Abstract：
:Nuclear actin has been elusive due to the lack of knowledge about molecular mechanisms. From actin-containing chromatin remodeling complexes, we discovered an arginine mono-methylation mark on an evolutionarily conserved R256 residue of actin (R256me1). Actin R256 mutations in yeast affect nuclear functions and cause diseases in human. Interestingly, we show that an antibody specific for actin R256me1 preferentially stains nuclear actin over cytoplasmic actin in yeast, mouse, and human cells. We also show that actin R256me1 is regulated by protein arginine methyl transferase-5 (PRMT5) in HEK293 cells. A genome-wide survey of actin R256me1 mark provides a landscape for nuclear actin correlated with transcription. Further, gene expression and protein interaction studies uncover extensive correlations between actin R256me1 and active transcription. The discovery of actin R256me1 mark suggests a fundamental mechanism to distinguish nuclear actin from cytoplasmic actin through post-translational modification (PTM) and potentially implicates an actin PTM mark in transcription and human diseases.
journal_name
Cell Repjournal_title
Cell reportsauthors
Kumar A,Zhong Y,Albrecht A,Sang PB,Maples A,Liu Z,Vinayachandran V,Reja R,Lee CF,Kumar A,Chen J,Xiao J,Park B,Shen J,Liu B,Person MD,Trybus KM,Zhang KYJ,Pugh BF,Kamm KE,Milewicz DM,Shen X,Kapoor Pdoi
10.1016/j.celrep.2020.108172subject
Has Abstractpub_date
2020-09-29 00:00:00pages
108172issue
13issn
2211-1247pii
S2211-1247(20)31161-Xjournal_volume
32pub_type
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