Multifaceted roles of HEAT SHOCK PROTEIN 90 molecular chaperones in plant development
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
32293686
DOI
10.1093/jxb/eraa177
PII: 5817050
Knihovny.cz E-resources
- Keywords
- Chaperone, HEAT SHOCK PROTEIN 90, client protein, co-chaperone, plant cell, plant development, protein kinase,
- MeSH
- Phenotype MeSH
- Genotype MeSH
- Molecular Chaperones genetics MeSH
- HSP90 Heat-Shock Proteins * genetics MeSH
- Plant Development * MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Molecular Chaperones MeSH
- HSP90 Heat-Shock Proteins * MeSH
HEAT SHOCK PROTEINS 90 (HSP90s) are molecular chaperones that mediate correct folding and stability of many client proteins. These chaperones act as master molecular hubs involved in multiple aspects of cellular and developmental signalling in diverse organisms. Moreover, environmental and genetic perturbations affect both HSP90s and their clients, leading to alterations of molecular networks determining respectively plant phenotypes and genotypes and contributing to a broad phenotypic plasticity. Although HSP90 interaction networks affecting the genetic basis of phenotypic variation and diversity have been thoroughly studied in animals, such studies are just starting to emerge in plants. Here, we summarize current knowledge and discuss HSP90 network functions in plant development and cellular homeostasis.
References provided by Crossref.org
Regulation of heat shock proteins 70 and their role in plant immunity
HEAT SHOCK PROTEIN 90 proteins and YODA regulate main body axis formation during early embryogenesis
Barley Root Proteome and Metabolome in Response to Cytokinin and Abiotic Stimuli
HSP90 chaperones regulate stomatal differentiation under normal and heat stress conditions
