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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, Vol. 179, No. 2, 22.10.2007, p. 209-17.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Michelsen, K, Schmid, V, Metz, J, Heusser, K, Liebel, U, Schwede, T, Spang, A & Schwappach, B 2007, 'Novel cargo-binding site in the beta and delta subunits of coatomer', J CELL BIOL, vol. 179, no. 2, pp. 209-17. https://doi.org/10.1083/jcb.200704142

APA

Michelsen, K., Schmid, V., Metz, J., Heusser, K., Liebel, U., Schwede, T., Spang, A., & Schwappach, B. (2007). Novel cargo-binding site in the beta and delta subunits of coatomer. J CELL BIOL, 179(2), 209-17. https://doi.org/10.1083/jcb.200704142

Vancouver

Michelsen K, Schmid V, Metz J, Heusser K, Liebel U, Schwede T et al. Novel cargo-binding site in the beta and delta subunits of coatomer. J CELL BIOL. 2007 Oct 22;179(2):209-17. https://doi.org/10.1083/jcb.200704142

Bibtex

@article{cc347e8143264fdaacec030307983845,
title = "Novel cargo-binding site in the beta and delta subunits of coatomer",
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.",
keywords = "Adaptor Protein Complex 1/metabolism, Amino Acid Sequence, Arginine, Binding Sites, Coatomer Protein/chemistry, Conserved Sequence, Endoplasmic Reticulum/metabolism, Genes, Fungal, Molecular Sequence Data, Mutant Proteins/metabolism, Mutation/genetics, Protein Sorting Signals, Protein Subunits/chemistry, Protein Transport, Saccharomyces cerevisiae/cytology, Structural Homology, Protein",
author = "Kai Michelsen and Volker Schmid and Jutta Metz and Katja Heusser and Urban Liebel and Torsten Schwede and Anne Spang and Blanche Schwappach",
year = "2007",
month = oct,
day = "22",
doi = "10.1083/jcb.200704142",
language = "English",
volume = "179",
pages = "209--17",
journal = "J CELL BIOL",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "2",

}

RIS

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 -