Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation

Vikas A. Tillu, James Rae, Ya Gao, Nicholas Ariotti, Matthias Floetenmeyer, Oleksiy Kovtun, Kerrie-Ann McMahon, Natasha Chaudhary, Robert G. Parton () and Brett M. Collins ()
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Vikas A. Tillu: The University of Queensland
James Rae: The University of Queensland
Ya Gao: The University of Queensland
Nicholas Ariotti: The University of New South Wales
Matthias Floetenmeyer: Centre for Microscopy and Microanalysis
Oleksiy Kovtun: The University of Queensland
Kerrie-Ann McMahon: The University of Queensland
Natasha Chaudhary: The University of Queensland
Robert G. Parton: The University of Queensland
Brett M. Collins: The University of Queensland

Nature Communications, 2021, vol. 12, issue 1, 1-18

Abstract: Abstract Caveolae are spherically shaped nanodomains of the plasma membrane, generated by cooperative assembly of caveolin and cavin proteins. Cavins are cytosolic peripheral membrane proteins with negatively charged intrinsically disordered regions that flank positively charged α-helical regions. Here, we show that the three disordered domains of Cavin1 are essential for caveola formation and dynamic trafficking of caveolae. Electrostatic interactions between disordered regions and α-helical regions promote liquid-liquid phase separation behaviour of Cavin1 in vitro, assembly of Cavin1 oligomers in solution, generation of membrane curvature, association with caveolin-1, and Cavin1 recruitment to caveolae in cells. Removal of the first disordered region causes irreversible gel formation in vitro and results in aberrant caveola trafficking through the endosomal system. We propose a model for caveola assembly whereby fuzzy electrostatic interactions between Cavin1 and caveolin-1 proteins, combined with membrane lipid interactions, are required to generate membrane curvature and a metastable caveola coat.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21035-4

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DOI: 10.1038/s41467-021-21035-4

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