Novel cargo-binding site in the beta and delta subunits of coatomer
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Novel cargo-binding site in the beta and delta subunits of coatomer. / Michelsen, Kai; Schmid, Volker; Metz, Jutta; Heusser, Katja; Liebel, Urban; Schwede, Torsten; Spang, Anne; Schwappach, Blanche.
in: J CELL BIOL, Jahrgang 179, Nr. 2, 22.10.2007, S. 209-17.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Novel cargo-binding site in the beta and delta subunits of coatomer
AU - Michelsen, Kai
AU - Schmid, Volker
AU - Metz, Jutta
AU - Heusser, Katja
AU - Liebel, Urban
AU - Schwede, Torsten
AU - Spang, Anne
AU - Schwappach, Blanche
PY - 2007/10/22
Y1 - 2007/10/22
N2 - 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.
AB - 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.
KW - Adaptor Protein Complex 1/metabolism
KW - Amino Acid Sequence
KW - Arginine
KW - Binding Sites
KW - Coatomer Protein/chemistry
KW - Conserved Sequence
KW - Endoplasmic Reticulum/metabolism
KW - Genes, Fungal
KW - Molecular Sequence Data
KW - Mutant Proteins/metabolism
KW - Mutation/genetics
KW - Protein Sorting Signals
KW - Protein Subunits/chemistry
KW - Protein Transport
KW - Saccharomyces cerevisiae/cytology
KW - Structural Homology, Protein
U2 - 10.1083/jcb.200704142
DO - 10.1083/jcb.200704142
M3 - SCORING: Journal article
C2 - 17954604
VL - 179
SP - 209
EP - 217
JO - J CELL BIOL
JF - J CELL BIOL
SN - 0021-9525
IS - 2
ER -