Structure and assembly of CAV1 8S complexes revealed by single particle electron microscopy.

Autor: Han B; Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA, USA.; Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, USA., Porta JC; Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA., Hanks JL; Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA., Peskova Y; Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA, USA.; Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, USA., Binshtein E; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA., Dryden K; Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, USA., Claxton DP; Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN, USA., Mchaourab HS; Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN, USA., Karakas E; Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN, USA., Ohi MD; Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA. mohi@umich.edu akk7hp@virginia.edu.; Department of Cell and Developmental Biology, University of Michigan School of Medicine, Ann Arbor, MI, USA., Kenworthy AK; Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA, USA. mohi@umich.edu akk7hp@virginia.edu.; Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA, USA.
Jazyk: angličtina
Zdroj: Science advances [Sci Adv] 2020 Dec 02; Vol. 6 (49). Date of Electronic Publication: 2020 Dec 02 (Print Publication: 2020).
DOI: 10.1126/sciadv.abc6185
Abstrakt: Highly stable oligomeric complexes of the monotopic membrane protein caveolin serve as fundamental building blocks of caveolae. Current evidence suggests these complexes are disc shaped, but the details of their structural organization and how they assemble are poorly understood. Here, we address these questions using single particle electron microscopy of negatively stained recombinant 8S complexes of human caveolin 1. We show that 8S complexes are toroidal structures ~15 nm in diameter that consist of an outer ring, an inner ring, and central protruding stalk. Moreover, we map the position of the N and C termini and determine their role in complex assembly, and visualize the 8S complexes in heterologous caveolae. Our findings provide critical insights into the structural features of 8S complexes and allow us to propose a model for how these highly stable membrane-embedded complexes are generated.
(Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).)
Databáze: MEDLINE