Related Experiment Video

Updated: Mar 6, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

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

Published on: July 21, 2021

3.3K

Mitochondrial chaperone HSP-60 regulates anti-bacterial immunity via p38 MAP kinase signaling

Dae-Eun Jeong1, Dongyeop Lee1, Sun-Young Hwang1

  • 1Department of Life Sciences, Pohang University of Science and Technology, Pohang, Gyeongbuk, Korea.

The EMBO Journal
|March 12, 2017
PubMed

Insights

Mitochondrial chaperone HSP-60 boosts anti-bacterial immunity by up-regulating p38 MAP kinase signaling. This conserved mechanism enhances host defense against pathogens like Pseudomonas aeruginosa.

Area of Science:

  • Cellular and organismal immunity
  • Mitochondrial biology
  • Host-pathogen interactions

Background:

  • Mitochondria are vital for cellular immunity, but their role in organismal immunity is unclear.
  • Understanding mitochondrial contributions to host defense is crucial for combating bacterial infections.

Purpose of the Study:

  • To investigate the role of mitochondrial components in organismal immunity against pathogenic bacteria.
  • To elucidate the molecular mechanisms by which mitochondria enhance anti-bacterial defense.

Main Methods:

  • Screening of conserved mitochondrial components in *Caenorhabditis elegans* for effects on immunity against *Pseudomonas aeruginosa*.
  • Genetic manipulation of HSP-60/HSPD1 and p38 MAP kinase signaling pathway components.
  • Biochemical assays to determine protein interactions and signaling pathway activation in human cells.

Main Results:

  • HSP-60 (HSPD1) is identified as a key mitochondrial chaperone essential for resistance to *P. aeruginosa*.
  • HSP-60 up-regulates the evolutionarily conserved p38 MAP kinase signaling pathway.
  • Cytosolic HSP-60 stabilizes SEK-1/MAP kinase kinase 3, leading to enhanced p38 MAP kinase activity and immunity.

Conclusions:

  • Mitochondrial chaperones, specifically HSP-60, play a significant role in bolstering organismal anti-bacterial immunity.
  • The mechanism involves the up-regulation of cytosolic p38 MAP kinase signaling, conserved across species.
  • This finding reveals a novel link between mitochondrial function and innate immune pathways.
Keywords:
Caenorhabditis elegansPseudomonas aeruginosaHSP‐60mitochondriap38 MAP kinase

More Related Videos

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

9.3K
Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections07:14

Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections

Published on: March 8, 2024

2.0K

Related Concept Videos

Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
646
Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
480
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...
20.6K
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
13.5K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
7.6K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.6K