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
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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Cites
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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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