Evidence map›Paper›PMID 20448467›Full record

ArticlePlant signaling & behavior2010

PCaPs, possible regulators of PtdInsP signals on plasma membrane.

Mariko Kato, Nahoko Nagasaki-Takeuchi, Yuki Ide, Rie Tomioka, Masayoshi Maeshima

Open access · bronzeAbstract readComment
In one paragraph

Article in Plant signaling & behavior, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Mariko KatoGraduate School of Bioagricultural Sciences; Nagoya University, Nagoya, Japan.
Nahoko Nagasaki-Takeuchi
Yuki Ide
Rie Tomioka
Masayoshi Maeshima
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, Ca(2+), phosphatidylinositol phosphates (PtdInsPs) and inositol phosphates are major components of intracellular signaling. Several kinds of proteins and enzymes, such as calmodulin (CaM), protein kinase, protein phosphatase, and the Ca(2+) channel, mediate the signaling. Two new Ca(2+)-binding proteins were identified from Arabidopsis thaliana and named PCaP1 and PCaP2 [plasma membrane (PM)-associated Ca(2+) (cation)-binding protein 1 and 2]. PCaP1 has an intrinsically disordered region in the central and C-terminal parts. The PCaP1 gene is expressed in most tissues and the PCaP2 gene is expressed predominantly in root hairs and pollen tubes. We recently demonstrated that these proteins are N-myristoylated, stably anchored in the PM, and are bound with phosphatidylinositol phosphates, especially PtdInsP2s. Here we propose a model for the switching mechanism of Ca (2+)-signaling mediated by PtdInsPs. Ca(2+) forms a complex with CaM (Ca(2+)-CaM) when there is an increase in the cytosol free Ca(2+). The binding of PCaPs with Ca(2+)-CaM causes PCaPs to release PtdInsPs. Until the release of PtdInsPs, the signaling is kept in the resting state.

Indexed as

calcium signalcalmodulininositol phosphateintrinsically disordered proteinmyristoylationphosphatidylinositol phosphateplasma membrane

Identifiers

PMID20448467
PMCPMC3014536
OpenAlexW2009694250

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.