Novel cargo-binding site in the β and δ subunits of coatomer

Michelsen, Kai; Schmid, Volker; Metz, Jutta; Heusser, Katja; Liebel, Urban; Schwede, Torsten; Spang, Anne; Schwappach, Blanche

doi:10.1083/jcb.200704142

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Novel cargo-binding site in the β and δ subunits of coatomer

Michelsen, Kai Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany
Schmid, Volker Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany
Metz, Jutta Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany
Heusser, Katja Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany
Liebel, Urban European Molecular Biology Laboratory (EMBL), Cell Biology Cell Biophysics Unit, D-69117 Heidelberg, Germany
Schwede, Torsten Swiss Institute of Bioinformatics, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
Spang, Anne Growth & Development, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
Schwappach, Blanche Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany

2007-10-22

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Journal of Cell Biology. - Rockefeller University Press. - 2007, vol. 179, no. 2, p. 209-217

Cell Biology

English 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 β- and δ-COPI subunits—are required to maintain Pmp2GFP reporters exposing R-based signals in the ER. Combining a deletion of 21 residues in δ-COP together with the mutation of three residues in β-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.

Language

English

Open access status

bronze

Identifiers

DOI 10.1083/jcb.200704142
ISSN 1540-8140

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https://sonar.ch/global/documents/231742

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