Publication Date:
2013-04-06
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baarlink, Christian -- Wang, Haicui -- Grosse, Robert -- New York, N.Y. -- Science. 2013 May 17;340(6134):864-7. doi: 10.1126/science.1235038. Epub 2013 Apr 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Pharmacology, Biochemical-Pharmacological Center, University of Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23558171" target="_blank"〉PubMed〈/a〉
Keywords:
Actins/*metabolism
;
Animals
;
Carrier Proteins/*metabolism
;
Cell Nucleus/*metabolism
;
HeLa Cells
;
Humans
;
Intracellular Signaling Peptides and Proteins/*metabolism
;
*Metabolic Networks and Pathways
;
Mice
;
Microtubule-Associated Proteins/*metabolism
;
NADPH Dehydrogenase/*metabolism
;
NIH 3T3 Cells
;
Nuclear Localization Signals/metabolism
;
Polymerization
;
Serum/metabolism
;
Serum Response Factor/*agonists
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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