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Cited by 675

The DOI matches its Crossref record.

Cloning and Characterization of a G Protein-Activated Human Phosphoinositide-3 Kinase

Stoyanov, Borislav, Volinia, Stefano, Hanck, Theodor, Rubio, Ignacio, Loubtchenkov, Michael, Malek, Daria, Stoyanova, Stefka, Vanhaesebroeck, Bart, Dhand, Ritu, Nürnberg, Bernd, Gierschik, Peter, Seedorf, Klaus, Hsuan, J. Justin, Waterfield, Michael D., Wetzker, Reinhard·1995·Science
DOI 10.1126/science.7624799
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Abstract

Phosphoinositide-3 kinase activity is implicated in diverse cellular responses triggered by mammalian cell surface receptors and in the regulation of protein sorting in yeast. Receptors with intrinsic and associated tyrosine kinase activity recruit heterodimeric phosphoinositide-3 kinases that consist of p110 catalytic subunits and p85 adaptor molecules containing Src homology 2 (SH2) domains. A phosphoinositide-3 kinase isotype, p110γ, was cloned and characterized. The p110γ enzyme was activated in vitro by both the α and βγ subunits of heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) and did not interact with p85. A potential pleckstrin homology domain is located near its amino terminus. The p110γ isotype may link signaling through G protein-coupled receptors to the generation of phosphoinositide second messengers phosphorylated in the D-3 position.

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Authors
Stoyanov, B., Volinia, S., Hanck, T., Rubio, I., Loubtchenkov, M., Malek, D., Stoyanova, S., Vanhaesebroeck, B., Dhand, R., Nürnberg, B., Gierschik, P., Seedorf, K., Hsuan, J. J., Waterfield, M. D., & Wetzker, R.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1995-08-04
Volume
269
Issue
5224
Pages
690-693
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.7624799
OpenAlex
W1994957003
Cited by
675
References
0
FWCI
22.14
Type
journal article
Language
en
Open access
closed

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