메뉴 건너뛰기




Volumn 8, Issue 10, 2002, Pages 1059-1062

The machinery and principles of vesicle transport in the cell

Author keywords

[No Author keywords available]

Indexed keywords

SNARE PROTEIN; MEMBRANE PROTEIN; VESICULAR TRANSPORT PROTEIN;

EID: 0036780223     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm770     Document Type: Note
Times cited : (127)

References (23)
  • 1
    • 0000930533 scopus 로고
    • Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport
    • Block, M., Glick, B., Wilcox, C., Wieland, F. & Rothman, J.E. Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport. Proc. Natl. Acad. Sci. USA 85, 7852-7856 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7852-7856
    • Block, M.1    Glick, B.2    Wilcox, C.3    Wieland, F.4    Rothman, J.E.5
  • 2
    • 0024342254 scopus 로고
    • A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast
    • Wilson, D.W. et al. A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast. Nature 339, 355-359 (1989).
    • (1989) Nature , vol.339 , pp. 355-359
    • Wilson, D.W.1
  • 3
    • 0009355284 scopus 로고
    • Transport of vesicular stomatitis virus glycoprotein in a cell-free extract
    • Fries, E. & Rothman, J.E. Transport of vesicular stomatitis virus glycoprotein in a cell-free extract. Proc. Natl. Acad. Sci. USA 77, 3870-3874 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3870-3874
    • Fries, E.1    Rothman, J.E.2
  • 4
    • 0019866089 scopus 로고
    • Transient activity of Golgi-like membranes as donors of vesicular stomatitis viral glycoprotein in vitro
    • Fries, E. & Rothman, J.E. Transient activity of Golgi-like membranes as donors of vesicular stomatitis viral glycoprotein in vitro. J. Cell Biol. 90, 697-704 (1981).
    • (1981) J. Cell Biol. , vol.90 , pp. 697-704
    • Fries, E.1    Rothman, J.E.2
  • 5
    • 0021738607 scopus 로고
    • Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine
    • Balch, W., Dunphy, W., Braell, W. & Rothman, J.E. Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell 39, 405-416 (1984).
    • (1984) Cell , vol.39 , pp. 405-416
    • Balch, W.1    Dunphy, W.2    Braell, W.3    Rothman, J.E.4
  • 6
    • 0021713454 scopus 로고
    • The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae
    • Braell, W., Balch, W., Dobbertin, D. & Rothman, J.E. The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae. Cell 39, 511-524 (1984).
    • (1984) Cell , vol.39 , pp. 511-524
    • Braell, W.1    Balch, W.2    Dobbertin, D.3    Rothman, J.E.4
  • 7
    • 0021741764 scopus 로고
    • Sequential intermediates in the pathway of intercompartmental transport in a cell-free system
    • Balch, W., Glick, B. & Rothman, J.E. Sequential intermediates in the pathway of intercompartmental transport in a cell-free system. Cell 39, 525-536 (1984).
    • (1984) Cell , vol.39 , pp. 525-536
    • Balch, W.1    Glick, B.2    Rothman, J.E.3
  • 8
    • 0023052287 scopus 로고
    • A new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stack
    • Orci, L., Glick, B.S. & Rothman, J.E. A new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stack. Cell 46, 171-184 (1986).
    • (1986) Cell , vol.46 , pp. 171-184
    • Orci, L.1    Glick, B.S.2    Rothman, J.E.3
  • 9
    • 0023663869 scopus 로고
    • Involvement of GTP-binding "G" proteins in transport through the Golgi stack
    • Melançon, P. et al. Involvement of GTP-binding "G" proteins in transport through the Golgi stack. Cell 51, 1053-1062 (1987).
    • (1987) Cell , vol.51 , pp. 1053-1062
    • Melançon, P.1
  • 10
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack
    • Malhotra, V., Serafini, T., Orci, L., Shepherd, J.C. & Rothman, J.E. Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack. Cell 58, 329-336 (1989).
    • (1989) Cell , vol.58 , pp. 329-336
    • Malhotra, V.1    Serafini, T.2    Orci, L.3    Shepherd, J.C.4    Rothman, J.E.5
  • 11
    • 0025957468 scopus 로고
    • 'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters, M., Serafini, T. & Rothman, J.E. 'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349, 248-251 (1991).
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.1    Serafini, T.2    Rothman, J.E.3
  • 12
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini, T. et al. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67, 239-253 (1991).
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1
  • 13
    • 0027291429 scopus 로고
    • Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • Orci, L., Palmer, D.J., Amherdt, M. & Rothman J.E. Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature 364, 732-734 (1993).
    • (1993) Nature , vol.364 , pp. 732-734
    • Orci, L.1    Palmer, D.J.2    Amherdt, M.3    Rothman, J.E.4
  • 14
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes, M.A. & Rothman, J.E. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell 73, 999-1005 (1993).
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 15
    • 0028233498 scopus 로고
    • COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • Barlowe, C. et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895-907 (1994).
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1
  • 16
    • 0025359065 scopus 로고
    • SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • Clary, D.O., Griff, I.C. & Rothman, J.E. SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell 61, 709-721 (1990).
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.O.1    Griff, I.C.2    Rothman, J.E.3
  • 17
    • 0023707176 scopus 로고
    • Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack
    • Malhotra, V., Orci, L., Glick, B., Block, M. & Rothman, J.E. Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack. Cell 54, 221-227 (1988).
    • (1988) Cell , vol.54 , pp. 221-227
    • Malhotra, V.1    Orci, L.2    Glick, B.3    Block, M.4    Rothman, J.E.5
  • 18
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Söllner T.H. et al. SNAP receptors implicated in vesicle targeting and fusion. Nature 362, 318-324 (1993).
    • (1993) Nature , vol.362 , pp. 318-324
    • Söllner, T.H.1
  • 19
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton, R.B., Fasshauer, D., Jahn, R. & Brunger, A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395, 347-353 (1998).
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 20
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber, T. et al. SNAREpins: minimal machinery for membrane fusion. Cell 92, 759-772 (1998).
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1
  • 21
    • 0034648836 scopus 로고    scopus 로고
    • Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
    • McNew, J. et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature 407, 153-159 (2000).
    • (2000) Nature , vol.407 , pp. 153-159
    • McNew, J.1
  • 22
    • 0037117610 scopus 로고    scopus 로고
    • Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity
    • Parlati, F. et al. Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity. Proc. Natl. Acad. Sci. USA 99, 5424-5429 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5424-5429
    • Parlati, F.1
  • 23
    • 0037067649 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
    • Gagnon, R. et al. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell 110, 119-131 (2002).
    • (2002) Cell , vol.110 , pp. 119-131
    • Gagnon, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.