Evidence map›Paper›PMID 26538089›Full record

ArticleAmerican journal of physiology. Cell physiology2016

Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics.

Rupalatha Maddala, Mark Walters, Peter J Brophy, Vann Bennett, Ponugoti V Rao

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 28 citations in OpenAlex.

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  13. Biochemical and biomechanical characteristics of dystrophin-deficient mdxBiochimica et biophysica acta. Molecular basis of disease · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Rupalatha MaddalaDepartment of Ophthalmology, Duke University School of Medicine, Durham, North Carolina;
Mark WaltersDepartment of Mechanical Engineering and Materials Science, Pratt School of Engineering, Duke University, Durham, North Carolina;
Peter J BrophyCentre for Neuroregeneration, University of Edinburgh, Edinburgh, United Kingdom;
Vann BennettHoward Hughes Medical Institute, Chevy Chase, Maryland; Department of Biochemistry, Duke University School of Medicine, Durham, North Carolina; and.
Ponugoti V RaoDepartment of Ophthalmology, Duke University School of Medicine, Durham, North Carolina; Department of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, North Carolina p.rao@dm.duke.edu.
Duke University · USHoward Hughes Medical Institute · USUniversity of Edinburgh · GB

Funding

VISION RESEARCHP30EY005722 · NEI · DUKE UNIVERSITY · PI Vadim Y Arshavsky · 1985 to 2026
$19.3M
Trabecular Meshwork Cytoskeletal Signaling-Regulation of Aqueous Humor OutflowR01EY018590 · NEI · DUKE UNIVERSITY · PI RAO, P VASANTHA · 2008 to 2022
$5.6M
Fiber Cell Membrane Organization-Role in Lens Architecture and FunctionR01EY025096 · NEI · DUKE UNIVERSITY · PI RAO, P VASANTHA · 2015 to 2019
$2.0M
Role of S100A4 in Lens Homeostasis and FunctionR21EY027053 · NEI · DUKE UNIVERSITY · PI MADDALA, RUPALATHA · 2016 to 2017
$358k
Howard Hughes Medical InstituteNEI NIH HHS P30 EY005722NEI NIH HHS P30-EY-005722NEI NIH HHS R01-EY-018590NEI NIH HHS R01 EY025096NEI NIH HHS R01-EY-025096NEI NIH HHS R21 EY027053Wellcome Trust
6 · The paper itself

Abstract

Periaxin (Prx), a PDZ domain protein expressed preferentially in myelinating Schwann cells and lens fibers, plays a key role in membrane scaffolding and cytoarchitecture. Little is known, however, about how Prx is anchored to the plasma membrane. Here we report that ankyrin-B (AnkB), a well-characterized adaptor protein involved in linking the spectrin-actin cytoskeleton to integral membrane proteins, is required for membrane association of Prx in lens fibers and colocalizes with Prx in hexagonal fiber cells. Under AnkB haploinsufficiency, Prx accumulates in the soluble fraction with a concomitant loss from the membrane-enriched fraction of mouse lenses. Moreover, AnkB haploinsufficiency induced age-dependent disruptions in fiber cell hexagonal geometry and radial alignment and decreased compressive stiffness in mouse lenses parallel to the changes observed in Prx null mouse lens. Both AnkB- and Prx-deficient mice exhibit disruptions in membrane organization of the spectrin-actin network and the dystrophin-glycoprotein complex in lens fiber cells. Taken together, these observations reveal that AnkB is required for Prx membrane anchoring and for maintenance of lens fiber cell hexagonal geometry, membrane skeleton organization, and biomechanics.

Indexed as

AnimalsAnkyrinsBinding SitesCell MembraneCell SizeCompressive StrengthElastic ModulusEpithelial CellsHardnessIn Vitro TechniquesLens, CrystallineMembrane ProteinsMiceMice, KnockoutProtein BindingStress, MechanicalAnkyrinsMembrane Proteinsperiaxinankyrin-Bcytoarchitecturedystrophinlens fibersperiaxinstiffness

Identifiers

PMID26538089
PMCPMC4719034
OpenAlexW2177709815

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.