ArticleThe Journal of biological chemistry2019
The ACT domain in chloroplast precursor-phosphorylating STY kinases binds metabolites and allosterically regulates kinase activity.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.
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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.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Identification of the STY13 gene family across the entire genome and an analysis of the essential function of GhSTY13-12 in cotton's response to abiotic stress.Functional & integrative genomics · 2025Article
- A putative membrane-associated YdjB-like protein from Salmonella enterica exhibits a non-canonical ACT-like fold.PloS one · 2025Article
- Loss of Arabidopsis ACR11 results in altered C/N balance and high sensitivity to nitrogen toxicity.Frontiers in plant science · 2025Article
- The activation ofPlant direct · 2024Article
- Coordination of Chloroplast Activity with Plant Growth: Clues Point to TOR.Plants (Basel, Switzerland) · 2022Article
- Characterization of a Novel Creeping Tartary Buckwheat (Frontiers in plant science · 2022Article
- A Cytosolic Protein Kinase STY46 in Arabidopsis thaliana is Involved in Plant Growth and Abiotic Stress Response.Plants (Basel, Switzerland) · 2020Article
- High Light Acclimation Induces Chloroplast Precursor Phosphorylation and Reduces Import Efficiency.Plants (Basel, Switzerland) · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein import of nucleus-encoded proteins into plant chloroplasts is a highly regulated process, requiring fine-tuning mechanisms especially during chloroplast differentiation. One way of altering import efficiency is phosphorylation of chloroplast transit peptides in the cytosol. We recently investigated the role of three serine/threonine/tyrosine (STY) kinases, STY8, STY17, and STY46, in precursor phosphorylation. These three kinases have a high degree of similarity and harbor a conserved aspartate kinase-chorismate mutase-tyrA (prephenate dehydrogenase) (ACT) domain upstream of the kinase domain. The ACT domain is a widely distributed structural motif known to be important for allosteric regulation of many enzymes. In this work, using biochemical and biophysical techniques
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