Evidence map›Paper›PMID 9276950›Full record

ArticlePlant physiology1997

Ca(2+)-activated anion channels and membrane depolarizations induced by blue light and cold in Arabidopsis seedlings.

B D Lewis, G Karlin-Neumann, R W Davis, E P Spalding

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

32 citing papers in PubMed, 97 citations in OpenAlex.

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  6. Channelrhodopsin-mediated optogenetics highlights a central role of depolarization-dependent plant proton pumps.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Function and solution structure of the Arabidopsis thaliana RALF8 peptide.Protein science : a publication of the Protein Society · 2019
    Article
  8. Article
  9. Review
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  12. Article
  13. Simulation of variation potential in higher plant cells.The Journal of membrane biology · 2013
    Article
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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

4 authors at 1 institution in 1 country.

B D LewisDepartment of Botany, University of Wisconsin, Madison 53706, USA.
G Karlin-Neumann
R W Davis
E P Spalding
University of Wisconsin–Madison · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activation of an anion channel in the plasma membrane of Arabidopsis thaliana hypocotyls by blue light (BL) is believed to be a signal-transducing event leading to growth inhibition. Here we report that the open probability of this particular anion channel depends on cytoplasmic Ca2+ ([Ca2+]cyt) within the concentration range of 1 to 10 microM, raising the possibility that BL activates the anion channel by increasing [Ca2+]cyt. Arabidopsis seedlings cytoplasmically expressing aequorin were generated to test this possibility. Aequorin luminescence did not increase during or after BL, providing evidence that Ca2+ does not play a second-messenger role in the activation of anion channels. However, cold shock simultaneously triggered a large increase in [Ca2+]cyt and a 110-mV transient depolarization of the plasma membrane. A blocker of the anion channel, 5-nitro-2-(3-phenylpropylamino)-benzoic acid, blocked 61% of the cold-induced depolarization without affecting the increase in [Ca2+]cyt. These data led us to propose that cold shock opens Ca2+ channels at the plasma membrane, allowing an inward, depolarizing Ca2+ current. The resulting large increase in [Ca2+]cyt activates the anion channel, which further depolarizes the membrane. Although an increase in [Ca2+]cyt may activate anion channels in response to cold, it appears that BL does so via a Ca(2+)-independent pathway.

Indexed as

Cold TemperatureLightAequorinAnionsArabidopsisCalciumIon ChannelsMembrane PotentialsNitrobenzoatesPlants, Genetically ModifiedRecombinant Proteins5-nitro-2-(3-phenylpropylamino)benzoic acidAequorinAnionsCalciumIon ChannelsNitrobenzoatesRecombinant ProteinsNASA Discipline Plant BiologyNon-NASA Center

Identifiers

PMID9276950
PMCPMC158425
OpenAlexW2099197988

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.