Evidence map›Paper›PMID 24239457›Full record

ArticleStructure (London, England : 1993)2014

Alternate splicing of dysferlin C2A confers Ca²⁺-dependent and Ca²⁺-independent binding for membrane repair.

Kerry Fuson, Anne Rice, Ryan Mahling, Adam Snow, Kamakshi Nayak, Prajna Shanbhogue, Austin G Meyer, Gregory M I Redpath, Anne Hinderliter, Sandra T Cooper and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 56 citations in OpenAlex.

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  13. CytochromeThe Journal of biological chemistry · 2020
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  20. Molecular Therapies for Muscular Dystrophies.Current treatment options in neurology · 2018
    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

11 authors at 4 institutions in 2 countries.

Kerry FusonDepartment of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA; Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Anne RiceDepartment of Chemistry and Biochemistry, University of Minnesota Duluth, Duluth 55812 MN, USA.
Ryan MahlingDepartment of Chemistry and Biochemistry, University of Minnesota Duluth, Duluth 55812 MN, USA.
Adam SnowDepartment of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA; Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Kamakshi NayakDepartment of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA; Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Prajna ShanbhogueDepartment of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA; Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Austin G MeyerDepartment of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA; Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA.
Gregory M I RedpathInstitute for Neuroscience and Muscle Research, Children's Hospital at Westmead, Sydney, NSW 2145, Australia.
Anne HinderliterDepartment of Chemistry and Biochemistry, University of Minnesota Duluth, Duluth 55812 MN, USA.
Sandra T CooperInstitute for Neuroscience and Muscle Research, Children's Hospital at Westmead, Sydney, NSW 2145, Australia.
R Bryan SuttonDepartment of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA; Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA. Electronic address: roger.b.sutton@ttuhsc.edu.
Texas Tech University Health Sciences Center · USUniversity of Minnesota, Duluth · USChildren's Hospital at Westmead · AUTexas Tech University · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Human dysferlin and its implications in Limb-Girdle Muscular DystrophyR01AR063634 · NIAMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI SUTTON, ROGER BRYAN · 2014 to 2018
$1.8M
NCRR NIH HHS P41 RR001209NIAMS NIH HHS R01 AR063634NIGMS NIH HHS P41 GM103393
6 · The paper itself

Abstract

Dysferlin plays a critical role in the Ca²⁺-dependent repair of microlesions that occur in the muscle sarcolemma. Of the seven C2 domains in dysferlin, only C2A is reported to bind both Ca²⁺ and phospholipid, thus acting as a key sensor in membrane repair. Dysferlin C2A exists as two isoforms, the "canonical" C2A and C2A variant 1 (C2Av1). Interestingly, these isoforms have markedly different responses to Ca²⁺ and phospholipid. Structural and thermodynamic analyses are consistent with the canonical C2A domain as a Ca²⁺-dependent, phospholipid-binding domain, whereas C2Av1 would likely be Ca²⁺-independent under physiological conditions. Additionally, both isoforms display remarkably low free energies of stability, indicative of a highly flexible structure. The inverted ligand preference and flexibility for both C2A isoforms suggest the capability for both constitutive and Ca²⁺-regulated effector interactions, an activity that would be essential in its role as a mediator of membrane repair.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsCalciumCell LineCrystallography, X-RayDysferlinHumansMembrane ProteinsMiceModels, MolecularMolecular Sequence DataMuscle ProteinsMutagenesis, Site-DirectedMyoblastsProtein BindingCalciumDysferlinDYSF protein, humanDysf protein, mouseMembrane ProteinsMuscle ProteinsRecombinant ProteinsRNA, Messenger

Identifiers

PMID24239457
PMCPMC5993433
OpenAlexW2041098512

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.