Structural and functional organization of the ESCRT-I trafficking complex. Academic Article uri icon

Overview

abstract

  • The endosomal sorting complex required for transport (ESCRT) complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. The yeast ESCRT-I complex contains the Vps23, Vps28, and Vps37 proteins, and its assembly is directed by the C-terminal steadiness box of Vps23, the N-terminal half of Vps28, and the C-terminal half of Vps37. The crystal structures of a Vps23:Vps28 core subcomplex and the Vps23:Vps28:Vps37 core were solved at 2.1 and 2.8 A resolution. Each subunit contains a structurally similar pair of helices that form the core. The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic. The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners.

publication date

  • April 7, 2006

Research

keywords

  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins

Identity

PubMed Central ID

  • PMC1576341

Scopus Document Identifier

  • 33646116786

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2006.01.049

PubMed ID

  • 16615894

Additional Document Info

volume

  • 125

issue

  • 1