Evidence map›Paper›PMID 38153765›Full record

ArticlePlant & cell physiology2024

Arabidopsis HECT and RING-type E3 Ligases Promote MAPKKK18 Degradation to Regulate Abscisic Acid Signaling.

Małgorzata Tajdel-Zielińska, Maciej Janicki, Małgorzata Marczak, Agnieszka Ludwików

Open access · hybridAbstract read
In one paragraph

Article in Plant & cell physiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
5.6field-weighted citation impact, top 5% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
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  4. Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  5. Article
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  11. International journal of molecular sciences · 2024
    Article
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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

4 authors at 1 institution in 1 country.

Małgorzata Tajdel-ZielińskaLaboratory Biotechnology, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University Poznan, Uniwersytetu Poznańskiego 6, Poznań 61-614, Poland.ORCID 0000-0003-1203-2029
Maciej JanickiLaboratory Biotechnology, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University Poznan, Uniwersytetu Poznańskiego 6, Poznań 61-614, Poland.ORCID 0000-0001-7800-2792
Małgorzata MarczakLaboratory Biotechnology, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University Poznan, Uniwersytetu Poznańskiego 6, Poznań 61-614, Poland.ORCID 0000-0002-0221-5342
Agnieszka LudwikówLaboratory Biotechnology, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University Poznan, Uniwersytetu Poznańskiego 6, Poznań 61-614, Poland.ORCID 0000-0002-6393-544X
Adam Mickiewicz University in Poznań · PL

Funding

Faculty of Biology, AMU GDWB-08/2015KNOW Poznan RNA Centre 01/KNOW2/2014The Center of European Projects POWR.03.02.00-00-I006/17The National Science Centre, Poland 2012/05/B/NZ3/00352 2015/17/N/NZ3/00532
6 · The paper itself

Abstract

Mitogen-activated protein kinase (MAPK) cascades are conserved signaling pathways that transduce extracellular signals into diverse cellular responses. Arabidopsis MAPKKK18 is a component of the MAPKKK17/18-MKK3-MPK1/2/7/14 cascades, which play critical roles in abscisic acid (ABA) signaling, drought tolerance and senescence. A very important aspect of MAP kinase signaling is both its activation and its termination, which must be tightly controlled to achieve appropriate biological responses. Recently, the ubiquitin-proteasome system (UPS) has received increasing attention as a key mechanism for maintaining the homeostasis of MAPK cascade components and other ABA signaling effectors. Previous studies have shown that the stability of MAPKKK18 is regulated by the UPS via the ABA core pathway. Here, using multiple proteomic approaches, we found that MAPKKK17/18 turnover is tightly controlled by three E3 ligases, UPL1, UPL4 and KEG. We also identified lysines 154 and 237 as critical for MAPKKK18 stability. Taken together, this study sheds new light on the mechanism that controls MAPKKK17/18 activity and function.

Indexed as

ArabidopsisArabidopsis ProteinsAbscisic AcidMAP Kinase Kinase KinasesProteasome Endopeptidase ComplexProteomicsUbiquitinUbiquitin-Protein LigasesAbscisic AcidArabidopsis ProteinsKEG protein, ArabidopsisMAP Kinase Kinase KinasesMAPKKK18 protein, ArabidopsisProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesABAE3 ligasesMAP kinase cascadesMAPKKK17/18UbiquitinationUPS

Identifiers

PMID38153765
PMCPMC11020294
OpenAlexW4390311704

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.