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Novel cargo-binding site in the beta and delta subunits of coatomer

Michelsen, K. and Schmid, V. and Metz, J. and Heusser, K. and Liebel, U. and Schwede, T. and Spang, A. and Schwappach, B.. (2007) Novel cargo-binding site in the beta and delta subunits of coatomer. The Journal of cell biology, Vol. 179, H. 2. pp. 209-217.

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Official URL: http://edoc.unibas.ch/dok/A5259738

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Abstract

Arginine (R)-based ER localization signals are sorting motifs that confer transient ER localization to unassembled subunits of multimeric membrane proteins. The COPI vesicle coat binds R-based signals but the molecular details remain unknown. Here, we use reporter membrane proteins based on the proteolipid Pmp2 fused to GFP and allele swapping of COPI subunits to map the recognition site for R-based signals. We show that two highly conserved stretches--in the beta- and delta-COPI subunits--are required to maintain Pmp2GFP reporters exposing R-based signals in the ER. Combining a deletion of 21 residues in delta-COP together with the mutation of three residues in beta-COP gave rise to a COPI coat that had lost its ability to recognize R-based signals, whilst the recognition of C-terminal di-lysine signals remained unimpaired. A homology model of the COPI trunk domain illustrates the recognition of R-based signals by COPI.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Spang)
05 Faculty of Science > Departement Biozentrum > Computational & Systems Biology > Bioinformatics (Schwede)
UniBasel Contributors:Schwede, Torsten and Spang, Anne
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Rockefeller University Press
ISSN:0021-9525
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
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Last Modified:31 Dec 2015 10:43
Deposited On:22 Mar 2012 13:23

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