FEBS Letters
Volume 583, Issue 23 , Pages 3758-3763, 3 December 2009

Mechanisms of COPI vesicle formation

  • Victor W. Hsu

      Affiliations

    • Corresponding Author InformationCorresponding author. Address: Brigham and Women’s Hospital, One Jimmy Fund Way, Smith 538, Boston, MA 02115, USA. Fax: +1 617 525 1104.
    • ,
  • Jia-Shu Yang

Division of Rheumatology, Immunology and Allergy, Brigham and Women’s Hospital, Boston, MA 02115, USA

Department of Medicine, Harvard Medical School, Boston, MA 02115, USA

Received 19 June 2009; received in revised form 15 October 2009; accepted 20 October 2009. published online 23 October 2009.

Edited by Alberto Luini

Abstract 

Coat Protein I (COPI) is one of the most intensely investigated coat complexes. Numerous studies have contributed to a general understanding of how coat proteins act to initiate intracellular vesicular transport. This review highlights key recent findings that have shaped our current understanding of how COPI vesicles are formed.

Abbreviations: ARF, ADP-ribosylation factor, ARFGAP, ADP-ribosylation factor GTPase activating protein, BARS, brefeldin-A ADP-ribosylated substrate, BFA, brefeldin A, COP, coat protein, CtBP, C-terminal binding protein, DAG, diacylglycerol, GAP, GTPase-activating protein, GBF1, Golgi-specific brefeldin A resistant guanine nucleotide exchange factor 1, GEF, guanine nucleotide exchange factor, GTP, guanosine-5′-triphosphate, NAD, nicotinamide adenine dinucleotide, PA, phosphatidic acid, p-CoA, palmitoyl-coenzyme A, PLD2, phospholipase D type 2

Keywords: ADP-ribosylation factor 1, ADP-ribosylation factor GTPase activating protein 1, Brefeldin-A ADP-ribosylated substrate, Coatomer, Coat Protein I, Golgi-specific brefeldin A resistant guanine nucleotide exchange factor 1

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PII: S0014-5793(09)00844-8

doi:10.1016/j.febslet.2009.10.056

FEBS Letters
Volume 583, Issue 23 , Pages 3758-3763, 3 December 2009

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