2ynp

Publication Abstract from PubMed

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 beta'-COP identifies electrostatic contacts between the motif and complementary patches at the center of the beta'-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 beta'-COP. Similar interactions are proposed to mediate binding of KKxx motifs by the homologous alpha-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 beta'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly.

Molecular Basis for Recognition of Dilysine Trafficking Motifs by COPI.,Jackson LP, Lewis M, Kent HM, Edeling MA, Evans PR, Duden R, Owen DJ Dev Cell. 2012 Nov 20. pii: S1534-5807(12)00480-7. doi:, 10.1016/j.devcel.2012.10.017. PMID:23177648^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.