Coatomer, the Coat Protein of Copi Transport Vesicles, Discriminates Endoplasmic Reticulum Residents from P24 Proteins.
From: Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany. Julien.Bethune@bzh.uni-heidelberg.de
Molecular and cellular biology
- Publish Date: Nov 2006
- ISSN: 0270-7306
- Volume: 26
- Issue: 21
- Pages: 8011-21
- Medium: Print
- Language: English
- Citation (JAMA): Béthune Julien, Kol Matthijs, Hoffmann Julia, et al. Coatomer, the Coat Protein of Copi Transport Vesicles, Discriminates Endoplasmic Reticulum Residents from P24 Proteins.. Mol. Cell. Biol. Nov 2006;26:8011-21
Abstract
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 gamma-COP. In contrast, ER-resident cargos bind to coatomer as monomers and to sites other than gamma-COP. The COPI coat therefore discriminates between p24 proteins and ER-resident proteins by differential binding involving distinct subunits.
Mesh Headings (Keywords): Amino Acid Motifs, Animals, COP-Coated Vesicles, Carrier Proteins, Coatomer Protein, Dimerization, Endoplasmic Reticulum, Mannose-Binding Lectins, Membrane Proteins, Models, Molecular, Peptides, Protein Binding, Protein Isoforms, Protein Structure, Tertiary
Check for Full Text / PubMed Unique Identifier (PMID): 16940185
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