Structure and dynamics of ESCRT-III membrane remodeling proteins by high-speed atomic force microscopy.

Autor:	Jukic N; Physiology, Biophysics and Systems Biology Graduate Program, Weill Cornell Medicine, New York, New York, USA., Perrino AP; Department of Anesthesiology, Weill Cornell Medicine, New York, New York, USA., Redondo-Morata L; CNRS, Inserm, Institut Pasteur de Lille, U1019-UMR9017-CIIL-Centre d'Infection et d'Immunité de Lille, Université de Lille, Lille, France., Scheuring S; Department of Anesthesiology, Weill Cornell Medicine, New York, New York, USA; Department of Physiology and Biophysics, Weill Cornell Medicine, New York, New York, USA; Kavli Institute at Cornell for Nanoscale Science, Cornell University, Ithaca, New York, USA. Electronic address: sis2019@med.cornell.edu.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2023 Apr; Vol. 299 (4), pp. 104575. Date of Electronic Publication: 2023 Mar 02.
DOI:	10.1016/j.jbc.2023.104575
Abstrakt:	Endosomal sorting complex required for transport (ESCRT) proteins assemble on the cytoplasmic leaflet of membranes and remodel them. ESCRT is involved in biological processes where membranes are bent away from the cytosol, constricted, and finally severed, such as in multivesicular body formation (in the endosomal pathway for protein sorting) or abscission during cell division. The ESCRT system is hijacked by enveloped viruses to allow buds of nascent virions to be constricted, severed, and released. ESCRT-III proteins, the most downstream components of the ESCRT system, are monomeric and cytosolic in their autoinhibited conformation. They share a common architecture, a four-helix bundle with a fifth helix that interacts with this bundle to prevent polymerizing. Upon binding to negatively charged membranes, the ESCRT-III components adopt an activated state that allows them to polymerize into filaments and spirals and to interact with the AAA-ATPase Vps4 for polymer remodeling. ESCRT-III has been studied with electron microscopy and fluorescence microscopy; these methods provided invaluable information about ESCRT assembly structures or their dynamics, respectively, but neither approach provides detailed insights into both aspects simultaneously. High-speed atomic force microscopy (HS-AFM) has overcome this shortcoming, providing movies at high spatiotemporal resolution of biomolecular processes, significantly increasing our understanding of ESCRT-III structure and dynamics. Here, we review the contributions of HS-AFM in the analysis of ESCRT-III, focusing on recent developments of nonplanar and deformable HS-AFM supports. We divide the HS-AFM observations into four sequential steps in the ESCRT-III lifecycle: (1) polymerization, (2) morphology, (3) dynamics, and (4) depolymerization. Competing Interests: Conflict of interest The authors declare no conflict of interest with the contents of this article. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu