., Basu, S. K. and Mukhopadhyay, A. (2000) Live Salmonella recruits N-ethylmaleimide sensitive fusion protein on phagosomal membrane and promotes fusion with early endosome. J. Cell Biol. 148, 741-753
    • (2000) J. Cell Biol. , vol.148 , pp. 741-753
    • Mukherjee, K.1    Siddiqi, S.A.2    Hashim, S.3    Raje, M.4    Basu, S.K.5    Mukhopadhyay, A.6
  • 39
    • 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. and 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, 27480-27487
    • (2001) J. Biol. Chem. , vol.276 , pp. 27480-27487
    • Zhang, T.1    Hong, W.2
  • 40
    • 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. and Hong, W. (1999) Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment. Mol. Biol. Cell 10, 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
  • 41
    • 0030890594 scopus 로고    scopus 로고
    • Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
    • Hay, J. C., Chao, D. S., Kuo, C. S. and Scheller, R. H. (1997) Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Cell 89, 149-158 (Pubitemid 27180594)
    • (1997) Cell , vol.89 , Issue.1 , pp. 149-158
    • Hay, J.C.1    Chao, D.S.2    Kuo, C.S.3    Scheller, R.H.4
  • 44
    • 0028143698 scopus 로고
    • Mechanism of intracellular transport
    • Rothman, J. E. (1994) Mechanism of intracellular transport. Nature 372, 55-63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 46
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner, T., Bennett, M. K., Whiteheart, S., Scheller, R. H. and Rothman, J. E. (1993) A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.3    Scheller, R.H.4    Rothman, J.E.5
  • 47
    • 0025374891 scopus 로고
    • The multisubunit structure of synaptophysin: Relationship between disulfide bonding and homo-oligomerization
    • Johnson, P. A. and Sudhof, T. C. (1990) The multisubunit structure of synaptophysin: relationship between disulfide bonding and homo-oligomerization. J. Biol. Chem. 265, 8869-8873
    • (1990) J. Biol. Chem. , vol.265 , pp. 8869-8873
    • Johnson, P.A.1    Sudhof, T.C.2
  • 49
    • 0037077295 scopus 로고    scopus 로고
    • A proteomic approach identifies proteins in hepatocytes that bind nascent apolipoproteins B
    • Rashid, K. A., Hevi, S., Chen, Y., Le Caherec, F. and Chuck, S. L. (2002) A proteomic approach identifies proteins in hepatocytes that bind nascent apolipoproteins B. J. Biol. Chem. 277, 22010-22017
    • (2002) J. Biol. Chem. , vol.277 , pp. 22010-22017
    • Rashid, K.A.1    Hevi, S.2    Chen, Y.3    Le Caherec, F.4    Chuck, S.L.5
  • 50
    • 0034671727 scopus 로고    scopus 로고
    • Subunit structure of a mammalian ER/Golgi SNARE complex
    • Xu, D., Joglekar, A. P., Williams, A. L. and Hay, J. C. (2000) Subunit structure of a mammalian ER/Golgi SNARE complex. J. Biol. Chem. 275, 39631-39639
    • (2000) J. Biol. Chem. , vol.275 , pp. 39631-39639
    • Xu, D.1    Joglekar, A.P.2    Williams, A.L.3    Hay, J.C.4
  • 51
    • 0037323502 scopus 로고    scopus 로고
    • Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain
    • Hasegawa, H., Zinsser, S., Rhee, Y., Vik-Mo, E. O., Davanger, S. and Hay, J. C. (2003) Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain. Mol. Biol. Cell 14, 698-720
    • (2003) Mol. Biol. Cell , vol.14 , pp. 698-720
    • Hasegawa, H.1    Zinsser, S.2    Rhee, Y.3    Vik-Mo, E.O.4    Davanger, S.5    Hay, J.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.