Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55

Ho Lee Hyung, Natalie Elia, Rodolfo Ghirlando, Jennifer Lippincott-Schwartz, James H. Hurley

Research output: Contribution to journalArticlepeer-review

203 Scopus citations

Abstract

The ESCRT (endosomal sorting complex required for transport) machinery is required for the scission of membrane necks in processes including the budding of HIV-1 and cytokinesis. An essential step in cytokinesis is recruitment of the ESCRT-I complex and the ESCRT-associated protein ALIX to the midbody (the structure that tethers two daughter cells) by the protein CEP55. Biochemical experiments show that peptides from ALIX and the ESCRT-I subunit TSG101 compete for binding to the ESCRT- and ALIX-binding region (EABR) of CEP55. We solved the crystal structure of EABR bound to an ALIX peptide at a resolution of 2.0 angstroms. The structure shows that EABR forms an aberrant dimeric parallel coiled coil. Bulky and charged residues at the interface of the two central heptad repeats create asymmetry and a single binding site for an ALIX or TSG101 peptide. Both ALIX and ESCRT-I are required for cytokinesis, which suggests that multiple CEP55 dimers are required for function.

Original languageEnglish
Pages (from-to)576-580
Number of pages5
JournalScience
Volume322
Issue number5901
DOIs
StatePublished - 24 Oct 2008
Externally publishedYes

ASJC Scopus subject areas

  • General

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