Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
dc.contributor.author | Klarlund, Jes K. | |
dc.contributor.author | Guilherme, Adilson L. | |
dc.contributor.author | Holik, John | |
dc.contributor.author | Virbasius, Joseph V. | |
dc.contributor.author | Chawla, Anil | |
dc.contributor.author | Czech, Michael P. | |
dc.date | 2022-08-11T08:09:35.000 | |
dc.date.accessioned | 2022-08-23T16:36:30Z | |
dc.date.available | 2022-08-23T16:36:30Z | |
dc.date.issued | 1997-03-28 | |
dc.date.submitted | 2009-03-31 | |
dc.identifier.citation | <p>Science. 1997 Mar 28;275(5308):1927-30.</p> | |
dc.identifier.issn | 0036-8075 (Print) | |
dc.identifier.pmid | 9072969 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/38802 | |
dc.description.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 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. | |
dc.language.iso | en_US | |
dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9072969&dopt=Abstract">Link to Article in PubMed</a></p> | |
dc.relation.url | https://doi.org/10.1126/science.275.5308.1927 | |
dc.subject | 1-Phosphatidylinositol 3-Kinase | |
dc.subject | ADP-Ribosylation Factor 1 | |
dc.subject | ADP-Ribosylation Factors | |
dc.subject | Adipocytes | |
dc.subject | Amino Acid Sequence | |
dc.subject | Animals | |
dc.subject | Antigens, CD18 | |
dc.subject | Blood Proteins | |
dc.subject | Brain Chemistry | |
dc.subject | Cell Adhesion Molecules | |
dc.subject | Cell Membrane | |
dc.subject | Cells, Cultured | |
dc.subject | Cloning, Molecular | |
dc.subject | DNA, Complementary | |
dc.subject | Fungal Proteins | |
dc.subject | GTP-Binding Proteins | |
dc.subject | *Guanine Nucleotide Exchange Factors | |
dc.subject | Humans | |
dc.subject | Mice | |
dc.subject | Molecular Sequence Data | |
dc.subject | Phosphatidylinositol Phosphates | |
dc.subject | *Phosphoproteins | |
dc.subject | Phosphorylation | |
dc.subject | Phosphotransferases (Alcohol Group Acceptor) | |
dc.subject | Receptors, Cytoplasmic and Nuclear | |
dc.subject | Recombinant Fusion Proteins | |
dc.subject | Sequence Homology, Amino Acid | |
dc.subject | *Signal Transduction | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains | |
dc.type | Journal Article | |
dc.source.journaltitle | Science (New York, N.Y.) | |
dc.source.volume | 275 | |
dc.source.issue | 5308 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/oapubs/1646 | |
dc.identifier.contextkey | 805467 | |
html.description.abstract | <p>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.</p> | |
dc.identifier.submissionpath | oapubs/1646 | |
dc.contributor.department | Department of Biochemistry and Molecular Biology | |
dc.contributor.department | Program in Molecular Medicine | |
dc.source.pages | 1927-30 |