Time to fold

Tom1 uses new tricks to regulate lipid binding of tollip

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

In this issue of Structure, Xiao et al. (2015) describe a new mechanism of regulation of lipid binding. Structural and functional studies demonstrate that Tom1 interactions with the cargo sorting protein Tollip induce the partially unfolded Tom1-binding domain of Tollip to fold. This folding modulates lipid binding of Tollip, mediating its dissociation from PI(3)P and committing Tollip to cargo trafficking.

Original languageEnglish (US)
Pages (from-to)1781-1782
Number of pages2
JournalStructure
Volume23
Issue number10
DOIs
StatePublished - Oct 6 2015

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Lipids
Protein Transport

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Time to fold : Tom1 uses new tricks to regulate lipid binding of tollip. / Stahelin, Robert.

In: Structure, Vol. 23, No. 10, 06.10.2015, p. 1781-1782.

Research output: Contribution to journalArticle

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