| First Author | Klarlund JK | Year | 1997 |
| Journal | Science | Volume | 275 |
| Issue | 5308 | Pages | 1927-30 |
| PubMed ID | 9072969 | Mgi Jnum | J:39322 |
| Mgi Id | MGI:86705 | Doi | 10.1126/science.275.5308.1927 |
| Citation | Klarlund JK, et al. (1997) Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains [see comments]. Science 275(5308):1927-30 |
| abstractText | 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 GRP1was identified. GRP1 binds phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4, 5)P3] 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 beta2 and catalyzes guanine nucleotide exchange of the small guanine nucleotide-binding protein ARF1, was also found to specifically bind PtdIns(3,4,5)P3. 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. |
