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XB-ART-56820
Cells January 1, 2020; 9 (3):

The Actin-Family Protein Arp4 Is a Novel Suppressor for the Formation and Functions of Nuclear F-Actin.

Yamazaki S , Gerhold C , Yamamoto K , Ueno Y , Grosse R , Miyamoto K , Harata M .


Abstract
The crosstalk between actin and actin-related proteins (Arps), namely Arp2 and Arp3, plays a central role in facilitating actin polymerization in the cytoplasm and also in the nucleus. Nuclear F-actin is required for transcriptional regulation, double-strand break repair, and nuclear organization. The formation of nuclear F-actin is highly dynamic, suggesting the involvement of positive and negative regulators for nuclear actin polymerization. While actin assembly factors for nuclear F-actin have been recently described, information about inhibitory factors is still limited. The actin-related protein Arp4 which is predominantly localized in the nucleus, has been previously identified as an integral subunit of multiple chromatin modulation complexes, where it forms a heterodimer with monomeric actin. Therefore, we tested whether Arp4 functions as a suppressor of nuclear F-actin formation. The knockdown of Arp4 (Arp4 KD) led to an increase in nuclear F-actin formation in NIH3T3 cells, and purified Arp4 potently inhibited F-actin formation in mouse nuclei transplanted into Xenopus laevis oocytes. Consistently, Arp4 KD facilitated F-actin-inducible gene expression (e.g., OCT4) and DNA damage repair. Our results suggest that Arp4 has a critical role in the formation and functions of nuclear F-actin.

PubMed ID: 32204557
PMC ID: PMC7140684
Article link: Cells
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: actr2 actr3 axin2 ccnd1 ctnnb1 gdf3 lefty nlrp1 pou5f3.1 sox2 srf tcf7


Article Images: [+] show captions
References [+] :
Baarlink, A transient pool of nuclear F-actin at mitotic exit controls chromatin organization. 2017, Pubmed