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- W2896975880 abstract "In addition to its essential functions within the cytoskeleton, actin also localizes to the cell nucleus, where it is linked to many important nuclear processes from gene expression to maintenance of genomic integrity. However, the molecular mechanisms by which actin operates in the nucleus remain poorly understood. Here we have used two complementary mass spectrometry (MS) techniques, AP-MS and BioID, to identify binding partners for nuclear actin. Common high-confidence interactions highlight the role of actin in chromatin remodeling complexes and identify the hATAC histone modifier as a novel actin-containing nuclear complex. Actin binds directly to the hATAC subunit KAT14, and modulates its histone acetyl transferase activity in vitro and in cells. Transient interactions detected by BioID link actin to several steps of transcription as well as to RNA processing. Alterations in nuclear actin levels disturb alternative splicing in minigene assays, likely by affecting transcription elongation rate. This interactome analysis thus identifies both novel direct binding partners and functional roles for nuclear actin, as well as forms a platform for further mechanistic studies on how actin operates during essential nuclear processes." @default.
- W2896975880 created "2018-10-26" @default.
- W2896975880 creator A5011142044 @default.
- W2896975880 creator A5022415698 @default.
- W2896975880 creator A5040917201 @default.
- W2896975880 creator A5060662450 @default.
- W2896975880 creator A5070893457 @default.
- W2896975880 creator A5080784387 @default.
- W2896975880 creator A5088559880 @default.
- W2896975880 date "2019-01-01" @default.
- W2896975880 modified "2023-10-16" @default.
- W2896975880 title "Nuclear actin interactome analysis links actin to KAT14 histone acetyl transferase and mRNA splicing" @default.
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