2YJF

Oligomeric assembly of actin bound to MRTF-A

Summary for 2YJF

• Entry DOI: 10.2210/pdb2yjf/pdb
• Related: 1ALM 1ATN 1EQY 1ESV 1H1V 1IJJ 1J6Z 1KXP 1LCU 1LOT 1M8Q 1MA9 1MVW 1NWK 1O18 1O19 1O1A 1O1B 1O1C 1O1D 1O1E 1O1F 1O1G 1P8Z 1QZ5 1QZ6 1RDW 1RFQ 1RGI 1S22 1SQK 1T44 1UY5 1WUA 1Y64 2A3Z 2A40 2A41 2A42 2A5X 2ASM 2ASO 2ASP 2D1K 2FF3 2FF6 2FXU 2V51 2V52 2VCP 2VYP 2W49 2W4U 2Y83 2YJE
• Descriptor: ACTIN, ALPHA SKELETAL MUSCLE, MKL/MYOCARDIN-LIKE PROTEIN 1, LATRUNCULIN B, ... (5 entities in total)
• Functional Keywords: motor protein
• Biological source: ORYCTOLAGUS CUNICULUS (RABBIT); More
• Cellular location: Cytoplasm, cytoskeleton: P68135; Cytoplasm: Q8K4J6
• Total number of polymer chains: 6
• Total formula weight: 229833.59

Authors

Mouilleron, S.,Langer, C.A.,Guettler, S.,McDonald, N.Q.,Treisman, R. (deposition date: 2011-05-19, release date: 2011-07-06, Last modification date: 2023-12-20)

Primary citation

Mouilleron, S.,Langer, C.A.,Guettler, S.,McDonald, N.Q.,Treisman, R.
Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator.
Sci Signal, 4:ra40-ra40, 2011

PubMed Abstract: 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.

PubMed: 21673315
DOI: 10.1126/scisignal.2001750

Experimental method

X-RAY DIFFRACTION (3.5 Å)