Imperial College London
Professor Michael Way

ProfessorMichaelWay

Faculty of Medicine, Department of Infectious Disease

Professor of Virology
 
 
 
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Contact

 

+44 (0)20 3796 2068michael.way1 Website

 
 
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Location

 

Francis Crick InstituteThe Francis Crick Institute

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Summary

 

Publications

Citation

BibTex format

@article{von:2020:10.1242/bio.054304,
author = {von, Loeffelholz O and Purkiss, A and Cao, L and Kjaer, S and Kogata, N and Romet-Lemonne, G and Way, M and Moores, CA},
doi = {10.1242/bio.054304},
journal = {Biol Open},
title = {Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms.},
url = {http://dx.doi.org/10.1242/bio.054304},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - von,Loeffelholz O
AU  - Purkiss,A
AU  - Cao,L
AU  - Kjaer,S
AU  - Kogata,N
AU  - Romet-Lemonne,G
AU  - Way,M
AU  - Moores,CA
DO  - 10.1242/bio.054304
PY  - 2020///
TI  - Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms.
T2  - Biol Open
UR  - http://dx.doi.org/10.1242/bio.054304
UR  - https://www.ncbi.nlm.nih.gov/pubmed/34004781
ER  -
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