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Updated: Aug 8, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
Published on: June 23, 2022
The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
Mylavarapu V S Sivaram1, Melonnie L M Furgason, Daniel N Brewer
1Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA.
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.
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