In:
Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 21, No. 5 ( 2010-03), p. 811-820
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, β-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 β-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 β-actin occupancy and the recruitment of RNA polymerase II at six selected target genes, and β-actin knockdown decreases the mRNA expression levels of these target genes induced by PMA. We further show that nuclear β-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 β-actin is involved in transcriptional regulation during macrophage-like differentiation of HL-60 cells.
Type of Medium:
Online Resource
ISSN:
1059-1524
,
1939-4586
DOI:
10.1091/mbc.e09-06-0534
Language:
English
Publisher:
American Society for Cell Biology (ASCB)
Publication Date:
2010
detail.hit.zdb_id:
1098979-1
detail.hit.zdb_id:
1474922-1
SSG:
12
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