Evidence map›Paper›PMID 20169529›Full record

ArticleCytoskeleton (Hoboken, N.J.)2010

Changes in plasma membrane structure and electromotile properties in prestin deficient outer hair cells.

David Z Z He, Shuping Jia, Takashi Sato, Jian Zuo, Leonardo R Andrade, Gavin P Riordan, Bechara Kachar

Open access · greenAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

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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

7 authors at 3 institutions in 1 country.

David Z Z HeDepartment of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska, USA. hed@creighton.edu
Shuping Jia
Takashi Sato
Jian Zuo
Leonardo R Andrade
Gavin P Riordan
Bechara Kachar
Creighton University · USNational Institute on Deafness and Other Communication Disorders · USSt. Jude Children's Research Hospital · US

Funding

Structural and Molecular Basis of Transduction in Auditory Sensory OrgansZIADC000002 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI KACHAR, BECHARA · 2009 to 2025
$38.3M
BIOPHYSICS AND DEVELOPMENT OF COCHLEAR OUTER HAIR CELLSR01DC004696 · NIDCD · FATHER FLANAGAN'S BOYS'HOME · PI HE, ZHI-ZHOU · 2001 to 2016
$4.2M
GENETIC ANALYSIS OF MAMMALIAN HEARING SENSITIVITYR01DC006471 · NIDCD · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ZUO, JIAN · 2004 to 2013
$3.5M
NIDCD NIH HHS DC 004696NIDCD NIH HHS DC 06471NIDCD NIH HHS R01 DC004696NIDCD NIH HHS R01 DC006471
6 · The paper itself

Abstract

Cochlear outer hair cells (OHCs) rapidly change their length and stiffness when their membrane potential is altered. Prestin, the motor protein for this electromotility, is present along the OHC lateral plasma membrane where there is a high density of intra-membrane protein particles (IMPs). However, it is not known to what extent prestin contributes to this unusual dense population of proteins and overall organization of the membrane to generate the unique electromechanical response of OHCs. We investigated the relationship of prestin with the IMPs, the underlying cortical cytoskeletal lattice, and electromotility in prestin-deficient mice. Using freeze-fracture, we observed a reduction in density and size of the IMPs that correlates with the reduction and absence of prestin in the heterozygous and homozygous mice, respectively. We also observed a reduction or absence of electromotility-related charge density, axial stiffness, and piezoelectric properties of the OHC. A comparison of the charge density with the number of IMPs suggests that prestin forms tetramers in the wild type but is likely to form lower number oligomers in the prestin-deficient OHCs from the heterozygous mice. Interestingly, the characteristic actin-based cortical cytoskeletal lattice that underlies the membrane is absent in the prestin-null OHCs, suggesting that prestin is also required for recruiting or maintaining the cortical cytoskeletal lattice. These results suggest that the majority of the IMPs are indeed prestin and that electrically evoked length and stiffness changes are interrelated and dependent on both prestin and on the cortical actin cytoskeletal lattice of the OHC lateral membrane.

Indexed as

Electric CapacitanceAnimalsCell MembraneCells, CulturedHair Cells, Auditory, OuterMiceMice, KnockoutMicroscopy, ElectronMolecular Motor ProteinsMolecular Motor ProteinsPres protein, mouse

Identifiers

PMID20169529
PMCPMC2842980
OpenAlexW2141611912

What OpenQuestion holds

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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.