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-Structure paper
タイトル | Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms. |
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ジャーナル・号・ページ | Biol Open, Vol. 9, Issue 7, Year 2020 |
掲載日 | 2020年7月31日 |
著者 | Ottilie von Loeffelholz / Andrew Purkiss / Luyan Cao / Svend Kjaer / Naoko Kogata / Guillaume Romet-Lemonne / Michael Way / Carolyn A Moores / |
PubMed 要旨 | The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce ...The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce a family of Arp2/3 complexes with different properties that may be suited to different physiological contexts. To shed light on how isoform diversification affects Arp2/3 function, we determined a 4.2 Å resolution cryo-EM structure of the most active human Arp2/3 complex containing ARPC1B and ARPC5L, and compared it with the structure of the least active ARPC1A-ARPC5-containing complex. The architecture of each isoform-specific Arp2/3 complex is the same. Strikingly, however, the N-terminal half of ARPC5L is partially disordered compared to ARPC5, suggesting that this region of ARPC5/ARPC5L is an important determinant of complex activity. Confirming this idea, the nucleation activity of Arp2/3 complexes containing hybrid ARPC5/ARPC5L subunits is higher when the ARPC5L N-terminus is present, thereby providing insight into activity differences between the different Arp2/3 complexes. |
リンク | Biol Open / PubMed:32661131 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.2 - 4.5 Å |
構造データ | EMDB-10959, PDB-6yw6: EMDB-10960, PDB-6yw7: |
化合物 | ChemComp-ATP: |
由来 |
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キーワード | STRUCTURAL PROTEIN / Cytoskeleton |