Evidence map›Paper›PMID 26700940›Full record

ReviewPflugers Archiv : European journal of physiology2016

Modulating Ca²⁺ signals: a common theme for TMEM16, Ist2, and TMC.

Karl Kunzelmann, Ines Cabrita, Podchanart Wanitchakool, Jiraporn Ousingsawat, Lalida Sirianant, Roberta Benedetto, Rainer Schreiber

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
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

45 citing papers in PubMed.

  1. Review
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  17. Review
  18. The diverse roles of TMEM16A CaJournal of advanced research · 2021
    Review
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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.

Karl KunzelmannInstitut für Physiologie, Universität Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany. Karl.Kunzelmann@vkl.uni-regensburg.de.
Ines CabritaInstitut für Physiologie, Universität Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.
Podchanart WanitchakoolInstitut für Physiologie, Universität Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.
Jiraporn OusingsawatInstitut für Physiologie, Universität Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.
Lalida SirianantInstitut für Physiologie, Universität Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.
Roberta BenedettoInstitut für Physiologie, Universität Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.
Rainer SchreiberInstitut für Physiologie, Universität Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since the discovery of TMEM16A (anoctamin 1, ANO1) as Ca(2+)-activated Cl(-) channel, the protein was found to serve different physiological functions, depending on the type of tissue. Subsequent reports on other members of the anoctamin family demonstrated a broad range of yet poorly understood properties. Compromised anoctamin function is causing a wide range of diseases, such as hearing loss (ANO2), bleeding disorder (ANO6), ataxia and dystonia (ANO3, 10), persistent borrelia and mycobacteria infection (ANO10), skeletal syndromes like gnathodiaphyseal dysplasia and limb girdle muscle dystrophy (ANO5), and cancer (ANO1, 6, 7). Animal models demonstrate CF-like airway disease, asthma, and intestinal hyposecretion (ANO1). Although present data indicate that ANO1 is a Ca(2+)-activated Cl(-) channel, it remains unclear whether all anoctamins form plasma membrane-localized or intracellular chloride channels. We find Ca(2+)-activated Cl(-) currents appearing by expression of most anoctamin paralogs, including the Nectria haematococca homologue nhTMEM16 and the yeast homologue Ist2. As recent studies show a role of anoctamins, Ist2, and the related transmembrane channel-like (TMC) proteins for intracellular Ca(2+) signaling, we will discuss the role of these proteins in generating compartmentalized Ca(2+) signals, which may give a hint as to the broad range of cellular functions of anoctamins.

Indexed as

Calcium SignalingAction PotentialsAnimalsAnoctamin-1CalciumChloride ChannelsChloridesHumansNeoplasm ProteinsANO1 protein, humanAnoctamin-1CalciumChloride ChannelsChloridesNeoplasm ProteinsAnoctamin 1Anoctamin 6Ca2+ signalingER Ca2+ storeIst2Lipid raftsnhTMEM16SCP2SecretionTMCTMEM16ATMEM16FTMEM16 proteins

Identifiers

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.