| LyGDI, a novel SHIP-interacting protein, is a negative regulator of FcγR-mediated phagocytosis. | |
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MedLine Citation:
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PMID: 21695085 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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SHIP and SHIP-2 are inositol phosphatases that regulate FcγR-mediated phagocytosis through catalytic as well as non-catalytic mechanisms. In this study we have used two-dimensional fluorescence difference gel electrophoresis (DIGE) analysis to identify downstream signaling proteins that uniquely associate with SHIP or SHIP-2 upon FcγR clustering in human monocytes. We identified LyGDI as a binding partner of SHIP, associating inducibly with the SHIP/Grb2/Shc complex. Immunodepletion and competition experiments with recombinant SHIP domains revealed that Grb2 and the proline-rich domain of SHIP were necessary for SHIP-LyGDI association. Functional studies in primary human monocytes showed that LyGDI sequesters Rac in the cytosol, preventing it from localizing to the membrane. Consistent with this, suppression of LyGDI expression resulted in significantly enhanced FcγR-mediated phagocytosis. |
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Authors:
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Payal Mehta; Anne-Sophie Wavreille; Steven E Justiniano; Rachel L Marsh; Jianhua Yu; Richard W Burry; David Jarjoura; Timothy Eubank; Michael A Caligiuri; Jonathan P Butchar; Susheela Tridandapani |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-06-14 |
Journal Detail:
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Title: PloS one Volume: 6 ISSN: 1932-6203 ISO Abbreviation: PLoS ONE Publication Date: 2011 |
Date Detail:
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Created Date: 2011-06-22 Completed Date: 2011-10-21 Revised Date: 2012-02-02 |
Medline Journal Info:
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Nlm Unique ID: 101285081 Medline TA: PLoS One Country: United States |
Other Details:
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Languages: eng Pagination: e21175 Citation Subset: IM |
Affiliation:
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The Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio, United States of America. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Line Cell Membrane / metabolism GRB2 Adaptor Protein / metabolism Guanine Nucleotide Dissociation Inhibitors / metabolism* Humans Monocytes / cytology, metabolism Phagocytosis* Phosphoric Monoester Hydrolases / chemistry, metabolism* Proline Protein Binding Protein Structure, Tertiary Protein Transport Receptors, IgG / metabolism* Shc Signaling Adaptor Proteins / metabolism Signal Transduction Tumor Suppressor Proteins / metabolism* rac GTP-Binding Proteins / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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09PRE2170054//PHS HHS; P01 CA095426/CA/NCI NIH HHS; R01 AI059406/AI/NIAID NIH HHS; T32 60013191//PHS HHS |
| Chemical | |
Reg. No./Substance:
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0/GRB2 Adaptor Protein; 0/GRB2 protein, human; 0/Guanine Nucleotide Dissociation Inhibitors; 0/Receptors, IgG; 0/Shc Signaling Adaptor Proteins; 0/Tumor Suppressor Proteins; 133312-85-3/rho guanine nucleotide dissociation inhibitors; 147-85-3/Proline; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC 3.1.3.56/inositol-1,4,5-trisphosphate 5-phosphatase; EC 3.6.5.2/rac GTP-Binding Proteins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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