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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1093/jxb/eraa177 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Phosphorylation of a nuclear condensate regulates cohesion and mRNA retention.
Nat Commun
January 2025
Department of Molecular Life Sciences, University of Zurich, Zurich, Switzerland.
Nuclear speckles are membraneless organelles that associate with active transcription sites and participate in post-transcriptional mRNA processing. During the cell cycle, nuclear speckles dissolve following phosphorylation of their protein components. Here, we identify the PP1 family as the phosphatases that counteract kinase-mediated dissolution.
View Article and Find Full Text PDFLanosterol 14α-Demethylase (CYP51)/Heat Shock Protein 90 (Hsp90) Dual Inhibitors for the Treatment of Invasive Candidiasis.
J Med Chem
January 2025
The Center for Basic Research and Innovation of Medicine and Pharmacy (MOE), School of Pharmacy, Second Military Medical University (Naval Medical University), 325 Guohe Road, Shanghai 200433, China.
Invasive candidiasis has attracted global attention with a high incidence and mortality. Current antifungal drugs are limited by unfavorable therapeutic efficacy, significant hepatorenal toxicity, and the development of drug resistance. Herein, we designed the first generation of lanosterol 14α-demethylase (CYP51)/heat shock protein 90 (Hsp90) dual inhibitors on the basis of antifungal synergism.
View Article and Find Full Text PDFWu-Mei-Wan enhances brown adipose tissue function and white adipose browning in obese mice via upregulation of HSF1.
Chin Med
January 2025
Department of Integrated Traditional Chinese and Western Medicine, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, 430030, Hubei, China.
Background: This research aims to explore the anti-obesity potential of Wu-Mei-Wan (WMW), particularly its effects on adipose tissue regulation in obese mice induced by a high-fat diet (HFD). The study focuses on understanding the role of heat shock factor 1 (HSF1) in mediating these effects.
Methods: HFD-induced obese mice were treated with WMW.
Assessing the efficacy of synthetic compounds foliar sprays in alleviating terminal heat stress in late-sown wheat ().
Funct Plant Biol
January 2025
Krishi Vigyan Kendra, Siwan, Dr. RPCAU, Pusa, Bihar, India.
Detrimental effects of terminal heat stress could be mitigated by exogenous application of synthetic compounds by preserving cell membrane integrity and protecting against oxidative damage. A field experiment was conducted to test the application of seven synthetic compounds on wheat growth traits: (1) thiourea (20 mM and 40mM); (2) potassium nitrate (1% and 2%); (3) sodium nitroprusside (400 μg mL-1 and 800μg mL-1 ); (4) dithiothreitol (25 ppm and 50ppm); (5) salicylic acid (100 ppm and 200ppm); (6) thioglycolic acid (200 ppm and 500ppm); and (7) putrescine (4 mM and 6mM). These compounds were applied at the anthesis and grain-filling stages to enhance physio-biochemical traits and yield attributes of wheat (Triticum aestivum ) cvs GW-11 and GW-496 under terminal heat stress.
View Article and Find Full Text PDFBasic Science and Pathogenesis.
Alzheimers Dement
December 2024
Delaware State University, Dover, DE, USA.
Background: Aggregation of transactive response DNA binding protein 43 (TDP-43) is the major pathological feature of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Recently, in up to 50% of Alzheimer's disease (AD) cases TDP-43 pathology was discovered and this pathology has been referred to as limbic-predominant age-related TDP43 encephalopathy (LATE). Several studies reported that TDP-43 binds to heat shock protein family B (small) member 1 (HSPB1 or HSP27) but no functional evaluation of this interaction has been explored.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!