Cryo-EM of ADP-Pi-F-actin
Ontology highlight
ABSTRACT:
SUBMITTER: Gregory M. Alushin
PROVIDER: EMPIAR-11129 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Bending forces and nucleotide state jointly regulate F-actin structure.
Reynolds Matthew J MJ Hachicho Carla C Carl Ayala G AG Gong Rui R Alushin Gregory M GM
Nature 20221026 7935
ATP-hydrolysis-coupled actin polymerization is a fundamental mechanism of cellular force generation<sup>1-3</sup>. In turn, force<sup>4,5</sup> and actin filament (F-actin) nucleotide state<sup>6</sup> regulate actin dynamics by tuning F-actin's engagement of actin-binding proteins through mechanisms that are unclear. Here we show that the nucleotide state of actin modulates F-actin structural transitions evoked by bending forces. Cryo-electron microscopy structures of ADP-F-actin and ADP-P<sub> ...[more]
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