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Nuclear Actin Regulates Dynamic Subcellular Localization and Activity of the SRF Cofactor MAL
Oleh:
Vartiainen, Maria K.
;
Guettler, Sebastian
;
Larijani, Banafshe
;
Treisman, Richard
Jenis:
Article from Bulletin/Magazine
Dalam koleksi:
SCIENCE (keterangan: ada di Proquest) vol. 316 no. 5832 (Jun. 2007)
,
page 1749.
Ketersediaan
Perpustakaan FK
Nomor Panggil:
S01.K.2007.06
Non-tandon:
1 (dapat dipinjam: 0)
Tandon:
tidak ada
Lihat Detail Induk
Isi artikel
Actin, which is best known as a cytoskeletal component, also participates in the control of gene expression. We report a function of nuclear actin in the regulation of MAL, a coactivator of the transcription factor serum response factor (SRF). MAL, which binds monomeric actin, is cytoplasmic in many cells but accumulates in the nucleus upon serum-induced actin polymerization. MAL rapidly shuttles between cytoplasm and nucleus in unstimulated cells. Serum stimulation effectively blocks MAL nuclear export, which requires MAL-actin interaction. Nuclear MAL binds SRF target genes but remains inactive unless actin binding is disrupted. Fluorescence resonance energy transfer analysis demonstrates that the MAL-actin interaction responds to extracellular signals. Serum-induced signaling is thus communicated to nuclear actin to control a transcriptional regulator.
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