Evidence map›Paper›PMID 26322575›Full record

ReviewPlant signaling & behavior2015

Phosphorylation of RACK1 in plants.

Jin-Gui Chen

Abstract readReview
In one paragraph

Review in Plant signaling & behavior, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
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

1 author.

Jin-Gui Chena Biosciences Division; Oak Ridge National Laboratory ; Oak Ridge , TN USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor for Activated C Kinase 1 (RACK1) is a versatile scaffold protein that interacts with a large, diverse group of proteins to regulate various signaling cascades. RACK1 has been shown to regulate hormonal signaling, stress responses and multiple processes of growth and development in plants. However, little is known about the molecular mechanism underlying these regulations. Recently, it has been demonstrated that Arabidopsis RACK1 is phosphorylated by an atypical serine/threonine protein kinase, WITH NO LYSINE 8 (WNK8). Furthermore, RACK1 phosphorylation by WNK8 negatively regulates RACK1 function by influencing its protein stability. These findings promote a new regulatory system in which the action of RACK1 is controlled by phosphorylation and subsequent protein degradation.

Indexed as

ArabidopsisArabidopsis ProteinsPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProteolysisReceptors, Cell SurfaceReceptors for Activated C KinaseArabidopsis ProteinsProtein Serine-Threonine KinasesRACK1 protein, ArabidopsisReceptors, Cell SurfaceReceptors for Activated C KinaseWNK8 protein, ArabidopsisArabidopsiskinasephosphorylationprotein degradationRACK1scaffold proteinWNK8

Identifiers

PMID26322575
PMCPMC4622689

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.