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dc.contributor.authorKlarlund, Jes K.
dc.contributor.authorGuilherme, Adilson L.
dc.contributor.authorHolik, John
dc.contributor.authorVirbasius, Joseph V.
dc.contributor.authorChawla, Anil
dc.contributor.authorCzech, Michael P.
dc.date2022-08-11T08:09:35.000
dc.date.accessioned2022-08-23T16:36:30Z
dc.date.available2022-08-23T16:36:30Z
dc.date.issued1997-03-28
dc.date.submitted2009-03-31
dc.identifier.citation<p>Science. 1997 Mar 28;275(5308):1927-30.</p>
dc.identifier.issn0036-8075 (Print)
dc.identifier.pmid9072969
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38802
dc.description.abstractSignal 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.isoen_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.urlhttps://doi.org/10.1126/science.275.5308.1927
dc.subject1-Phosphatidylinositol 3-Kinase
dc.subjectADP-Ribosylation Factor 1
dc.subjectADP-Ribosylation Factors
dc.subjectAdipocytes
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectAntigens, CD18
dc.subjectBlood Proteins
dc.subjectBrain Chemistry
dc.subjectCell Adhesion Molecules
dc.subjectCell Membrane
dc.subjectCells, Cultured
dc.subjectCloning, Molecular
dc.subjectDNA, Complementary
dc.subjectFungal Proteins
dc.subjectGTP-Binding Proteins
dc.subject*Guanine Nucleotide Exchange Factors
dc.subjectHumans
dc.subjectMice
dc.subjectMolecular Sequence Data
dc.subjectPhosphatidylinositol Phosphates
dc.subject*Phosphoproteins
dc.subjectPhosphorylation
dc.subjectPhosphotransferases (Alcohol Group Acceptor)
dc.subjectReceptors, Cytoplasmic and Nuclear
dc.subjectRecombinant Fusion Proteins
dc.subjectSequence Homology, Amino Acid
dc.subject*Signal Transduction
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSignaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
dc.typeArticle
dc.source.journaltitleScience (New York, N.Y.)
dc.source.volume275
dc.source.issue5308
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1646
dc.identifier.contextkey805467
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.submissionpathoapubs/1646
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages1927-30


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