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Nat Commun. 2018 Dec 5;9(1):5187. doi: 10.1038/s41467-018-07586-z.

ATP-dependent membrane remodeling links EHD1 functions to endocytic recycling.

Author information

1
Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411008, Maharashtra, India.
2
Indian Institute of Science Education and Research, Sector 81, S.A.S Nagar, Mohali, 140306, Punjab, India.
3
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, Karnataka, India.
4
Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411008, Maharashtra, India. pucadyil@iiserpune.ac.in.

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 protein1 (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.

PMID:
30518883
PMCID:
PMC6281616
DOI:
10.1038/s41467-018-07586-z
[Indexed for MEDLINE]
Free PMC Article

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