ArticleCell stress & chaperones2010
Characterization of plant p23-like proteins for their co-chaperone activities.
Article in Cell stress & chaperones, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- RBM14 enhances transcriptional activity of p23 regulating CXCL1 expression to induce lung cancer metastasis.Acta pharmaceutica Sinica. B · 2025Article
- The role of the co-chaperone HOP in plant homeostasis during development and stress.Journal of experimental botany · 2024Review
- The p23 co-chaperone is a succinate-activated COX-2 transcription factor in lung adenocarcinoma tumorigenesis.Science advances · 2023Article
- The anti-oncogenic effect of 17-DMAG via the inactivation of HSP90 and MET pathway in osteosarcoma cells.Oncology research · 2023Article
- Rational design strategies for functional reconstitution of plant cytochrome P450s in microbial systems.Current opinion in plant biology · 2021Review
- Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.Nature communications · 2021Article
- Phosphorylation of p23-1 cochaperone by protein kinase CK2 affects root development in Arabidopsis.Scientific reports · 2019Article
- Review
- The co-chaperone p23 controls root development through the modulation of auxin distribution in the Arabidopsis root meristem.Journal of experimental botany · 2015Article
- The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis.Molecular and cellular biochemistry · 2011Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
The small acidic protein p23 is best described as a co-chaperone of Hsp90, an essential molecular chaperone in eukaryotes. p23 binds to the ATP-bound form of Hsp90 and stabilizes the Hsp90-client protein complex by slowing down ATP turnover. The stabilizing activity of p23 was first characterized in studies of steroid receptor-Hsp90 complexes. Earlier studies of the Hsp90 chaperone complex in plants suggested that a p23-like stabilizing activity was absent in plant cell lysates. Here, we show that p23-like proteins are present in plants and are capable of binding Hsp90, but unlike human p23 and yeast ortholog Sba1, the plant p23-like proteins do not stabilize the steroid receptor-Hsp90 complexes formed in wheat germ lysate. Furthermore, these proteins do not inhibit the ATPase activity of plant Hsp90. While transcripts of Arabidopsis thaliana p23-1 and Atp23-2 were detected under normal growing conditions, those of the closely related Brassica napus p23-1 were present only after moderate heat stress. These observations suggest that p23-like proteins in plants are conserved in their binding to Hsp90 but have evolved mechanisms of action different from their yeast and animal counterparts.
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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.