NDLI: Adaptor protein SLAT modulates Fcgamma receptor-mediated phagocytosis in murine macrophages.

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Adaptor protein SLAT modulates Fcgamma receptor-mediated phagocytosis in murine macrophages.

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Adaptor protein SLAT modulates Fcgamma receptor-mediated phagocytosis in murine macrophages.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mehta, Harshini Bécart, Stephane Altman, Amnon Coggeshall, K. Mark Glogauer, Michael
Description	Author Affiliation: Mehta H ( Program in Immunobiology and Cancer, Oklahoma Medical Research Foundation, and Department of Cell Biology, University of Oklahoma, Oklahoma City, Oklahoma 73104, USA.)
Abstract	SLAT (SWAP-70-like adaptor protein of T cells) is an adaptor protein expressed in cells of the hematopoietic system. SLAT interacts with and alters the function of small GTPase Rac1 in fibroblasts. In these nonhematopoietic models, the SLAT-Rac interaction leads to changes in F-actin and causes cytoskeletal reorganization. In T cells, SLAT expression regulates the development of T helper cells through Cdc42- and Rac1-mediated activation of the NF-AT transcription factor. Here we show that SLAT is expressed in macrophages. Overexpression of SLAT in a macrophage cell line inhibits the IgG Fcgamma receptor-mediated phagocytic ability of THP1 cells. In bone marrow-derived macrophages, SLAT protein is recruited to the early phagosomes formed via Fcgamma receptor engagement. SLAT recruitment to the phagosome was most efficient when the macrophages express at least one isoform of Rac (Rac1 or Rac2), because SLAT recruitment was reduced in macrophages of Rac-deficient mice. Macrophages derived from animals lacking SLAT show an elevation in the rate of Fcgamma receptor-mediated phagocytosis. The absence of SLAT is associated with an increase in the amount of F-actin formed around these phagosomes as well as an increase in the amount of Rac1 protein recruited to the phagosome. Our results suggest that SLAT acts as a gatekeeper for the amount of Rac recruited to the phagosomes formed by Fcgamma receptor engagement and thus is able to regulate F-actin re-organization and consequently phagocytosis.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	18
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA-Binding Proteins Metabolism Macrophages Nuclear Proteins Phagocytosis Physiology Phagosomes Receptors, IgG Actins Genetics Animals Cell Line Cytoskeleton Guanine Nucleotide Exchange Factors Mice Mice, Knockout NFATC Transcription Factors Neuropeptides T-Lymphocytes Cdc42 GTP-Binding Protein Rac GTP-Binding Proteins Rac1 GTP-Binding Protein Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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