Evidence map›Paper›PMID 32997199›Full record

ArticleCellular and molecular life sciences : CMLS2021

Cooperativity of membrane-protein and protein-protein interactions control membrane remodeling by epsin 1 and affects clathrin-mediated endocytosis.

Benjamin Kroppen, Nelli Teske, King F Yambire, Niels Denkert, Indrani Mukherjee, Daryna Tarasenko, Garima Jaipuria, Markus Zweckstetter, Ira Milosevic, Claudia Steinem and 1 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 29% of its field
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

5 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Generation of nanoscopic membrane curvature for membrane trafficking.Nature reviews. Molecular cell biology · 2023
    Review
  4. Article
  5. 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

11 authors at 6 institutions in 2 countries.

Benjamin KroppenDepartment of Cellular Biochemistry, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.
Nelli TeskeInstitute for Organic and Biomolecular Chemistry, University of Göttingen, Tammannstr. 2, 37077, Göttingen, Germany.
King F YambireEuropean Neuroscience Institute, Göttingen - A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society, Grisebachstr. 5, 37077, Göttingen, Germany.
Niels DenkertDepartment of Cellular Biochemistry, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.
Indrani MukherjeeDepartment of Cellular Biochemistry, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.
Daryna TarasenkoDepartment of Cellular Biochemistry, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.
Garima JaipuriaGerman Center for Neurodegenerative Diseases (DZNE), Von-Siebold-Str. 3a, 37075, Göttingen, Germany.
Markus ZweckstetterGerman Center for Neurodegenerative Diseases (DZNE), Von-Siebold-Str. 3a, 37075, Göttingen, Germany.
Ira MilosevicEuropean Neuroscience Institute, Göttingen - A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society, Grisebachstr. 5, 37077, Göttingen, Germany.
Claudia SteinemInstitute for Organic and Biomolecular Chemistry, University of Göttingen, Tammannstr. 2, 37077, Göttingen, Germany. csteine@gwdg.de.
Michael MeineckeDepartment of Cellular Biochemistry, University Medical Center Göttingen, Humboldtallee 23, 37073, Göttingen, Germany. mmeinec@gwdg.de.ORCID http://orcid.org/0000-0003-1414-6951
Universitätsmedizin Göttingen · DEGerman Center for Neurodegenerative Diseases · DECentre for Human Genetics · GBMax Planck Institute for Dynamics and Self-Organization · DEMax Planck Society · DEUniversity of Göttingen · DE

Funding

Deutsche Forschungsgemeinschaft SFB803
6 · The paper itself

Abstract

Membrane remodeling is a critical process for many membrane trafficking events, including clathrin-mediated endocytosis. Several molecular mechanisms for protein-induced membrane curvature have been described in some detail. Contrary, the effect that the physico-chemical properties of the membrane have on these processes is far less well understood. Here, we show that the membrane binding and curvature-inducing ENTH domain of epsin1 is regulated by phosphatidylserine (PS). ENTH binds to membranes in a PI(4,5)P

Indexed as

EndocytosisAdaptor Proteins, Vesicular TransportBinding SitesCell MembraneClathrinHumansMembrane LipidsMembrane ProteinsMicroscopy, ElectronMutationPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein DomainsProtein TransportAdaptor Proteins, Vesicular TransportClathrinepsinMembrane LipidsMembrane ProteinsPhosphatidylinositol 4,5-DiphosphateClathrin-mediated endocytosisENTH domainMembrane curvatureMembrane dynamicsReconstitution of membrane dynamics

Identifiers

PMID32997199
PMCPMC7966211
OpenAlexW3091566941

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.