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Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin

Tutkimustuotosvertaisarvioitu

Standard

Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. / Kotila, Tommi; Wioland, Hugo; Enkavi, Giray; Kogan, Konstantin; Vattulainen, Ilpo; Jégou, Antoine; Romet-Lemonne, Guillaume; Lappalainen, Pekka.

julkaisussa: Nature Communications, Vuosikerta 10, Nro 1, 01.11.2019.

Tutkimustuotosvertaisarvioitu

Harvard

Kotila, T, Wioland, H, Enkavi, G, Kogan, K, Vattulainen, I, Jégou, A, Romet-Lemonne, G & Lappalainen, P 2019, 'Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin', Nature Communications, Vuosikerta. 10, Nro 1. https://doi.org/10.1038/s41467-019-13213-2

APA

Kotila, T., Wioland, H., Enkavi, G., Kogan, K., Vattulainen, I., Jégou, A., ... Lappalainen, P. (2019). Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Nature Communications, 10(1). https://doi.org/10.1038/s41467-019-13213-2

Vancouver

Kotila T, Wioland H, Enkavi G, Kogan K, Vattulainen I, Jégou A et al. Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Nature Communications. 2019 marras 1;10(1). https://doi.org/10.1038/s41467-019-13213-2

Author

Kotila, Tommi ; Wioland, Hugo ; Enkavi, Giray ; Kogan, Konstantin ; Vattulainen, Ilpo ; Jégou, Antoine ; Romet-Lemonne, Guillaume ; Lappalainen, Pekka. / Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin. Julkaisussa: Nature Communications. 2019 ; Vuosikerta 10, Nro 1.

Bibtex - Lataa

@article{260ba52dcf4a464ba8bdbd4c9dd51e04,
title = "Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin",
abstract = "The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes.",
author = "Tommi Kotila and Hugo Wioland and Giray Enkavi and Konstantin Kogan and Ilpo Vattulainen and Antoine J{\'e}gou and Guillaume Romet-Lemonne and Pekka Lappalainen",
note = "EXT={"}Enkavi, Giray{"}",
year = "2019",
month = "11",
day = "1",
doi = "10.1038/s41467-019-13213-2",
language = "English",
volume = "10",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin

AU - Kotila, Tommi

AU - Wioland, Hugo

AU - Enkavi, Giray

AU - Kogan, Konstantin

AU - Vattulainen, Ilpo

AU - Jégou, Antoine

AU - Romet-Lemonne, Guillaume

AU - Lappalainen, Pekka

N1 - EXT="Enkavi, Giray"

PY - 2019/11/1

Y1 - 2019/11/1

N2 - The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes.

AB - The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes.

U2 - 10.1038/s41467-019-13213-2

DO - 10.1038/s41467-019-13213-2

M3 - Article

VL - 10

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

ER -