Evidence map›Paper›PMID 39420071›Full record

ArticleCommunications biology2024

Protein kinase 2 of the giant sarcomeric protein UNC-89 regulates mitochondrial morphology and function.

Yohei Matsunaga, Hiroshi Qadota, Nasab Ghazal, Leila Lesanpezeshki, Till Dorendorf, Jasmine C Moody, Arnaud Ahier, Courtney J Matheny, Siva A Vanapalli, Steven Zuryn and 3 more

Abstract read
In one paragraph

Article in Communications biology, 2024. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025
    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

13 authors.

Yohei MatsunagaDepartment of Pathology, Emory University, Atlanta, GA, USA.
Hiroshi QadotaDepartment of Pathology, Emory University, Atlanta, GA, USA.
Nasab GhazalDepartment of Pediatrics, Emory University, Atlanta, GA, USA.ORCID 0000-0001-9298-3144
Leila LesanpezeshkiDepartment of Chemical Engineering, Texas Tech University, Lubbock, TX, USA.
Till DorendorfDepartment of Biology, University of Konstanz, Konstanz, Germany.ORCID 0000-0002-8319-8010
Jasmine C MoodyDepartment of Pathology, Emory University, Atlanta, GA, USA.
Arnaud AhierClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, QLD, Australia.
Courtney J MathenyDepartment of Pathology, Emory University, Atlanta, GA, USA.ORCID 0000-0001-7707-5180
Siva A VanapalliDepartment of Chemical Engineering, Texas Tech University, Lubbock, TX, USA.
Steven ZurynClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, QLD, Australia.
Olga MayansDepartment of Biology, University of Konstanz, Konstanz, Germany.
Jennifer Q KwongDepartment of Pediatrics, Emory University, Atlanta, GA, USA.ORCID 0000-0001-9867-7658
Guy M BenianDepartment of Pathology, Emory University, Atlanta, GA, USA. pathgb@emory.edu.ORCID 0000-0002-8236-3176

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
A Model Multi-systems Approach for Understanding the Role of the PIX Pathway in Cardiac Muscle and CardiomyopathyR01HL160693 · NHLBI · EMORY UNIVERSITY · PI BENIAN, GUY MARTIN · 2022 to 2025
$2.3M
Acylations: a novel pathway in the response to mitochondrial energy dysfunctionR01GM144729 · NIGMS · EMORY UNIVERSITY · PI Jennifer Q. Kwong · 2022 to 2026
$1.6M
National Science Foundation (NSF) 2050009NHLBI NIH HHS R01 HL160693NIGMS NIH HHS R01 GM144729NIH HHS P40 OD010440
6 · The paper itself

Abstract

UNC-89 is a giant sarcomeric M-line protein required for sarcomere organization and optimal muscle function. UNC-89 contains two protein kinase domains, PK1 and PK2, separated by an elastic region. Here we show that PK2 is a canonical kinase expected to be catalytically active. C. elegans expressing UNC-89 with a lysine to alanine (KtoA) mutation to inactivate PK2 have normally organized sarcomeres and SR, and normal muscle function. PK2 KtoA mutants have fragmented mitochondria, correlated with more mitochondrially-associated DRP-1. PK2 KtoA mutants have increased ATP levels, increased glycolysis and altered levels of electron transport chain complexes. Muscle mitochondria show increased complex I and decreased complex II basal respiration, each of which cannot be uncoupled. This suggests that mutant mitochondria are already uncoupled, possibly resulting from an increased level of the uncoupling protein, UCP-4. Our results suggest signaling from sarcomeres to mitochondria, to help match energy requirements with energy production.

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsMitochondriaSarcomeresAnimalsMuscle ProteinsMutationCaenorhabditis elegans ProteinsMuscle ProteinsUnc-89 protein, C elegans

Identifiers

PMID39420071
PMCPMC11487192

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.