Evidence map›Paper›PMID 20016007›Full record

ArticleMolecular biology of the cell2010

Live-cell imaging in Caenorhabditis elegans reveals the distinct roles of dynamin self-assembly and guanosine triphosphate hydrolysis in the removal of apoptotic cells.

Bin He, Xiaomeng Yu, Moran Margolis, Xianghua Liu, Xiaohong Leng, Yael Etzion, Fei Zheng, Nan Lu, Florante A Quiocho, Dganit Danino and 1 more

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The nucleoside diphosphate kinase NDK-1/NME1 promotes phagocytosis in concert with DYN-1/Dynamin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  7. Article
  8. Article
  9. Nucleoside diphosphate kinases (NDPKs) in animal development.Cellular and molecular life sciences : CMLS · 2015
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Membrane trafficking and phagosome maturation during the clearance of apoptotic cells.International review of cell and molecular biology · 2012
    Review
  16. Article
  17. Article
  18. Article
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 2 institutions in 2 countries.

Bin HeVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Xiaomeng Yu
Moran Margolis
Xianghua Liu
Xiaohong Leng
Yael Etzion
Fei Zheng
Nan Lu
Florante A Quiocho
Dganit Danino
Zheng Zhou
Baylor College of Medicine · USTechnion – Israel Institute of Technology · IL

Funding

Recognition of Apoptotic Cells for Their PhagocytosisR01GM067848 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI ZHOU, ZHENG · 2003 to 2021
$5.7M
Molecular Studies of the Roles and Regulations of the v-ATPase V0 SectorR01GM088803 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI QUIOCHO, FLORANTE A · 2009 to 2010
$971k
NIGMS NIH HHS GM-067848NIGMS NIH HHS GM088803NIGMS NIH HHS R01 GM067848NIGMS NIH HHS R01 GM088803
6 · The paper itself

Abstract

Dynamins are large GTPases that oligomerize along membranes. Dynamin's membrane fission activity is believed to underlie many of its physiological functions in membrane trafficking. Previously, we reported that DYN-1 (Caenorhabditis elegans dynamin) drove the engulfment and degradation of apoptotic cells through promoting the recruitment and fusion of intracellular vesicles to phagocytic cups and phagosomes, an activity distinct from dynamin's well-known membrane fission activity. Here, we have detected the oligomerization of DYN-1 in living C. elegans embryos and identified DYN-1 mutations that abolish DYN-1's oligomerization or GTPase activities. Specifically, abolishing self-assembly destroys DYN-1's association with the surfaces of extending pseudopods and maturing phagosomes, whereas inactivating guanosine triphosphate (GTP) binding blocks the dissociation of DYN-1 from these membranes. Abolishing the self-assembly or GTPase activities of DYN-1 leads to common as well as differential phagosomal maturation defects. Whereas both types of mutations cause delays in the transient enrichment of the RAB-5 GTPase to phagosomal surfaces, only the self-assembly mutation but not GTP binding mutation causes failure in recruiting the RAB-7 GTPase to phagosomal surfaces. We propose that during cell corpse removal, dynamin's self-assembly and GTP hydrolysis activities establish a precise dynamic control of DYN-1's transient association to its target membranes and that this control mechanism underlies the dynamic recruitment of downstream effectors to target membranes.

Indexed as

Caenorhabditis elegansAmino Acid SequenceAnimalsAnimals, Genetically ModifiedApoptosisCaenorhabditis elegans ProteinsCell MembraneDynaminsGuanosine TriphosphateHumansMolecular Sequence DataMutationPhagosomesProtein Structure, Tertiaryrab5 GTP-Binding Proteinsrab7 GTP-Binding ProteinsCaenorhabditis elegans ProteinsDynaminsGuanosine Triphosphaterab5 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsRecombinant Fusion Proteins

Identifiers

PMID20016007
PMCPMC2820425
OpenAlexW2000388632

What OpenQuestion holds

Textmetadata
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.