Evidence map›Paper›PMID 33591770›Full record

ArticleThe journal of physical chemistry letters2021

FAM134B-RHD Protein Clustering Drives Spontaneous Budding of Asymmetric Membranes.

Marc Siggel, Ramachandra M Bhaskara, Melanie K Moesser, Ivan D Ikić, Gerhard Hummer

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
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  9. Intrinsically disordered region amplifies membrane remodeling to augment selective ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Making the cut: Multiscale simulation of membrane remodeling.Current opinion in structural biology · 2024
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Molecular Dynamics Simulations of Curved Lipid Membranes.International journal of molecular sciences · 2022
    Review
  19. Review
  20. ER remodeling via ER-phagy.Molecular cell · 2022
    Review
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

5 authors.

Marc SiggelDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0003-3393-4988
Ramachandra M BhaskaraDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-7742-0391
Melanie K MoesserDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0001-9661-0695
Ivan D IkićInstitute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0001-8156-9511
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438 Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0001-7768-746X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Living cells constantly remodel the shape of their lipid membranes. In the endoplasmic reticulum (ER), the reticulon homology domain (RHD) of the reticulophagy regulator 1 (RETR1/FAM134B) forms dense autophagic puncta that are associated with membrane removal by ER-phagy. In molecular dynamics (MD) simulations, we find that FAM134B-RHD spontaneously forms clusters, driven in part by curvature-mediated attractions. At a critical size, as in a nucleation process, the FAM134B-RHD clusters induce the formation of membrane buds. The kinetics of budding depends sensitively on protein concentration and bilayer asymmetry. Our MD simulations shed light on the role of FAM134B-RHD in ER-phagy and show that membrane asymmetry can be used to modulate the kinetic barrier for membrane remodeling.

Indexed as

AutophagyEndoplasmic ReticulumIntracellular Signaling Peptides and ProteinsKineticsLipid BilayersMembrane ProteinsMolecular Dynamics SimulationProtein BindingProtein ConformationProtein DomainsProtein MultimerizationIntracellular Signaling Peptides and ProteinsLipid BilayersMembrane ProteinsRETREG1 protein, human

Identifiers

PMID33591770
PMCPMC8028312

What OpenQuestion holds

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Registered trials

None linked

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.