2cay

OverviewOverview

ESCRT complexes form the main machinery driving protein sorting from, endosomes to lysosomes. Currently, the picture regarding assembly of, ESCRTs on endosomes is incomplete. The structure of the conserved, heterotrimeric ESCRT-I core presented here shows a fan-like arrangement of, three helical hairpins, each corresponding to a different subunit., Vps23/Tsg101 is the central hairpin sandwiched between the other subunits, explaining the critical role of its "steadiness box" in the stability of, ESCRT-I. We show that yeast ESCRT-I links directly to ESCRT-II, through a, tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger, insertion within the GLUE domain of Vps36 (ESCRT-II). The crystal, structure of the GLUE domain missing this insertion reveals it is a split, PH domain, with a noncanonical lipid binding pocket that binds PtdIns3P., The simultaneous and reinforcing interactions of ESCRT-II GLUE domain with, membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo, progression from early to late endosomes.

About this StructureAbout this Structure

2CAY is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes., Teo H, Gill DJ, Sun J, Perisic O, Veprintsev DB, Vallis Y, Emr SD, Williams RL, Cell. 2006 Apr 7;125(1):99-111. PMID:16615893

Page seeded by OCA on Tue Dec 18 19:16:21 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA