Evidence map›Paper›PMID 30518883›Full record

ArticleNature communications2018

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

Raunaq Deo, Manish S Kushwah, Sukrut C Kamerkar, Nagesh Y Kadam, Srishti Dar, Kavita Babu, Anand Srivastava, Thomas J Pucadyil

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed.

  1. Article
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  7. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Review
  15. Dynamics of membrane tubulation coupled with fission by a two-component module.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Raunaq DeoIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411008, Maharashtra, India.ORCID http://orcid.org/0000-0002-5915-0826
Manish S KushwahIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411008, Maharashtra, India.ORCID http://orcid.org/0000-0001-5088-0403
Sukrut C KamerkarIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411008, Maharashtra, India.
Nagesh Y KadamIndian Institute of Science Education and Research, Sector 81, S.A.S Nagar, Mohali, 140306, Punjab, India.
Srishti DarIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411008, Maharashtra, India.
Kavita BabuIndian Institute of Science Education and Research, Sector 81, S.A.S Nagar, Mohali, 140306, Punjab, India.
Anand SrivastavaMolecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, Karnataka, India.ORCID http://orcid.org/0000-0002-2757-1511
Thomas J PucadyilIndian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune, 411008, Maharashtra, India. pucadyil@iiserpune.ac.in.ORCID http://orcid.org/0000-0002-2907-9889

Funding

DBT-Wellcome Trust India Alliance IA/I/12/1/500516DBT-Wellcome Trust India Alliance IA/S/16/2/502708Wellcome Trust
6 · The paper itself

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.

Indexed as

EndocytosisAdenosine TriphosphateAmino Acid MotifsAnimalsBiological TransportCaenorhabditis elegansCaenorhabditis elegans ProteinsCell MembraneHydrolysisSequence DeletionAdenosine TriphosphateCaenorhabditis elegans ProteinsRME-1 protein, C elegans

Identifiers

PMID30518883
PMCPMC6281616

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LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.