Phosphoinositide 3-kinase gamma has multiple phospholipid binding sites.

Abstract

Phosphoinositide 3-kinase gamma is a multifunctional enzyme with lipid and protein kinase activities that also acts as a scaffold protein in many diverse signalling processes. The enzyme contains five different domains, but their individual contributions to membrane binding are not fully understood. Here, using in vitro liposome binding assays of individual domains and deletion constructs of human phosphoinositide 3-kinase gamma, we show that each domain is capable of binding anionic phospholipids to varying degrees, depending on the charge of the anionic substrate. Moreover, with the exception of the C2-domain, deletion of any single protein domain results in a complete loss of kinase activity toward both lipids and proteins.

DOI: 10.1007/s10930-010-9232-x

Statistics

02004006002014201520162017
Citations per Year

203 Citations

Semantic Scholar estimates that this publication has 203 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Schmidt2010Phosphoinositide3G, title={Phosphoinositide 3-kinase gamma has multiple phospholipid binding sites.}, author={Carsten Schmidt and Margret Schilli-Westermann and Reinhard Klinger and Cornelia Kirsch}, journal={The protein journal}, year={2010}, volume={29 2}, pages={127-35} }