A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1

Richard A Kahn; David G Lambright

doi:10.1016/j.str.2015.10.002

A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1

Structure. 2015 Nov 3;23(11):1971-3. doi: 10.1016/j.str.2015.10.002.

Authors

Richard A Kahn¹, David G Lambright²

Affiliations

¹ Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. Electronic address: rkahn@emory.edu.
² Program in Molecular Medicine and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address: david.lambright@umassmed.edu.

PMID: 26536378
DOI: 10.1016/j.str.2015.10.002

Abstract

In this issue of Structure, Jian et al. (2015) report the crystal structures of the apo- and dibutyryl-PI(4,5)P2 bound forms of the PH domain from the ARF GAP, ASAP1. This PH domain has two anionic phospholipid binding sites proposed to work in concert to regulate ASAP1 GAP activity.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Adaptor Proteins, Signal Transducing / chemistry*
Binding Sites
Models, Molecular*
Phospholipids / metabolism
Protein Binding
Protein Structure, Tertiary

Substances

Adaptor Proteins, Signal Transducing
Phospholipids

Abstract

Publication types

MeSH terms

Substances

Grants and funding