ArticleThe Plant cell2013
Protein S-ACYL Transferase10 is critical for development and salt tolerance in Arabidopsis.
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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.
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.
Who cites it
69 citing papers in PubMed, 138 citations in OpenAlex.
- S-acylation switches the fate of a plant peptide precursor in cell wall damage responses.Science advances · 2026Article
- Genome-wide identification, structural analysis, and heterologous functional inference of FvPAT10, a protein S-acyl transferase in woodland strawberry (Fragaria vesca).BMC plant biology · 2025Article
- Rab5 GTPases mediate the targeting of ROP signalling to establish polarity for pollen germination.Nature plants · 2025Article
- Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025Article
- Integrative analysis of genome-wide association studies of polyphenols in apple fruits identifies the MdDof2.4Horticulture research · 2025Article
- Bioinformatics and Expression Profiling of the DHHC-CRD S-Acyltransferases Reveal Their Roles in Growth and Stress Response in Woodland Strawberry (Plants (Basel, Switzerland) · 2025Article
- Article
- Arabidopsis class A S-acyl transferases modify the pollen receptors LIP1 and PRK1 to regulate pollen tube guidance.The Plant cell · 2024Article
- The S-acylation cycle of transcription factor MtNAC80 influences cold stress responses in Medicago truncatula.The Plant cell · 2024Article
- Aw, snap! How reversible protein lipidation helps plants deal with sudden temperature dives.The Plant cell · 2024Article
- Arabidopsis proteinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Arabidopsis Sar1 isoforms play redundant roles in female gametophytic development.Plant reproduction · 2023Article
- Article
- Salicylic acid attenuates brassinosteroid signaling via protein de-S-acylation.The EMBO journal · 2023Article
- Genetic Variation inInternational journal of molecular sciences · 2022Article
- Protein S-acyltransferases and acyl protein thioesterases, regulation executors of protein S-acylation in plants.Frontiers in plant science · 2022Review
- An ABHD17-like hydrolase screening system to identify de-S-acylation enzymes of protein substrates in plant cells.The Plant cell · 2021Article
- S-acylation of P2K1 mediates extracellular ATP-induced immune signaling in Arabidopsis.Nature communications · 2021Article
- Function of membrane domains in rho-of-plant signaling.Plant physiology · 2021Review
- The canonical α-SNAP is essential for gametophytic development in Arabidopsis.PLoS genetics · 2021Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein S-acylation, commonly known as palmitoylation, is a reversible posttranslational modification that catalyzes the addition of a saturated lipid group, often palmitate, to the sulfhydryl group of a Cys. Palmitoylation regulates enzyme activity, protein stability, subcellular localization, and intracellular sorting. Many plant proteins are palmitoylated. However, little is known about protein S-acyl transferases (PATs), which catalyze palmitoylation. Here, we report that the tonoplast-localized PAT10 is critical for development and salt tolerance in Arabidopsis thaliana. PAT10 loss of function resulted in pleiotropic growth defects, including smaller leaves, dwarfism, and sterility. In addition, pat10 mutants are hypersensitive to salt stresses. We further show that PAT10 regulates the tonoplast localization of several calcineurin B-like proteins (CBLs), including CBL2, CBL3, and CBL6, whose membrane association also depends on palmitoylation. Introducing a C192S mutation within the highly conserved catalytic motif of PAT10 failed to complement pat10 mutants, indicating that PAT10 functions through protein palmitoylation. We propose that PAT10-mediated palmitoylation is critical for vacuolar function by regulating membrane association or the activities of tonoplast proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.