Crystal Structures of the BAR-PH and PTB Domains of Human APPL1

Jiang Li, Xuming Mao, Lily Q. Dong, Feng Liu, Liang Tong

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

APPL1 interacts with adiponectin receptors and other important signaling molecules. It contains a BAR and a PH domain near its N terminus, and the two domains may function as a unit (BAR-PH domain). We report here the crystal structures of the BAR-PH and PTB domains of human APPL1. The structures reveal novel features for BAR domain dimerization and for the interactions between the BAR and PH domains. The BAR domain dimer of APPL1 contains two four-helical bundles, whereas other BAR domain dimers have only three helices in each bundle. The PH domain is located at the opposite ends of the BAR domain dimer. Yeast two-hybrid assays confirm the interactions between the BAR and PH domains. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. The ability of APPL1 to interact with multiple signaling molecules and phospholipids supports an important role for this adaptor in cell signaling.

Original languageEnglish (US)
Pages (from-to)525-533
Number of pages9
JournalStructure
Volume15
Issue number5
DOIs
StatePublished - May 16 2007

Keywords

  • CELLBIO
  • SIGNALING

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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