Evidence map›Paper›PMID 19837819›Full record

ArticlePlant physiology2009

Specific domain structures control abscisic acid-, salicylic acid-, and stress-mediated SIZ1 phenotypes.

Mi Sun Cheong, Hyeong Cheol Park, Mi Ju Hong, Jiyoung Lee, Wonkyun Choi, Jing Bo Jin, Hans J Bohnert, Sang Yeol Lee, Ray A Bressan, Dae-Jin Yun

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

36 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
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    Article
  4. Nitrate-induced NLP1 SUMOylation regulates nitrate signaling and root nodulation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  8. Review
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  11. Cells · 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

10 authors at 3 institutions in 3 countries.

Mi Sun CheongDivision of Applied Life Science (Brain Korea 21 Program), PMBBRC, EB-NCRC, Gyeongsang National University, Jinju City 660-701, Korea.
Hyeong Cheol Park
Mi Ju Hong
Jiyoung Lee
Wonkyun Choi
Jing Bo Jin
Hans J Bohnert
Sang Yeol Lee
Ray A Bressan
Dae-Jin Yun
Institute of Botany · CNGyeongsang National University · KRPurdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SIZ1 (for yeast SAP and MIZ1) encodes the sole ortholog of mammalian PIAS (for protein inhibitor of activated STAT) and yeast SIZ SUMO (for small ubiquitin-related modifier) E3 ligases in Arabidopsis (Arabidopsis thaliana). Four conserved motifs in SIZ1 include SAP (for scaffold attachment factor A/B/acinus/PIAS domain), PINIT (for proline-isoleucine-asparagine-isoleucine-threonine), SP-RING (for SIZ/PIAS-RING), and SXS (for serine-X-serine, where X is any amino acid) motifs. SIZ1 contains, in addition, a PHD (for plant homeodomain) typical of plant PIAS proteins. We determined phenotypes of siz1-2 knockout mutants transformed with SIZ1 alleles carrying point mutations in the predicted domains. Domain SP-RING is required for SUMO conjugation activity and nuclear localization of SIZ1. Salicylic acid (SA) accumulation and SA-dependent phenotypes of siz1-2, such as diminished plant size, heightened innate immunity, and abscisic acid inhibition of cotyledon greening, as well as SA-independent basal thermotolerance were not complemented by the altered SP-RING allele of SIZ1. The SXS domain also controlled SA accumulation and was involved in greening and expansion of cotyledons of seedlings germinated in the presence of abscisic acid. Mutations of the PHD zinc finger domain and the PINIT motif affected in vivo SUMOylation. Expression of the PHD and/or PINIT domain mutant alleles of SIZ1 in siz1-2 promoted hypocotyl elongation in response to sugar and light. The various domains of SIZ1 make unique contributions to the plant's ability to cope with its environment.

Indexed as

Abscisic AcidAdaptation, PhysiologicalArabidopsisArabidopsis ProteinsCarbohydratesCotyledonGenetic Complementation TestGerminationHeat-Shock ResponseHypocotylLigasesLightModels, BiologicalMutationPhenotypePlant LeavesAbscisic AcidArabidopsis ProteinsCarbohydratesLigasesSalicylic AcidSIZ1 protein, Arabidopsis

Identifiers

PMID19837819
PMCPMC2785975
OpenAlexW1972299678

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.