Evidence map›Paper›PMID 38019609›Full record

ArticleMolecular biology of the cell2024

Effects of phosphorylation on Drp1 activation by its receptors, actin, and cardiolipin.

Ao Liu, Anna L Hatch, Henry N Higgs

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
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  7. Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
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  9. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Ao LiuDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover NH 03755.ORCID 0000-0002-6800-8012
Anna L HatchDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover NH 03755.
Henry N HiggsDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover NH 03755.ORCID 0000-0002-2917-9644
Dartmouth College · US

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
The impact of dynamic actin polymerization on mitochondrial dynamics and functionR35GM122545 · NIGMS · DARTMOUTH COLLEGE · PI HENRY N HIGGS · 2017 to 2026
$7.7M
INF2 in kidney function and dysfunctionR01DK088826 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI HENRY N HIGGS, MARTIN R. POLLAK · 2010 to 2026
$6.3M
Comparative molecular physiology of mammalian forminsR01GM069818 · NIGMS · DARTMOUTH COLLEGE · PI HIGGS, HENRY N · 2004 to 2017
$4.3M
NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R01 GM069818NIGMS NIH HHS R35 GM122545
6 · The paper itself

Abstract

Drp1 is a dynamin family GTPase required for mitochondrial and peroxisomal division. Oligomerization increases Drp1 GTPase activity through interactions between neighboring GTPase domains. In cells, Drp1 is regulated by several factors including Drp1 receptors, actin filaments, cardiolipin, and phosphorylation at two sites: S579 and S600. Commonly, phosphorylation of S579 is considered activating, while S600 phosphorylation is considered inhibiting. However, direct effects of phosphorylation on Drp1 GTPase activity have not been investigated in detail. Here, we compare effects of S579 and S600 phosphorylation on purified Drp1, using phosphomimetic mutants and in vitro phosphorylation. Both phosphomimetic mutants are shifted toward smaller oligomers. Both phosphomimetic mutations maintain basal GTPase activity, but eliminate GTPase stimulation by actin and decrease GTPase stimulation by cardiolipin, Mff, and MiD49. Phosphorylation of S579 by Erk2 produces similar effects. When mixed with wildtype Drp1, both S579D and S600D phosphomimetic mutants reduce the actin-stimulated GTPase activity of Drp1-WT. Conversely, a Drp1 mutant (K38A) lacking GTPase activity stimulates Drp1-WT GTPase activity under both basal and actin-stimulated conditions. These results suggest that the effect of S579 phosphorylation is not to activate Drp1 directly. In addition, our results suggest that nearest neighbor interactions within the Drp1 oligomer affect catalytic activity.

Indexed as

ActinsCardiolipinsDynaminsGTP PhosphohydrolasesMitochondrial DynamicsMitochondrial ProteinsPhosphorylationActinsCardiolipinsDynaminsGTP PhosphohydrolasesMitochondrial Proteins

Identifiers

PMID38019609
PMCPMC10881151
OpenAlexW4389132746

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.