2yjf

Oligomeric assembly of actin bound to MRTF-A

spinqualitylabelsall models 2yjf, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yjf is a 6 chain structure with sequence from European rabbit and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, LAB, MG Related: 1lcu, 2a42, 2aso, 1ijj, 1wua, 1o1a, 1m8q, 1o18, 1uy5, 1rfq, 1ma9, 2d1k, 2w49, 1rdw, 2y83, 1o1b, 1o1d, 2a40, 2a5x, 1qz5, 2v52, 1nwk, 1j6z, 1sqk, 1atn, 1s22, 1t44, 2ff3, 1mvw, 1eqy, 2ff6, 1o1f, 2fxu, 1kxp, 2v51, 2asp, 1rgi, 1o19, 1y64, 2yje, 1alm, 1o1e, 1p8z, 1esv, 1o1c, 1h1v, 2vcp, 1o1g, 2a3z, 1lot, 2a41, 2asm, 1qz6, 2vyp, 2w4u Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [MKL1_MOUSE] Transcriptional coactivator of serum response factor (SRF) with the potential to modulate SRF target genes. Suppresses TNF-induced cell death by inhibiting activation of caspases; its transcriptional activity is indispensable for the antiapoptotic function. It may up-regulate antiapoptotic molecules, which in turn inhibit caspase activation. Publication Abstract from PubMed Subcellular localization of the actin-binding transcriptional coactivator MRTF-A is controlled by its interaction with monomeric actin (G-actin). Signal-induced decreases in G-actin concentration reduce MRTF-A nuclear export, leading to its nuclear accumulation, whereas artificial increases in G-actin concentration in resting cells block MRTF-A nuclear import, retaining it in the cytoplasm. This regulation is dependent on three actin-binding RPEL motifs in the regulatory domain of MRTF-A. We describe the structures of pentavalent and trivalent G-actin*RPEL domain complexes. In the pentavalent complex, each RPEL motif and the two intervening spacer sequences bound an actin monomer, forming a compact assembly. In contrast, the trivalent complex lacked the C-terminal spacer- and RPEL-actins, both of which bound only weakly in the pentavalent complex. Cytoplasmic localization of MRTF-A in unstimulated fibroblasts also required binding of G-actin to the spacer sequences. The bipartite MRTF-A nuclear localization sequence was buried in the pentameric assembly, explaining how increases in G-actin concentration prevent nuclear import of MRTF-A. Analyses of the pentavalent and trivalent complexes show how actin loads onto the RPEL domain and reveal a molecular mechanism by which actin can control the activity of one of its binding partners. Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator.,Mouilleron S, Langer CA, Guettler S, McDonald NQ, Treisman R Sci Signal. 2011 Jun 14;4(177):ra40. PMID:21673315 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin Transcriptional activator

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