Evidence map›Paper›PMID 24891099›Full record

ArticleTraffic (Copenhagen, Denmark)2014

Regulation of dynamin oligomerization in cells: the role of dynamin-actin interactions and its GTPase activity.

Changkyu Gu, Joann Chang, Valentina A Shchedrina, Vincent A Pham, John H Hartwig, Worawit Suphamungmee, William Lehman, Bradley T Hyman, Brian J Bacskai, Sanja Sever

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Cytoskeleton Rearrangement in Podocytopathies: An Update.International journal of molecular sciences · 2024
    Review
  9. Dynamin-dependent entry ofResearch square · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Role of actin cytoskeleton in podocytes.Pediatric nephrology (Berlin, Germany) · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

10 authors at 4 institutions in 1 country.

Changkyu GuDivision of Nephrology, Massachusetts General Hospital, Charlestown, MA, 02129, USA.
Joann Chang
Valentina A Shchedrina
Vincent A Pham
John H Hartwig
Worawit Suphamungmee
William Lehman
Bradley T Hyman
Brian J Bacskai
Sanja Sever
Harvard University · USMassachusetts General Hospital · USBoston University · USBrigham and Women's Hospital · US

Funding

Multiphoton microscopy for in vivo neural imaging.R01EB000768 · NIBIB · MASSACHUSETTS GENERAL HOSPITAL · PI BACSKAI, BRIAN J · 2002 to 2015
$5.0M
Thin Filaments and Muscle RegulationR37HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEHMAN, WILLIAM J · 2008 to 2017
$4.1M
Use of small molecules that stabilize dynamin rings in podocytopathiesR01DK087985 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI SEVER, SANJA · 2011 to 2020
$3.4M
Role of dynamin for podocytes structure and functionR01DK093773 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI SEVER, SANJA · 2011 to 2021
$3.4M
NHLBI NIH HHS R37 HL036153NHLBI NIH HHS R37-HL036153NIBIB NIH HHS R01 EB000768NIDDK NIH HHS R01 DK087985NIDDK NIH HHS R01 DK093773NIDDK NIH HHS R01 DK93773
6 · The paper itself

Abstract

Dynamin is a 96-kDa protein that has multiple oligomerization states that influence its GTPase activity. A number of different dynamin effectors, including lipids, actin filaments, and SH3-domain-containing proteins, have been implicated in the regulation of dynamin oligomerization, though their roles in influencing dynamin oligomerization have been studied predominantly in vitro using recombinant proteins. Here, we identify higher order dynamin oligomers such as rings and helices in vitro and in live cells using fluorescence lifetime imaging microscopy (FLIM). FLIM detected GTP- and actin-dependent dynamin oligomerization at distinct cellular sites, including the cell membrane and transition zones where cortical actin transitions into stress fibers. Our study identifies a major role for direct dynamin-actin interactions and dynamin's GTPase activity in the regulation of dynamin oligomerization in cells.

Indexed as

Protein MultimerizationActinsAmino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsDynaminsGuanosine TriphosphateMiceMolecular Sequence DataProtein BindingProtein Structure, TertiaryActinsDynaminsGuanosine Triphosphateactindynamindynamin oligomerizationfluorescence lifetime imaging microscopy

Identifiers

PMID24891099
PMCPMC4107071
OpenAlexW2001402908

What OpenQuestion holds

Textmetadata
LicenceTDM
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.