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Cited by 414

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Signaling by Phosphoinositide-3,4,5-Trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains

Klarlund, Jes K., Guilherme, Adilson, Holik, John J., Virbasius, Joseph V., Chawla, Anil, Czech, Michael P.·1997·Science

Abstract

Signal transmission by many cell surface receptors results in the activation of phosphoinositide (PI) 3-kinases that phosphorylate the 3′ position of polyphosphoinositides. From a screen for mouse proteins that bind phosphoinositides, the protein GRP1 was identified. GRP1 binds phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4,5)P 3 ] through a pleckstrin homology (PH) domain and displays a region of high sequence similarity to the yeast Sec7 protein. The PH domain of the closely related protein cytohesin-1, which, through its Sec7 homology domain, regulates integrin β2 and catalyzes guanine nucleotide exchange of the small guanine nucleotide-binding protein ARF1, was also found to specifically bind PtdIns(3,4,5)P 3 . GRP1 and cytohesin-1 appear to connect receptor-activated PI 3-kinase signaling pathways with proteins that mediate biological responses such as cell adhesion and membrane trafficking.

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Metadata

Authors
Klarlund, J. K., Guilherme, A., Holik, J. J., Virbasius, J. V., Chawla, A., & Czech, M. P.
Venue
Science
Published
1997-03-28
Volume
275
Issue
5308
Pages
1927-1930
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2054379164
Cited by
414
References
1
FWCI
21.52
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Signaling by Phosphoinositide-3,4,5-Trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains. https://app.cochat.ai/papers/10.1126/science.275.5308.1927
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Klarlund, J. K., Guilherme, A., Holik, J. J., Virbasius, J. V., Chawla, A., & Czech, M. P. (1997). Signaling by Phosphoinositide-3,4,5-Trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains. Science. https://doi.org/10.1126/science.275.5308.1927

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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