Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Persulfidation-induced structural change in SnRK2.6 establishes intramolecular interaction between phosphorylation and persulfidation.

Molecular plant - 1 Nov 2021

Chen Sisi, Wang Xiaofeng, Jia Honglei, Li Fali, Ma Ying, Liesche Johannes, Liao Mingzhi, Ding Xueting, Liu Cuixia, Chen Ying, Li Na, Li Jisheng

Abstract excerpt

Post-translational modifications (PTMs), including phosphorylation and persulfidation, regulate the activity of SNF1-RELATED PROTEIN KINASE2.6 (SnRK2.6). Here, we report how persulfidations and phosphorylations of SnRK2.6 influence each other. The persulfidation of cysteine C131/C137 alters SnRK2.6 structure and brings the serine S175 residue closer to the aspartic acid D140 that acts as ATP-γ-phosphate proton...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acclimatization
Share to Arabidopsis Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Droughts

Share to Phosphorus

Share to Protein Kinases

Share to Protein Processing, Post-Translational

Share to Structure-Activity Relationship

Share to Sulfur

Source

Identifiers

PMID: 34242849
DOI: 10.1016/j.molp.2021.07.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Persulfidation-induced structural change in SnRK2.6 establishes intramolecular interaction between phosphorylation and persulfidation.PMID 34242849Read ↗

Hydrogen Sulfide Positively Regulates Abscisic Acid Signaling through Persulfidation of SnRK2.6 in Guard Cells.Semantic proximity Read ↗

Chemical activation of Arabidopsis SnRK2.6 by pladienolide B.Semantic proximity Read ↗

SnRK2.6/OST1 from Arabidopsis thaliana: cloning, expression, purification, crystallization and preliminary X-ray analysis of K50N and D160A mutants.Semantic proximity Read ↗

MAP3Kinase-dependent SnRK2-kinase activation is required for abscisic acid signal transduction and rapid osmotic stress response.Semantic proximity Read ↗

Allelic variation in UVR8 modulates thermotolerance-yield tradeoffs in plants.Semantic proximity Read ↗

A natural variation in OsDSK2a modulates plant growth and salt tolerance through phosphorylation by SnRK1A in rice.Semantic proximity Read ↗

Quantitative phosphoproteomics identifies SnRK2 protein kinase substrates and reveals the effectors of abscisic acid action.Semantic proximity Read ↗

The structure of Arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress.Semantic proximity Read ↗

The SnRK1-JMJ15-CRF6 module integrates energy and mitochondrial signaling to balance growth and the oxidative stress response in Arabidopsis.Semantic proximity Read ↗

Pohsphorylation of MAP4K1 and MAP4K2 by OST1 is required for drought tolerance.Semantic proximity Read ↗

Threonine at position 306 of the KAT1 potassium channel is essential for channel activity and is a target site for ABA-activated SnRK2/OST1/SnRK2.6 protein kinase.Semantic proximity Read ↗

Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in ArabidopsisSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.