PMID: 9552154Apr 29, 1998Paper

A phosphoinositide-binding sequence is shared by PH domain target molecules--a model for the binding of PH domains to proteins

Proteins
S Alberti

Abstract

Pleckstrin homology (PH) domains have been proven to bind phosphoinositides (PI) and inositolphosphates (IP). On the other hand, a binding of PH domains to proteins is still a matter of debate. The goal of this work was to identify potential PH domain protein target sites and to build a model for PH domain-protein binding. A candidate sequence, called HIKE, was identified by sequence homology analysis of the proteins that are considered the strongest PH binding candidates, i.e., Gbeta, PKC, and Akt. HIKE contains a PI binding sequence and fulfills several criteria for a potential PH-binding site, i.e., it is present in other PH-binding candidates, lies in regulatory regions independently predicted to bind PH domains, and is conserved in 3-D structure among different molecules. These findings and the similarities with the mode of binding of PTB and PDZ domains suggest a beta strand-beta strand coordination model for PH-protein binding. The HIKE model predicts that membrane anchoring of PH domains and their targets could be a critical step in their interaction, which would consistently explain why PH-protein binding has only been detected in the presence of PI.

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Citations

May 9, 2012·Oncogene·E GuerraS Alberti
Apr 3, 2003·Immunological Reviews·Lawrence P Kane, Arthur Weiss
Aug 31, 2000·Annual Review of Biochemistry·J L Popot, D M Engelman
Aug 18, 2000·The Journal of Biological Chemistry·T ObataL C Cantley
Jan 28, 2005·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Mary Ellen K Olsten, David W Litchfield
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