Evidence map›Paper›PMID 26667038›Full record

ArticleMolecular and cellular biology2016

A Role of TMEM16E Carrying a Scrambling Domain in Sperm Motility.

Sayuri Gyobu, Haruhiko Miyata, Masahito Ikawa, Daiju Yamazaki, Hiroshi Takeshima, Jun Suzuki, Shigekazu Nagata

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 78 citations in OpenAlex.

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  10. Intrinsic signalling factors associated with cancer cell-cell fusion.Cell communication and signaling : CCS · 2023
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  17. Polymodal Control of TMEM16x Channels and Scramblases.International journal of molecular sciences · 2022
    Review
  18. Article
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  20. SPATA33 localizes calcineurin to the mitochondria and regulates sperm motility in mice.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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 2 institutions in 1 country.

Sayuri GyobuLaboratory of Biochemistry & Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.
Haruhiko MiyataDepartment of Experimental Genome Research, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
Masahito IkawaDepartment of Experimental Genome Research, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
Daiju YamazakiDepartment of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Hiroshi TakeshimaDepartment of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Jun SuzukiLaboratory of Biochemistry & Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.
Shigekazu NagataLaboratory of Biochemistry & Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan snagata@ifrec.osaka-u.ac.jp.
Osaka University · JPKyoto Pharmaceutical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmembrane protein 16E (TMEM16E) belongs to the TMEM16 family of proteins that have 10 transmembrane regions and appears to localize intracellularly. Although TMEM16E mutations cause bone fragility and muscular dystrophy in humans, its biochemical function is unknown. In the TMEM16 family, TMEM16A and -16B serve as Ca(2+)-dependent Cl(-) channels, while TMEM16C, -16D, -16F, -16G, and -16J support Ca(2+)-dependent phospholipid scrambling. Here, we show that TMEM16E carries a segment composed of 35 amino acids homologous to the scrambling domain in TMEM16F. When the corresponding segment of TMEM16A was replaced by this 35-amino-acid segment of TMEM16E, the chimeric molecule localized to the plasma membrane and supported Ca(2+)-dependent scrambling. We next established TMEM16E-deficient mice, which appeared to have normal skeletal muscle. However, fertility was decreased in the males. We found that TMEM16E was expressed in germ cells in early spermatogenesis and thereafter and localized to sperm tail. TMEM16E(-/-) sperm showed no apparent defect in morphology, beating, mitochondrial function, capacitation, or binding to zona pellucida. However, they showed reduced motility and inefficient fertilization of cumulus-free but zona-intact eggs in vitro. Our results suggest that TMEM16E may function as a phospholipid scramblase at inner membranes and that its defect affects sperm motility.

Indexed as

FertilizationSperm MotilityAmino Acid SequenceAnimalsAnoctaminsCell LineChloride ChannelsFemaleGene DeletionMaleMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataMutationProtein Structure, TertiaryANO5 protein, mouseAnoctaminsChloride Channels

Identifiers

PMID26667038
PMCPMC4751691
OpenAlexW2204735739

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.