GSBS Student Publications

Title

The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Pharmacology

Date

5-16-2006

Document Type

Article

Medical Subject Headings

Animals; Drosophila Proteins; Models, Molecular; Protein Conformation; Vesicular Transport Proteins

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The exocyst is a conserved protein complex essential for trafficking secretory vesicles to the plasma membrane. The structure of the C-terminal domain of the exocyst subunit Sec6p reveals multiple helical bundles, which are structurally and topologically similar to Exo70p and the C-terminal domains of Exo84p and Sec15, despite <10% sequence identity. The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins.

Rights and Permissions

Citation: Nat Struct Mol Biol. 2006 Jun;13(6):555-6. Epub 2006 May 14. Link to article on publisher's site

DOI of Published Version

10.1038/nsmb1096

Related Resources

Link to Article in PubMed

Journal Title

Nature structural and molecular biology

PubMed ID

16699513