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• W2112716407 abstract "Studies have shown that nuclear translocation of actin occurs under certain conditions of cellular stress; however, the functional significance of actin import remains unclear. Here, we demonstrate that during the phorbol 12-myristate 13-acetate (PMA)-induced differentiation of HL-60 cells toward macrophages, beta-actin translocates from the cytoplasm to the nucleus and that this process is dramatically inhibited by pretreatment with p38 mitogen-activated protein kinase inhibitors. Using chromatin immunoprecipitation-on-chip assays, the genome-wide maps of beta-actin binding to gene promoters in response to PMA treatment is analyzed in HL-60 cells. A gene ontology-based analysis shows that the identified genes belong to a broad spectrum of functional categories such as cell growth and differentiation, signal transduction, response to external stimulus, ion channel activity, and immune response. We also demonstrate a correlation between beta-actin occupancy and the recruitment of RNA polymerase II at six selected target genes, and beta-actin knockdown decreases the mRNA expression levels of these target genes induced by PMA. We further show that nuclear beta-actin is required for PMA-induced transactivation of one target gene, solute carrier family 11 member 1, which is important for macrophage activation. Our data provide novel evidence that nuclear accumulation of beta-actin is involved in transcriptional regulation during macrophage-like differentiation of HL-60 cells." @default.
• W2112716407 created "2016-06-24" @default.
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• W2112716407 date "2010-03-01" @default.
• W2112716407 modified "2023-10-13" @default.
• W2112716407 title "Nuclear Translocation of β-Actin Is Involved in Transcriptional Regulation during Macrophage Differentiation of HL-60 Cells" @default.
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• W2112716407 doi "https://doi.org/10.1091/mbc.e09-06-0534" @default.
• W2112716407 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2828967" @default.
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