This Article Full Text Full Text (PDF) Other Versions of this Article: MCB.01055-06v1 26/21/8011    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Béthune, J. Articles by Wieland, F. Search for Related Content PubMed PubMed Citation Articles by Béthune, J. Articles by Wieland, F.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2006, p. 8011-8021, Vol. 26, No. 21
0270-7306/06/$08.00+0     doi:10.1128/MCB.01055-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Coatomer, the Coat Protein of COPI Transport Vesicles, Discriminates Endoplasmic Reticulum Residents from p24 Proteins

Biochemie-Zentrum der Universität Heidelberg (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany

Received 12 June 2006/ Returned for modification 3 August 2006/ Accepted 17 August 2006

In the formation of COPI vesicles, interactions take place between the coat protein coatomer and membrane proteins: either cargo proteins for retrieval to the endoplasmic reticulum (ER) or proteins that cycle between the ER and the Golgi. While the binding sites on coatomer for ER residents have been characterized, how cycling proteins bind to the COPI coat is still not clear. In order to understand at a molecular level the mechanism of uptake of such proteins, we have investigated the binding to coatomer of p24 proteins as examples of cycling proteins as well as that of ER-resident cargos. The p24 proteins required dimerization to interact with coatomer at two independent binding sites in -COP. In contrast, ER-resident cargos bind to coatomer as monomers and to sites other than -COP. The COPI coat therefore discriminates between p24 proteins and ER-resident proteins by differential binding involving distinct subunits.

Published ahead of print on 28 August 2006.

This article has been cited by other articles:

• Burman, J. L., Bourbonniere, L., Philie, J., Stroh, T., Dejgaard, S. Y., Presley, J. F., McPherson, P. S. (2008). Scyl1, Mutated in a Recessive Form of Spinocerebellar Neurodegeneration, Regulates COPI-mediated Retrograde Traffic. J. Biol. Chem. 283: 22774-22786 [Abstract] [Full Text]  
• Styers, M. L., O'Connor, A. K., Grabski, R., Cormet-Boyaka, E., Sztul, E. (2008). Depletion of {beta}-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1. Am. J. Physiol. Cell Physiol. 294: C1485-C1498 [Abstract] [Full Text]  
• Mitrovic, S., Ben-Tekaya, H., Koegler, E., Gruenberg, J., Hauri, H.-P. (2008). The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi. Mol. Biol. Cell 19: 1976-1990 [Abstract] [Full Text]  
• Aguilera-Romero, A., Kaminska, J., Spang, A., Riezman, H., Muniz, M. (2008). The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus. J. Cell Biol. 180: 713-720 [Abstract] [Full Text]  
• Moelleken, J., Malsam, J., Betts, M. J., Movafeghi, A., Reckmann, I., Meissner, I., Hellwig, A., Russell, R. B., Sollner, T., Brugger, B., Wieland, F. T. (2007). Differential localization of coatomer complex isoforms within the Golgi apparatus. Proc. Natl. Acad. Sci. USA 104: 4425-4430 [Abstract] [Full Text]