Nuclear Actin Network Assembly by Formins Regulates the SRF Coactivator MAL

被引：277

作者：

Baarlink, Christian ^{[1
]}

Wang, Haicui ^{[1
]}

Grosse, Robert ^{[1
]}

机构：

[1] Univ Marburg, Inst Pharmacol, BPC, D-35032 Marburg, Germany

来源：

SCIENCE | 2013年 / 340卷 / 6134期

关键词：

SERUM RESPONSE FACTOR; AUTOREGULATORY DOMAIN; GENE-TRANSCRIPTION; DYNAMICS; MDIA1;

D O I：

10.1126/science.1235038

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Formins are potent activators of actin filament assembly in the cytoplasm. In turn, cytoplasmic actin polymerization can promote release of actin from megakaryocytic acute leukemia (MAL) protein for serum response factor (SRF) transcriptional activity. We found that formins polymerized actin inside the mammalian nucleus to drive serum-dependent MAL-SRF activity. Serum stimulated rapid assembly of actin filaments within the nucleus in a formin-dependent manner. The endogenous formin mDia was regulated with an optogenetic tool, which allowed for photoreactive release of nuclear formin autoinhibition. Activated mDia promoted rapid and reversible nuclear actin network assembly, subsequent MAL nuclear accumulation, and SRF activity. Thus, a dynamic polymeric actin structure within the nucleus is part of the serum response.

引用

页码：864 / 867

页数：4

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