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HSPA8 regulates anti-bacterial autophagy through liquid-liquid phase separation.

Chunhui Miao1, Yajie Zhang1, Mingyu Yu1

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Heat shock protein HSPA8 (heat shock protein family A member 8) stabilizes RHOB and BECN1 proteins, inducing autophagy to clear intracellular bacteria. This discovery reveals HSPA8

Keywords:
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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Immunology

Background:

  • Heat shock protein HSPA8 (heat shock protein family A member 8) is known for protein degradation roles.
  • Its specific function in protein stabilization and anti-bacterial autophagy is not well understood.

Purpose of the Study:

  • To investigate the role of HSPA8 in protein stabilization and anti-bacterial autophagy.
  • To elucidate the mechanism by which HSPA8 modulates autophagy for intracellular bacteria clearance.

Main Methods:

  • Co-immunoprecipitation assays to identify binding partners.
  • Domain mapping to determine binding sites on HSPA8, RHOB, and BECN1.
  • Liquid-liquid phase separation (LLPS) assays to assess droplet formation.
  • Intracellular bacteria clearance assays.

Main Results:

  • HSPA8 binds to RHOB and BECN1, preventing their degradation and inducing autophagy.
  • HSPA8 utilizes its NBD and LID domains for physical binding to specific RHOB residues and the BECN1 ECD domain.
  • HSPA8 promotes LLPS, concentrating RHOB and BECN1 into liquid-phase droplets, enhancing their interaction and stability.
  • The HSPA8-RHOB-BECN1 complex enhances autophagy-mediated clearance of intracellular bacteria.

Conclusions:

  • HSPA8 plays a novel role in anti-bacterial autophagy by stabilizing RHOB and BECN1 through LLPS.
  • The HSPA8-RHOB-BECN1 complex enhances protein interactions and stabilization, improving autophagy-based defense against bacteria.
  • This study advances the understanding of HSPA8's function in cellular defense mechanisms and protein homeostasis.