Related Experiment Video

Updated: Feb 1, 2026

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
09:39

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

3.7K

Glucose intake hampers PKA-regulated HSP90 chaperone activity

Yu-Chen Chen1, Pei-Heng Jiang1, Hsuan-Ming Chen1

  • 1Department of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan.

Elife
|December 6, 2018
PubMed

Insights

Calorie restriction extends lifespan by regulating protein quality. Researchers found that Ids2 protein, activated by PP2C under calorie restriction, helps maintain protein folding and cell longevity.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Gerontology

Background:

  • Aging involves loss of physiological functions, with nutrient sensing and proteostasis impacting lifespan.
  • Identifying genes governing longevity is crucial, but molecular links between aging pathways remain unclear.

Purpose of the Study:

  • To identify phosphorylation/dephosphorylation sites responding to calorie restriction (CR).
  • To investigate the role of identified regulators in aging and cellular stress response.

Main Methods:

  • Quantitative mass spectrometry to identify protein phosphorylation sites under CR.
  • Functional screening of 135 potential regulators.
  • Assessing heat sensitivity and lifespan in yeast strains with altered Ids2 activity.

Main Results:

  • Identified protein phosphorylation sites responding to CR.
  • Uncovered Ids2 activation by PP2C under CR and inactivation by PKA with glucose intake.
  • Ids2 acts as a co-chaperone with Hsc82/Hsp82; phosphorylation hinders HSP90 association.

Conclusions:

  • Ids2 plays a role in cellular stress response and lifespan regulation.
  • PP2C and PKA may coordinate glucose sensing and protein folding for sustained longevity.
  • Ids2 phosphorylation status is critical for its function in maintaining protein quality.
Keywords:
S. cerevisiaecalorie restrictioncell biologychaperonephosphorylation

More Related Videos

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

3.2K
Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

9.2K

Related Concept Videos

Regulation of Water Intake01:25

Regulation of Water Intake

Osmolality refers to the number of solute particles per kilogram of solvent in a solution. Plasma osmolality specifically indicates the total number of solute particles per kilogram of water in blood plasma. This value reflects the body's hydration status and is tightly regulated through mechanisms controlling water intake and output. While water consumption is a conscious decision, the body has intrinsic regulatory systems to maintain fluid balance. Dehydration, a state of water deficit...
2.8K
Regulation of Food Intake01:30

Regulation of Food Intake

Short-term regulation of food intake primarily involves neural signals from the gastrointestinal (GI) tract, blood nutrient levels, and GI tract hormones. Communication between the gut and brain via vagal nerve fibers plays a significant role in evaluating the contents of the gut. Clinical studies have shown that protein ingestion produces a more prolonged response in these nerve fibers compared to an equivalent amount of glucose. Additionally, the activation of stretch receptors caused by GI...
2.9K
Glucose Homeostasis: Regulation of Blood Glucose01:02

Glucose Homeostasis: Regulation of Blood Glucose

Carbohydrates consumed through foods are converted into glucose, a crucial energy source for the body. In the prandial state, high blood glucose levels stimulate the secretion of insulin from the pancreas. Insulin inhibits hepatic glucose production and stimulates glucose uptake and metabolism by muscle and adipose tissue. The excess glucose is converted into glycogen and stored in the liver and muscles.
During fasting, when blood glucose levels are low, the pancreas secretes glucagon. it...
4.1K
Hormones Regulating Blood Glucose01:16

Hormones Regulating Blood Glucose

Insulin is released by beta cells of the pancreas when blood glucose levels are high. It facilitates glucose absorption and utilization in insulin-dependent cells with insulin receptors on their plasma membranes. Insulin promotes glucose uptake by increasing the number of glucose transport proteins in the cell membrane, allowing glucose to enter the cell. As a result, glucose utilization and ATP production are enhanced.
In addition to accelerating glucose uptake and utilization, insulin has...
6.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.0K