Allosteric properties of PH domains in Arf regulatory proteins. Issue 2 (2nd April 2016)

• Record Type: Journal Article
• Authors: Roy, Neeladri Sekhar; Yohe, Marielle E.; Randazzo, Paul A.; Gruschus, James M.
• Is Part Of: Cellular logistics. Volume 6:Issue 2(2016)
• Publication Date: 2016-04-02
• Subjects: ADP-ribosylation factor -- allosterism -- cooperativity -- GTPase-activating protein -- guanine nucleotide exchange factor -- Pleckstrin homology; Cytology -- Periodicals; 571.6
• DOI: 10.1080/21592799.2016.1181700
• Languages: English
• ISSNs: 2159-2799

Abstract

ABSTRACT: Pleckstrin Homology (PH) domains bind phospholipids and proteins. They are critical regulatory elements of a number enzymes including guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) for Ras-superfamily guanine nucleotide binding proteins such as ADP-ribosylation factors (Arfs). Recent studies have indicated that many PH domains may bind more than one ligand cooperatively. Here we discuss the molecular basis of PH domain-dependent allosteric behavior of 2 ADP-ribosylation factor exchange factors, Grp1 and Brag2, cooperative binding of ligands to the PH domains of Grp1 and the Arf GTPase-activating protein, ASAP1, and the consequences for activity of the associated catalytic domains.