Structural basis of actin monomer re-charging by cyclase-associated protein

Tommi Kotila; Konstantin Kogan; Giray Enkavi; Siyang Guo; Ilpo Vattulainen; Bruce L. Goode; Pekka Lappalainen

doi:10.1038/s41467-018-04231-7

Nature Communications (May 2018)

Structural basis of actin monomer re-charging by cyclase-associated protein

Tommi Kotila,
Konstantin Kogan,
Giray Enkavi,
Siyang Guo,
Ilpo Vattulainen,
Bruce L. Goode,
Pekka Lappalainen

Affiliations

Tommi Kotila: Institute of Biotechnology, University of Helsinki
Konstantin Kogan: Institute of Biotechnology, University of Helsinki
Giray Enkavi: Department of Physics, University of Helsinki
Siyang Guo: Department of Biology, Brandeis University
Ilpo Vattulainen: Department of Physics, University of Helsinki
Bruce L. Goode: Department of Biology, Brandeis University
Pekka Lappalainen: Institute of Biotechnology, University of Helsinki

DOI: https://doi.org/10.1038/s41467-018-04231-7
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 12

Abstract

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Depolymerized ADP-actin monomers must be recharged with ATP for new rounds of filament assembly. Here the authors show that cyclase-associated protein (CAP) catalyzes actin nucleotide exchange in vivo and their CAP–actin complex structure reveals the molecular mechanism of CAP-mediated actin nucleotide exchange.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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