Nuclear actin interactome analysis links actin to KAT14 histone acetyl transferase and mRNA splicing

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Viita , T , Kyheroinen , S , Prajapati , B , Virtanen , J , Frilander , M J , Varjosalo , M & Vartiainen , M K 2019 , ' Nuclear actin interactome analysis links actin to KAT14 histone acetyl transferase and mRNA splicing ' , Journal of Cell Science , vol. 132 , no. 8 , 226852 . https://doi.org/10.1242/jcs.226852

Title: Nuclear actin interactome analysis links actin to KAT14 histone acetyl transferase and mRNA splicing
Author: Viita, Tiina; Kyheroinen, Salla; Prajapati, Bina; Virtanen, Jori; Frilander, Mikko J.; Varjosalo, Markku; Vartiainen, Maria K.
Contributor: University of Helsinki, Institute of Biotechnology
University of Helsinki, Institute of Biotechnology
University of Helsinki, Institute of Biotechnology
University of Helsinki, Institute of Biotechnology
University of Helsinki, University Management
University of Helsinki, University Management
University of Helsinki, Institute of Biotechnology
Date: 2019-04
Language: eng
Number of pages: 16
Belongs to series: Journal of Cell Science
ISSN: 0021-9533
URI: http://hdl.handle.net/10138/304973
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 histone-modifying complex human Ada-Two-A-containing (hATAC) 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 through 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 the 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. This article has an associated First Person interview with the first author of the paper.
Subject: hATAC
Actin
Nucleus
Transcription
Histone acetyl transferase
Pre-mRNA processing
LEUCINE-RICH REPEAT
ACETYLTRANSFERASE COMPLEX
AFFINITY PURIFICATION
CRYSTAL-STRUCTURE
HNRNP-U
F-ACTIN
PROTEIN
CHROMATIN
TRANSCRIPTION
GENE
1182 Biochemistry, cell and molecular biology
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