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Signaling by Phosphoinositide-3,4,5-trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains
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-...
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| Published in: | Science (American Association for the Advancement of Science) 1997-03, Vol.275 (5308), p.1927-1930 |
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| Main Authors: | , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c837t-913fb383b36b87eb494414776ee4889db08e9b5b5ac095d7d2d3826512d548cb3 |
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| cites | cdi_FETCH-LOGICAL-c837t-913fb383b36b87eb494414776ee4889db08e9b5b5ac095d7d2d3826512d548cb3 |
| container_end_page | 1930 |
| container_issue | 5308 |
| container_start_page | 1927 |
| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 275 |
| creator | Klarlund, Jes K. Guilherme, Adilson Holik, John J. Virbasius, Joseph V. Chawla, Anil Czech, Michael P. |
| description | 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. |
| doi_str_mv | 10.1126/science.275.5308.1927 |
| format | article |
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Michigan</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Klarlund, Jes K.</au><au>Guilherme, Adilson</au><au>Holik, John J.</au><au>Virbasius, Joseph V.</au><au>Chawla, Anil</au><au>Czech, Michael P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Signaling by Phosphoinositide-3,4,5-trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1997-03-28</date><risdate>1997</risdate><volume>275</volume><issue>5308</issue><spage>1927</spage><epage>1930</epage><pages>1927-1930</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><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.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9072969</pmid><doi>10.1126/science.275.5308.1927</doi><tpages>4</tpages></addata></record> |
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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1997-03, Vol.275 (5308), p.1927-1930 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78906350 |
| source | American Association for the Advancement of Science; Social Science Premium Collection; Alma/SFX Local Collection; Education Collection |
| subjects | Adipocytes - chemistry ADP-Ribosylation Factor 1 ADP-Ribosylation Factors Amino Acid Sequence Amino acids Animals Biological and medical sciences Blood Proteins - chemistry Brain Brain Chemistry CD18 Antigens - metabolism Cell adhesion Cell Adhesion Molecules - chemistry Cell Adhesion Molecules - metabolism Cell Membrane - metabolism Cell physiology Cells, Cultured Cellular signal transduction Cellulose nitrate Cloning, Molecular Complementary DNA DNA, Complementary Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry GTP-Binding Proteins - metabolism Guanine Nucleotide Exchange Factors Humans Integrins Libraries Lipids Mice Molecular and cellular biology Molecular biology Molecular Sequence Data Phosphatidylinositol Phosphatidylinositol 3-Kinases Phosphatidylinositol Phosphates - metabolism Phosphatidylinositols Phosphoinositides Phosphoproteins Phosphorylation Phosphotransferases (Alcohol Group Acceptor) - metabolism Protein isoforms Proteins Receptors, Cytoplasmic and Nuclear - metabolism Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Responses to growth factors, tumor promotors, other factors Rodents Screening Tests Sequence Homology, Amino Acid Signal Transduction |
| title | Signaling by Phosphoinositide-3,4,5-trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T21%3A06%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Signaling%20by%20Phosphoinositide-3,4,5-trisphosphate%20Through%20Proteins%20Containing%20Pleckstrin%20and%20Sec7%20Homology%20Domains&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Klarlund,%20Jes%20K.&rft.date=1997-03-28&rft.volume=275&rft.issue=5308&rft.spage=1927&rft.epage=1930&rft.pages=1927-1930&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.275.5308.1927&rft_dat=%3Cgale_proqu%3EA19318758%3C/gale_proqu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c837t-913fb383b36b87eb494414776ee4889db08e9b5b5ac095d7d2d3826512d548cb3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=213554702&rft_id=info:pmid/9072969&rft_galeid=A19318758&rft_jstor_id=2893077&rfr_iscdi=true |