| Title: |
Molecular Basis for Recognition of Dilysine Trafficking Motifs by COPI |
| Authors: |
Jackson, LP; Lewis, M; Kent, HM; Edeling, MA; Evans, PR; Duden, R; Owen, DJ |
| Publisher Information: |
CELL PRESS |
| Publication Year: |
2012 |
| Collection: |
The University of Melbourne: Digital Repository |
| Description: |
COPI mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) and within the Golgi stack, sorting transmembrane proteins bearing C-terminal KKxx or KxKxx motifs. The structure of KxKxx motifs bound to the N-terminal WD-repeat domain of β'-COP identifies electrostatic contacts between the motif and complementary patches at the center of the β'-COP propeller. An absolute requirement of a two-residue spacing between the terminal carboxylate group and first lysine residue results from interactions of carbonyl groups in the motif backbone with basic side chains of β'-COP. Similar interactions are proposed to mediate binding of KKxx motifs by the homologous α-COP domain. Mutation of key interacting residues in either domain or in their cognate motifs abolishes in vitro binding and results in mistrafficking of dilysine-containing cargo in yeast without compromising cell viability. Flexibility between β'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| ISSN: |
1534-5807 |
| Relation: |
https://hdl.handle.net/11343/277210 |
| Availability: |
https://hdl.handle.net/11343/277210 |
| Rights: |
https://creativecommons.org/licenses/by/4.0 ; CC BY |
| Accession Number: |
edsbas.5B0806CF |
| Database: |
BASE |