Heterocomplex formation by Arp4 and β-actin is involved in the integrity of the Brg1 chromatin remodeling complex

Naoki Nishimoto, Masanori Watanabe, Shinya Watanabe, Nozomi Sugimoto, Takashi Yugawa, Tsuyoshi Ikura, Osamu Koiwai, Tohru Kiyono, Masatoshi Fujita

研究成果: ジャーナルへの寄稿記事

26 引用 (Scopus)

抜粋

Although nuclear actin and Arps (actin-related proteins) are often identified as components of multi-protein chromatin-modifying enzyme complexes, such as chromatin remodeling and histone acetyltransferase (HAT) complexes, their molecular functions still remain largely elusive. Here, we investigated the role of human Arp4 (BAF53, also known as actin-like protein 6A) in Brg1-containing chromatin remodeling complexes. Depletion of Arp4 by RNA interference impaired the integrity of these complexes and accelerated the degradation of Brg1, indicating a crucial role in their maintenance, at least in certain human cell lines. We further found that Arp4 can form a heterocomplex with β-actin. Based on structural similarities between conventional actin and Arp4, and the assumption that actin- Arp4 binding might mimic actin-actin binding, we introduced a series of mutations in Arp4 that might be expected to impair its interaction with β-actin. Some of them indeed caused reduced binding to β-actin. Interestingly, such mutant Arp4 proteins also showed reduced incorporation into Brg1 complexes, and their interaction with Myc-associated complexes as well as Tip60 HAT complexes were also impaired. Based on these findings, we propose that β-actin-Arp4 complex formation might be a crucial feature in some chromatinmodifying enzyme complexes, such as the Brg1 complex.

元の言語英語
ページ(範囲)3870-3882
ページ数13
ジャーナルJournal of Cell Science
125
発行部数16
DOI
出版物ステータス出版済み - 8 15 2012

All Science Journal Classification (ASJC) codes

  • Cell Biology

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