The Phosphorylation Status of Hsp82 Regulates Mitochondrial Homeostasis During Glucose Sensing in Saccharomyces cerevisiae.
J Mol Biol
; 435(13): 168106, 2023 07 01.
Article
em En
| MEDLINE
| ID: mdl-37068581
ABSTRACT
Sensing extracellular glucose, budding yeast switches from aerobic glycolysis to oxidative phosphorylation to adapt to environmental changes. During the conversion of metabolic mode, mitochondrial function and morphology change significantly. Mitochondria are the main supply factories of energy for various life activities in cells. However, the research on the signal pathways from glucose sensing to changes in mitochondrial function and morphology is still scarce and worthy of further exploration. In this study, we found that in addition to the known involvement of molecular chaperone Hsp82 in stress response during the conversion of metabolic mode, the phosphorylation status of Hsp82 at S485 residue regulates mitochondrial function and morphology to maintain mitochondrial homeostasis. The Hsp82S485A mutant that mimics dephosphorylation at S485 residue showed abnormal growth phenotypes related to mitochondrial defects, such as the petite phenotype, slow growth rates, and inability to use non-fermentable carbon sources. Further exploring the causes of growth defects, we found that the Hsp82S485A mutant caused mitochondrial dysfunction, including a decrease in cellular oxygen consumption rate, defects in mitochondrial electron transport chain, decreased mitochondrial membrane potential and complete loss of mtDNA. Furthermore, the Hsp82S485A mutant displayed fragmented or globular mitochondria, which may be responsible for its mitochondrial dysfunction. Our findings suggested that the phosphorylation status of Hsp82 at S485 residue might regulate mitochondrial function and morphology by affecting the stability of mitochondrial fission and fusion-related proteins. Thus, Hsp82 might be a key molecule in the signal pathway from glucose sensing to changes in mitochondrial function and morphology.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
/
Proteínas de Choque Térmico HSP90
/
Proteínas de Saccharomyces cerevisiae
/
Glucose
/
Mitocôndrias
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article