Evidence map›Paper›PMID 31745110›Full record

ArticleScientific reports2019

Ubiquitin carboxyl-terminal hydrolases are required for period maintenance of the circadian clock at high temperature in Arabidopsis.

Ryosuke Hayama, Peizhen Yang, Federico Valverde, Tsuyoshi Mizoguchi, Ikuyo Furutani-Hayama, Richard D Vierstra, George Coupland

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 46 citations in OpenAlex.

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  15. A combination of QTL mapping and genome-wide association study revealed the key gene for husk number in maize.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
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  19. Genetic Analyses of Seed Longevity inPlants (Basel, Switzerland) · 2023
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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

7 authors at 4 institutions in 4 countries.

Ryosuke HayamaDepartment of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, D-50829, Cologne, Germany. hryosuke@icu.ac.jp.
Peizhen YangDepartment of Genetics, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA.
Federico ValverdeDepartment of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, D-50829, Cologne, Germany.ORCID http://orcid.org/0000-0001-8063-0974
Tsuyoshi MizoguchiDepartment of Natural Sciences, International Christian University, 3-10-2 Osawa, Mitaka, 181-8585, Tokyo, Japan.
Ikuyo Furutani-HayamaDepartment of Natural Sciences, International Christian University, 3-10-2 Osawa, Mitaka, 181-8585, Tokyo, Japan.
Richard D VierstraDepartment of Genetics, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA.
George CouplandDepartment of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, D-50829, Cologne, Germany. coupland@mpipz.mpg.de.
International Christian University · JPUniversity of Wisconsin–Madison · USInstituto de Bioquímica Vegetal y Fotosíntesis · ESMax Planck Institute for Plant Breeding Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein ubiquitylation participates in a number of essential cellular processes including signal transduction and transcription, often by initiating the degradation of specific substrates through the 26S proteasome. Within the ubiquitin-proteasome system, deubiquitylating enzymes (DUBs) not only help generate and maintain the supply of free ubiquitin monomers, they also directly control functions and activities of specific target proteins by modulating the pool of ubiquitylated species. Ubiquitin carboxyl-terminal hydrolases (UCHs) belong to an enzymatic subclass of DUBs, and are represented by three members in Arabidopsis, UCH1, UCH2 and UCH3. UCH1 and UCH2 influence auxin-dependent developmental pathways in Arabidopsis through their deubiquitylation activities, whereas biological and enzymatic functions of UCH3 remain unclear. Here, we demonstrate that Arabidopsis UCH3 acts to maintain the period of the circadian clock at high temperatures redundantly with UCH1 and UCH2. Whereas single uch1, uch2 and uch3 mutants have weak circadian phenotypes, the triple uch mutant displays a drastic lengthening of period at high temperatures that is more extreme than the uch1 uch2 double mutant. UCH3 also possesses a broad deubiquitylation activity against a range of substrates that link ubiquitin via peptide and isopeptide linkages. While the protein target(s) of UCH1-3 are not yet known, we propose that these DUBs act on one or more factors that control period length of the circadian clock through removal of their bound ubiquitin moieties, thus ensuring that the clock oscillates with a proper period even at elevated temperatures.

Indexed as

ArabidopsisCircadian ClocksDeubiquitinating EnzymesGene Expression Regulation, PlantHot TemperatureSignal TransductionUbiquitinUbiquitinationUbiquitin ThiolesteraseDeubiquitinating EnzymesUbiquitinUbiquitin Thiolesterase

Identifiers

PMID31745110
PMCPMC6863813
OpenAlexW2989949238

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LicenceCC BY
Read underepoch 390

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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.