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

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Structure

DOI:https://doi.org/10.1016/j.str.2007.03.011· OSTI ID:930443

Li, J; Mao, X; Dong, L; Liu, F; Tong, L

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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 930443
• Report Number(s): BNL--81188-2008-JA
• Journal Information: Structure, Journal Name: Structure Vol. 15; ISSN 0969-2126
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
DIMERIZATION
DIMERS
GENES
HUMAN CHROMOSOMES
LIPIDS
PHOSPHOLIPIDS
RECEPTORS
YEASTS
national synchrotron light source