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Publication : The phagosomal proteome in interferon-gamma-activated macrophages.

First Author  Trost M Year  2009
Journal  Immunity Volume  30
Issue  1 Pages  143-54
PubMed ID  19144319 Mgi Jnum  J:143718
Mgi Id  MGI:3828867 Doi  10.1016/j.immuni.2008.11.006
Citation  Trost M, et al. (2009) The phagosomal proteome in interferon-gamma-activated macrophages. Immunity 30(1):143-54
abstractText  The ability of macrophages to clear pathogens and elicit a sustained immune response is regulated by various cytokines, including interferon-gamma (IFN-gamma). To investigate the molecular mechanisms by which IFN-gamma modulates phagosome functions, we profiled the changes in composition, abundance, and phosphorylation of phagosome proteins in resting and activated macrophages by using quantitative proteomics and bioinformatics approaches. We identified 2415 phagosome proteins together with 2975 unique phosphorylation sites with a high level of sensitivity. Using network analyses, we determined that IFN-gamma delays phagosomal acquisition of lysosomal hydrolases and peptidases for the gain of antigen presentation. Furthermore, this gain in antigen presentation is dependent on phagosomal networks of the actin cytoskeleton and vesicle-trafficking proteins, as well as Src kinases and calpain proteases. Major histocompatibility complex class I antigen-presentation assays validated the molecular participation of these networks in the enhanced capacity of IFN-gamma-activated macrophages to crosspresent exogenous antigens to CD8(+) T cells.
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