FEBS Letters
Volume 581, Issue 11 , Pages 2076-2082, 22 May 2007

Mechanisms of COPII vesicle formation and protein sorting

Edited by Thomas Söllner

  • Ken Sato

      Affiliations

    • Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Hirosawa, Wako, Saitama 351-0198, Japan
    • Corresponding Author InformationCorresponding author. Fax: +81 48 462 4679.
  • ,
  • Akihiko Nakano

      Affiliations

    • Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, Hirosawa, Wako, Saitama 351-0198, Japan
    • Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

Received 29 November 2006; received in revised form 23 January 2007; accepted 30 January 2007. published online 13 February 2007.

Abstract 

The evolutionarily conserved coat protein complex II (COPII) generates transport vesicles that mediate protein transport from the endoplasmic reticulum (ER). COPII coat is responsible for direct capture of cargo proteins and for the physical deformation of the ER membrane that drives the COPII vesicle formation. In addition to coat proteins, recent data have indicated that the Ras-like small GTPase Sar1 plays multiple roles, such as COPII coat recruitment, cargo sorting, and completion of the final fission. In the present review, we summarize current knowledge of COPII-mediated vesicle formation from the ER, as well as highlighting non-canonical roles of COPII components.

Keywords: COPII, Sar1, Small GTPase, Endoplasmic reticulum, Vesicular transport

To access this article, please choose from the options below

Login to an existing account or Register a new account.

  • Purchase this article for 31.50 USD (You must login/register to purchase this article)

    Online access for 24 hours. The PDF version can be downloaded as your permanent record.

  • Subscribe to this title

    Get unlimited online access to this article and all other articles in this title 24/7 for one year.

  • Claim access now

    For current subscribers with Society Membership or Account Number.

  • Visit SciVerse ScienceDirect to see if you have access via your institution.
 

PII: S0014-5793(07)00153-6

doi:10.1016/j.febslet.2007.01.091

FEBS Letters
Volume 581, Issue 11 , Pages 2076-2082, 22 May 2007