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The functional association between filamin B (FLNB) and histone deacetylase 7 (HDAC7) in endothelial cells (ECs)
Author(s) -
Su YuTing,
Gao Chengzhuo,
Liu Yu,
Tempst Paul,
ErdjumentBromage Hediye,
Kao HungYing
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.561.14
Histone deacetylase 7 (HDAC7) is a transcriptional corepressor that plays a critical role in the maintenance of blood vessel integrity, in part, through repression of myocyte enhancer factor‐2 (MEF2) target genes expression. We have identified the actin‐binding protein, filamin B (FLNB) as a component of HDAC7 cytoplasmic complexes. We demonstrate that FLNB regulates vascular endothelial growth factor (VEGF)‐induced cytoplasmic sequestration of HDAC7, MEF2 target gene expression and cell permeability in human primary endothelial cells (ECs). Protein‐protein interaction studies indicate that the interaction between HDAC7 and FLNB requires post‐translational modifications and that calcium/calmodulin‐dependent protein kinase (CaMK) enhances this interaction. Taken together, we have identified FLNB as a novel HDAC7 interacting protein that has an essential role in VEGF signaling in ECs.