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MeSH Review

COP-Coated Vesicles

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High impact information on COP-Coated Vesicles

  • It is inferred that, in vivo, sorting signal selection is under kinetic control, with coatomer governing a GTPase discard pathway that excludes dilysine-tagged proteins from one class of COPI-coated vesicles [1].
  • In the complex, the effector-binding region appears to be unobstructed, suggesting that ARFGAP could stimulate GTP hydrolysis while ARF1 maintains an interaction with its effector, the coatomer complex of COPI-coated vesicles [2].
  • Liposome-derived COPI-coated vesicles are similar to their native counterparts with respect to diameter, buoyant density, morphology, and the requirement for an elevated temperature for budding [3].
  • Budding of COP-coated vesicles (the likely carriers of newly synthesized proteins from the endoplasmic reticulum through the Golgi stack) from Golgi cisternae requires ADP-ribosylation factor (ARF), coatomer proteins from the cytosol, GTP, and fatty acyl-coenzyme A (CoA) [4].
  • The small GTP-binding protein, ADP-ribosylation factor (ARF), has previously been shown to mediate the binding to Golgi membranes of the coatomer of non-cathrin-coated (COP-coated) vesicles [5].

Biological context of COP-Coated Vesicles


Anatomical context of COP-Coated Vesicles


Associations of COP-Coated Vesicles with chemical compounds


Gene context of COP-Coated Vesicles

  • Experiments with an epitope-tagged version of Erv14p indicate that this protein localizes to the ER and is selectively packaged into COPII-coated vesicles [14].
  • Formation of COPII-coated vesicles at the endoplasmic reticulum (ER) requires assembly onto the membrane of five cytosolic coat proteins, Sec23p, Sec24p, Sec13p, Sec31p, and Sar1p [15].
  • These observations indicate that GBF1 is involved in the formation of COPI-coated vesicles from the cis-Golgi or the pre-Golgi intermediate compartment through activating ADP-ribosylation factors [16].
  • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi [17].
  • Vesicle formation from an erv25Delta strain, an emp24Delta strain and a double erv25Delta emp24Delta strain proceed at wild-type levels; however, incorporation of the Erv25p or the Emp24p protein into COPII-coated vesicles requires expression of both subunits [18].


  1. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Goldberg, J. Cell (2000) [Pubmed]
  2. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Goldberg, J. Cell (1999) [Pubmed]
  3. Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. Bremser, M., Nickel, W., Schweikert, M., Ravazzola, M., Amherdt, M., Hughes, C.A., Söllner, T.H., Rothman, J.E., Wieland, F.T. Cell (1999) [Pubmed]
  4. Stepwise assembly of functionally active transport vesicles. Ostermann, J., Orci, L., Tani, K., Amherdt, M., Ravazzola, M., Elazar, Z., Rothman, J.E. Cell (1993) [Pubmed]
  5. 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. Cell (1993) [Pubmed]
  6. A role for ADP ribosylation factor in the control of cargo uptake during COPI-coated vesicle biogenesis. Malsam, J., Gommel, D., Wieland, F.T., Nickel, W. FEBS Lett. (1999) [Pubmed]
  7. Modulation of intracellular transport by transported proteins: insight from regulation of COPI-mediated transport. Aoe, T., Lee, A.J., van Donselaar, E., Peters, P.J., Hsu, V.W. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  8. Drosophila Cornichon acts as cargo receptor for ER export of the TGFalpha-like growth factor Gurken. Bökel, C., Dass, S., Wilsch-Bräuninger, M., Roth, S. Development (2006) [Pubmed]
  9. Evidence for segregation of sphingomyelin and cholesterol during formation of COPI-coated vesicles. Brügger, B., Sandhoff, R., Wegehingel, S., Gorgas, K., Malsam, J., Helms, J.B., Lehmann, W.D., Nickel, W., Wieland, F.T. J. Cell Biol. (2000) [Pubmed]
  10. The production of post-Golgi vesicles requires a protein kinase C-like molecule, but not its phosphorylating activity. Simon, J.P., Ivanov, I.E., Adesnik, M., Sabatini, D.D. J. Cell Biol. (1996) [Pubmed]
  11. Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles. Ktistakis, N.T., Brown, H.A., Waters, M.G., Sternweis, P.C., Roth, M.G. J. Cell Biol. (1996) [Pubmed]
  12. Secretory bulk flow of soluble proteins is efficient and COPII dependent. Phillipson, B.A., Pimpl, P., daSilva, L.L., Crofts, A.J., Taylor, J.P., Movafeghi, A., Robinson, D.G., Denecke, J. Plant Cell (2001) [Pubmed]
  13. ADP-ribosylation factor and phosphatidic acid levels in Golgi membranes during budding of coatomer-coated vesicles. Stamnes, M., Schiavo, G., Stenbeck, G., Söllner, T.H., Rothman, J.E. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  14. Transport of axl2p depends on erv14p, an ER-vesicle protein related to the Drosophila cornichon gene product. Powers, J., Barlowe, C. J. Cell Biol. (1998) [Pubmed]
  15. COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Gimeno, R.E., Espenshade, P., Kaiser, C.A. Mol. Biol. Cell (1996) [Pubmed]
  16. GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Kawamoto, K., Yoshida, Y., Tamaki, H., Torii, S., Shinotsuka, C., Yamashina, S., Nakayama, K. Traffic (2002) [Pubmed]
  17. The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. Schimmöller, F., Singer-Krüger, B., Schröder, S., Krüger, U., Barlowe, C., Riezman, H. EMBO J. (1995) [Pubmed]
  18. Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport. Belden, W.J., Barlowe, C. J. Biol. Chem. (1996) [Pubmed]
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