Evidence map›Paper›PMID 36902136›Full record

ArticleInternational journal of molecular sciences2023

Analysis of Dysferlin Direct Interactions with Putative Repair Proteins Links Apoptotic Signaling to Ca

Dennis G Drescher, Marian J Drescher, Dakshnamurthy Selvakumar, Neeraja P Annam

Open access · goldFull text read
In one paragraph

Article in International journal of molecular sciences, 2023. 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
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

5 citing papers in PubMed, 15 citations in OpenAlex.

  1. A Novel Dysferlin-Binding Kinase CK2α Promotes Plasma Membrane Repair in Dysferlinopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Otoferlin as a multirole CaFrontiers in cellular neuroscience · 2023
    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.

Dennis G DrescherLaboratory of Bio-otology, Department of Otolaryngology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Marian J DrescherLaboratory of Bio-otology, Department of Otolaryngology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Dakshnamurthy SelvakumarLaboratory of Bio-otology, Department of Otolaryngology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Neeraja P AnnamLaboratory of Bio-otology, Department of Otolaryngology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Wayne State University · US

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI Julie Lynn Boerner · 1985 to 2026
$68.4M
IDENTIFICATION OF ACOUSTICO-LATERALIS TRANSMITTERSR01DC000156 · NIDCD · WAYNE STATE UNIVERSITY · PI DRESCHER, DENNIS G · 1989 to 2013
$3.9M
A stable path for a core based scientist to advance imaging and cytometry in basic and preclinical research at the Karmanos Cancer InstituteR50CA251068 · NCI · WAYNE STATE UNIVERSITY · PI MOIN, KAMIAR · 2020 to 2024
$1.4M
NCI NIH HHS P30 CA022453NCI NIH HHS R50 CA251068NIDCD NIH HHS R01 DC000156NIH HHS P30 CA022453NIH HHS R01 DC000156NIH HHS R50 CA251068
6 · The paper itself

Abstract

Quantitative surface plasmon resonance (SPR) was utilized to determine binding strength and calcium dependence of direct interactions between dysferlin and proteins likely to mediate skeletal muscle repair, interrupted in limb girdle muscular dystrophy type 2B/R2. Dysferlin canonical C2A (cC2A) and C2F/G domains directly interacted with annexin A1, calpain-3, caveolin-3, affixin, AHNAK1, syntaxin-4, and mitsugumin-53, with cC2A the primary target and C2F lesser involved, overall demonstrating positive calcium dependence. Dysferlin C2 pairings alone showed negative calcium dependence in almost all cases. Like otoferlin, dysferlin directly interacted via its carboxy terminus with FKBP8, an anti-apoptotic outer mitochondrial membrane protein, and via its C2DE domain with apoptosis-linked gene (ALG-2/PDCD6), linking anti-apoptosis with apoptosis. Confocal Z-stack immunofluorescence confirmed co-compartmentalization of PDCD6 and FKBP8 at the sarcolemmal membrane. Our evidence supports the hypothesis that prior to injury, dysferlin C2 domains self-interact and give rise to a folded, compact structure as indicated for otoferlin. With elevation of intracellular Ca

Indexed as

Apoptosis Regulatory ProteinsCalciumCalcium-Binding ProteinsDysferlinMuscle, SkeletalRegenerationTacrolimus Binding ProteinsAnimalsAnnexin A1ApoptosisCalpainCaveolin 3RatsSarcolemmaSignal TransductionSurface Plasmon ResonanceAnnexin A1Apoptosis Regulatory ProteinsCalciumCalcium-Binding ProteinsCalpainCaveolin 3DysferlinTacrolimus Binding ProteinsC2 domainscalcium dependencedysferlinFKBP8limb girdle muscular dystrophy type 2B/R2PDCD6protein–protein interactionssurface plasmon resonance

Identifiers

PMID36902136
PMCPMC10002499
OpenAlexW4322743444

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read47
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.