NDLI: p110δ, a novel phosphoinositide 3-kinase in leukocytes

Content Provider	PubMed Central
Author	Bart, Vanhaesebroeck Welham, Melanie J. Kotani, Kei Stein, Rob Warne, Patricia H. Zvelebil, Markéta J. Higashi, Kyoichiro Stefano, Volinia Downward, Julian Waterfield, Michael D.
Copyright Year	1997
Abstract	Phosphoinositide 3-kinases (PI3Ks) are a family of lipid kinases that have been implicated in signal transduction through tyrosine kinase- and heterotrimeric G-protein-linked receptors. We report herein the cloning and characterization of p110δ, a novel class I PI3K. Like p110α and p110β, other class I PI3Ks, p110δ displays a broad phosphoinositide lipid substrate specificity and interacts with SH2/SH3 domain-containing p85 adaptor proteins and with GTP-bound Ras. In contrast to the widely distributed p110α and β, p110δ is exclusively found in leukocytes. In these cells, p110α and δ both associate with the p85α and β adaptor subunits and are similarly recruited to activated signaling complexes after treatment with the cytokines interleukin 3 and 4 and stem cell factor. Thus, these class I PI3Ks appear not to be distinguishable at the level of p85 adaptor selection or recruitment to activated receptor complexes. However, distinct biochemical and structural features of p110δ suggest divergent functional/regulatory capacities for this PI3K. Unlike p110α, p110δ does not phosphorylate p85 but instead harbors an intrinsic autophosphorylation capacity. In addition, the p110δ catalytic domain contains unique potential protein–protein interaction modules such as a Pro-rich region and a basic-region leucine-zipper (bZIP)-like domain. Possible selective functions of p110δ in white blood cells are discussed.
Starting Page	4330
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	94
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1997-04-29
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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