Evidence map›Paper›PMID 32579424›Full record

ArticleMolecular biology of the cell2020

Early and nonredundant functions of dynamin isoforms in clathrin-mediated endocytosis.

Madhura Bhave, Marcel Mettlen, Xinxin Wang, Sandra L Schmid

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. CALM supports clathrin-coated vesicle completion upon membrane tension increase.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Review
  10. Functional characterization of 67 endocytic accessory proteins using multiparametric quantitative analysis of CCP dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. 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

4 authors at 1 institution in 1 country.

Madhura BhaveDepartment of Cell Biology, University of Texas Southwestern Medical Center, TX 75390.
Marcel MettlenDepartment of Cell Biology, University of Texas Southwestern Medical Center, TX 75390.
Xinxin WangDepartment of Cell Biology, University of Texas Southwestern Medical Center, TX 75390.
Sandra L SchmidDepartment of Cell Biology, University of Texas Southwestern Medical Center, TX 75390.
The University of Texas Southwestern Medical Center · US

Funding

EARLY STEPS IN RECEPTOR-MEDIATED ENDOCYTOSISR01GM042455 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI METTLEN, MARCEL BERNARD · 1989 to 2020
$8.2M
Request for administrative supplement to Parent R01 GM073165 entitled "Mechanisms regulating clathrin-mediated endocytosis"R01GM073165 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI METTLEN, MARCEL BERNARD · 2006 to 2022
$6.8M
NIGMS NIH HHS R01 GM042455NIGMS NIH HHS R01 GM073165
6 · The paper itself

Abstract

Dynamin GTPases (Dyn1 and Dyn2) are indispensable proteins of the core clathrin-mediated endocytosis (CME) machinery. Best known for their role in fission at the late stages of CME, many studies have suggested that dynamin also plays a regulatory role during the early stages of CME; however, detailed studies regarding isoform-specific early regulatory functions of the dynamins are lacking. With a recent understanding of the regulation of Dyn1 in nonneuronal cells and improved algorithms for highly sensitive and quantitative analysis of clathrin-coated pit (CCP) dynamics, we have evaluated the differential functions of dynamin isoforms in CME using domain swap chimeras. We report that Dyn1 and Dyn2 play nonredundant, early regulatory roles during CME in nonneuronal cells. The proline/arginine-rich domain of Dyn2 is important for its targeting to nascent and growing CCPs, whereas the membrane-binding and curvature-generating pleckstrin homology domain of Dyn1 plays an important role in stabilizing nascent CCPs. We confirm the enhanced ability of dephosphorylated Dyn1 to support CME, even at substoichiometric levels compared with Dyn2. Domain swap chimeras also revealed previously unknown functional differences in the GTPase and stalk domains. Our study significantly extends the current understanding of the regulatory roles played by dynamin isoforms during early stages of CME.

Indexed as

Cell LineClathrinClathrin-Coated VesiclesDynamin IDynamin IIDynaminsEndocytosisGTP PhosphohydrolasesHumansProtein IsoformsSignal TransductionClathrinDynamin IDynamin IIDynaminsGTP PhosphohydrolasesProtein Isoforms

Identifiers

PMID32579424
PMCPMC7543069
OpenAlexW3037733345

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.