Parcs is a dual regulator of cell proliferation and Apaf-1 function
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Here we identify a novel protein, named Parcs for pro-apoptotic protein required for cell survival, that is involved in both cell cycle progression and apoptosis. Parcs interacted with Apaf-1 by binding to the oligomerization domain of Apaf-1. Apaf-1-mediated activation of caspase-9 and caspase-3 was markedly decreased in a cytosolic fraction isolated from HeLa cells with reduced parcs expression. Interestingly, parcs deficiency blocked cell proliferation in non-tumorigenic cells but not in multiple tumor cell lines. In MCF-10A cells, parcs deficiency led to early G1 arrest. Conditional inactivation of parcs in genetically modified primary mouse embryonic fibroblasts using the Cre-LoxP system also resulted in the inhibition of cell proliferation. We conclude that Parcs may define a molecular checkpoint in the control of cell proliferation for normal cells that is lost in tumor cells. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
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Cell culture; Cell death; Cell proliferation; Cells; Oligomerization; Tumors; Apoptosis; Apoptotic proteins; Caspase; Caspase-3; Cell cycles; Cell survivals; Cytosolic fractions; Do-mains; Genetically modified; Mouse embryonic fibroblasts; Novel proteins; Tumor cell lines; Tumor cells; Tumorigenic cells; Cytology; apoptotic protease activating factor 1; caspase 3; caspase 9; cell protein; cre recombinase; pro apoptotic protein; protein parcs; unclassified drug; Apaf1 protein, mouse; Casp3 protein, mouse; cell cycle protein; animal cell; apoptosis; article; cell cycle arrest; cell cycle G1 phase; cell cycle G2 phase; cell cycle M phase; cell cycle S phase; cell proliferation; cell survival; controlled study; enzyme activation; fibroblast; HeLa cell; human; human cell; LoxP site; mouse; nonhuman; oligomerization; priority journal; protein analysis; protein expression; protein function; protein isolation; protein protein interaction; animal; cell cycle G1 phase; genetics; metabolism; mouse mutant; physiology; protein tertiary structure; Animals; Apoptotic Protease-Activating Factor 1; Caspase 3; Caspase 9; Cell Cycle Proteins; G1 Phase; Hela Cells; Humans; Mice; Mice, Knockout; Protein Structure, Tertiary
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