Evidence map›Paper›PMID 22645532›Full record

ArticleFrontiers in plant science2011

Calcium-dependent protein kinases from Arabidopsis show substrate specificity differences in an analysis of 103 substrates.

Amy Curran, Ing-Feng Chang, Chia-Lun Chang, Shilpi Garg, Rodriguez Milla Miguel, Yoshimi D Barron, Ying Li, Shawn Romanowsky, John C Cushman, Michael Gribskov and 2 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 10% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 92 citations in OpenAlex.

  1. Pooled it
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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

12 authors at 5 institutions in 3 countries.

Amy CurranDepartment of Biochemistry and Molecular Biology, University of Nevada Reno, NV, USA.
Ing-Feng Chang
Chia-Lun Chang
Shilpi Garg
Rodriguez Milla Miguel
Yoshimi D Barron
Ying Li
Shawn Romanowsky
John C Cushman
Michael Gribskov
Alice C Harmon
Jeffrey F Harper
University of Nevada, Reno · USNational Taiwan University · TWCentro de Investigaciones Biológicas Margarita Salas · ESPurdue University West Lafayette · USUniversity of Florida · US

Funding

UNDERGRADUATE RESEARCH AND TRAININGP20RR016464 · NCRR · UNIVERSITY OF NEVADA RENO · PI REIBER, CARL · 2001 to 2011
$30.3M
Ca2+-Pumps in Plants: Pollen Growth and FertilizationR01GM070813 · NIGMS · UNIVERSITY OF NEVADA RENO · PI HARPER, JEFFREY F · 2004 to 2008
$951k
NCRR NIH HHS P20 RR016464NIGMS NIH HHS R01 GM070813
6 · The paper itself

Abstract

The identification of substrates represents a critical challenge for understanding any protein kinase-based signal transduction pathway. In Arabidopsis, there are more than 1000 different protein kinases, 34 of which belong to a family of Ca(2+)-dependent protein kinases (CPKs). While CPKs are implicated in regulating diverse aspects of plant biology, from ion transport to transcription, relatively little is known about isoform-specific differences in substrate specificity, or the number of phosphorylation targets. Here, in vitro kinase assays were used to compare phosphorylation targets of four CPKs from Arabidopsis (CPK1, 10, 16, and 34). Significant differences in substrate specificity for each kinase were revealed by assays using 103 different substrates. For example CPK16 phosphorylated Serine 109 in a peptide from the stress-regulated protein, Di19-2 with K(M) ∼70 μM, but this site was not phosphorylated significantly by CPKs 1, 10, or 34. In contrast, CPKs 1, 10, and 34 phosphorylated 93 other peptide substrates not recognized by CPK16. Examples of substrate specificity differences among all four CPKs were verified by kinetic analyses. To test the correlation between in vivo phosphorylation events and in vitro kinase activities, assays were performed with 274 synthetic peptides that contained phosphorylation sites previously mapped in proteins isolated from plants (in vivo-mapped sites). Of these, 74 (27%) were found to be phosphorylated by at least one of the four CPKs tested. This 27% success rate validates a robust strategy for linking the activities of specific kinases, such as CPKs, to the thousands of in planta phosphorylation sites that are being uncovered by emerging technologies.

Indexed as

calcium-dependent protein kinasephospho-proteomicsphosphorylationsubstrate specificity

Identifiers

PMID22645532
PMCPMC3355778
OpenAlexW2043772373

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.