Evidence map›Paper›PMID 23820729›Full record

ArticleMolecular & cellular proteomics : MCP2013

Sucrose-induced receptor kinase SIRK1 regulates a plasma membrane aquaporin in Arabidopsis.

Xu Na Wu, Clara Sanchez Rodriguez, Heidi Pertl-Obermeyer, Gerhard Obermeyer, Waltraud X Schulze

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
15.3field-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

48 citing papers in PubMed, 99 citations in OpenAlex.

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  18. Phosphoproteomics Profiling of Receptor Kinase Mutants.Methods in molecular biology (Clifton, N.J.) · 2021
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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

5 authors at 3 institutions in 2 countries.

Xu Na WuMax Planck Institute for Molecular Plant Physiology, Am Mühlenberg 1, 14476 Golm, Germany;
Clara Sanchez Rodriguez
Heidi Pertl-Obermeyer
Gerhard Obermeyer
Waltraud X Schulze
Max Planck Society · DEUniversity of Hohenheim · DEUniversity of Salzburg · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmembrane receptor kinase family is the largest protein kinase family in Arabidopsis, and it contains the highest fraction of proteins with yet uncharacterized functions. Here, we present functions of SIRK1, a receptor kinase that was previously identified with rapid transient phosphorylation after sucrose resupply to sucrose-starved seedlings. SIRK1 was found to be an active kinase with increasing activity in the presence of an external sucrose supply. In sirk1 T-DNA insertional mutants, the sucrose-induced phosphorylation patterns of several membrane proteins were strongly reduced; in particular, pore-gating phosphorylation sites in aquaporins were affected. SIRK1-GFP fusions were found to directly interact with aquaporins in affinity pull-down experiments on microsomal membrane vesicles. Furthermore, protoplast swelling assays of sirk1 mutants and SIRK1-GFP expressing lines confirmed a direct functional interaction of receptor kinase SIRK1 and aquaporins as substrates for phosphorylation. A lack of SIRK1 expression resulted in the failure of mutant protoplasts to control water channel activity upon changes in external sucrose concentrations. We propose that SIRK1 is involved in the regulation of sucrose-specific osmotic responses through direct interaction with and activation of an aquaporin via phosphorylation and that the duration of this response is controlled by phosphorylation-dependent receptor internalization.

Indexed as

AquaporinsArabidopsisArabidopsis ProteinsCell MembraneGreen Fluorescent ProteinsProtein KinasesRecombinant Fusion ProteinsSucroseAquaporinsArabidopsis ProteinsGreen Fluorescent ProteinsProtein KinasesRecombinant Fusion ProteinsRPK1 protein, ArabidopsisSucrose

Identifiers

PMID23820729
PMCPMC3790296
OpenAlexW2122210253

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.