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ATP-dependent membrane remodeling links EHD1 functions to endocytic recycling

Deo, Raunaq and Kushwah, Manish S and Kamerkar, Sukrut C and Kadam, Nagesh Y and Dar, Srishti and Babu, Kavita and Srivastava, Anand and Pucadyil, Thomas J (2018) ATP-dependent membrane remodeling links EHD1 functions to endocytic recycling. In: NATURE COMMUNICATIONS, 9 .

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Official URL: https://doi.org/10.1038/s41467-018-07586-z

Abstract

Endocytic and recycling pathways generate cargo-laden transport carriers by membrane fission. Classical dynamins, which generate transport carriers during endocytosis, constrict and cause fission of membrane tubes in response to GTP hydrolysis. Relatively, less is known about the ATP-binding Eps15-homology domain-containing proteinl (EHD1), a dynamin family member that functions at the endocytic-recycling compartment. Here, we show using cross complementation assays in C. elegans that EHD1's membrane binding and ATP hydrolysis activities are necessary for endocytic recycling. Further, we show that ATP-bound EHD1 forms membrane-active scaffolds that bulge tubular model membranes. ATP hydrolysis promotes scaffold self-assembly, causing the bulge to extend and thin down intermediate regions on the tube. On tubes below 25 nm in radius, such thinning leads to scission. Molecular dynamics simulations corroborate this scission pathway. Deletion of N-terminal residues causes defects in stable scaffolding, scission and endocytic recycling. Thus, ATP hydrolysis-dependent membrane remodeling links EHD1 functions to endocytic recycling.

Item Type: Journal Article
Publication: NATURE COMMUNICATIONS
Publisher: NATURE PUBLISHING GROUP
Additional Information: Copyright of this article belongs to NATURE PUBLISHING GROUP
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 10 Feb 2019 09:44
Last Modified: 10 Feb 2019 09:44
URI: http://eprints.iisc.ac.in/id/eprint/61362

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