Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
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Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins. / Michelsen, Kai; Yuan, Hebao; Schwappach, Blanche.
in: EMBO REP, Jahrgang 6, Nr. 8, 08.2005, S. 717-22.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung
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T1 - Hide and run. Arginine-based endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
AU - Michelsen, Kai
AU - Yuan, Hebao
AU - Schwappach, Blanche
PY - 2005/8
Y1 - 2005/8
N2 - Arginine-based endoplasmic reticulum (ER)-localization signals are sorting motifs that are involved in the biosynthetic transport of multimeric membrane proteins. After their discovery in the invariant chain of the major histocompatibility complex class II, several hallmarks of these signals have emerged. They occur in polytopic membrane proteins that are subunits of membrane protein complexes; the presence of the signal maintains improperly assembled subunits in the ER by retention or retrieval until it is masked as a result of heteromultimeric assembly. A distinct consensus sequence and their position independence with respect to the distal termini of the protein distinguish them from other ER-sorting motifs. Recognition by the coatomer (COPI) vesicle coat explains ER retrieval. Often, di-leucine endocytic signals occur close to arginine-based signals. Recruitment of 14-3-3 family or PDZ-domain proteins can counteract ER-localization activity, as can phosphorylation. This, and the occurrence of arginine-based signals in alternatively spliced regions, implicates them in the regulated surface expression of multimeric membrane proteins in addition to their function in quality control.
AB - Arginine-based endoplasmic reticulum (ER)-localization signals are sorting motifs that are involved in the biosynthetic transport of multimeric membrane proteins. After their discovery in the invariant chain of the major histocompatibility complex class II, several hallmarks of these signals have emerged. They occur in polytopic membrane proteins that are subunits of membrane protein complexes; the presence of the signal maintains improperly assembled subunits in the ER by retention or retrieval until it is masked as a result of heteromultimeric assembly. A distinct consensus sequence and their position independence with respect to the distal termini of the protein distinguish them from other ER-sorting motifs. Recognition by the coatomer (COPI) vesicle coat explains ER retrieval. Often, di-leucine endocytic signals occur close to arginine-based signals. Recruitment of 14-3-3 family or PDZ-domain proteins can counteract ER-localization activity, as can phosphorylation. This, and the occurrence of arginine-based signals in alternatively spliced regions, implicates them in the regulated surface expression of multimeric membrane proteins in addition to their function in quality control.
KW - 14-3-3 Proteins/chemistry
KW - Amino Acid Motifs
KW - Animals
KW - Arginine/chemistry
KW - Cell Membrane/metabolism
KW - Endocytosis
KW - Endoplasmic Reticulum/metabolism
KW - Humans
KW - Ions
KW - Macromolecular Substances
KW - Membrane Proteins/chemistry
KW - Models, Biological
KW - Potassium/chemistry
KW - Protein Structure, Tertiary
KW - Protein Transport
U2 - 10.1038/sj.embor.7400480
DO - 10.1038/sj.embor.7400480
M3 - SCORING: Review article
C2 - 16065065
VL - 6
SP - 717
EP - 722
JO - EMBO REP
JF - EMBO REP
SN - 1469-221X
IS - 8
ER -