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Functional diversity between HSP70 paralogs caused by variable interactions with specific co-chaperones.

Despina Serlidaki1, Maria A W H van Waarde1, Lukas Rohland2

  • 1Department of Biomedical Sciences of Cells and Systems, University Medical Center Groningen, University of Groningen, 9713 AV Groningen, The Netherlands.

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Two human heat shock protein 70 (HSP70) variants, HSPA1A and HSPA1L, show opposing effects on protein aggregation, challenging the assumption of functional redundancy among HSP70 paralogs.

Keywords:
70 kilodalton heat shock protein (Hsp70)HSPA4HSPH2Hsp110amyotrophic lateral sclerosis (ALS) (Lou Gehrig disease)heat shock protein (HSP)protein foldingproteostasissuperoxide dismutase (SOD)

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Protein Homeostasis

Background:

  • Heat shock protein 70 (HSP70) chaperones are essential for protein quality control, including folding, degradation, and disaggregation.
  • Human HSP70s comprise 13 members that function with co-chaperones, with their interplay dictating substrate fate.
  • It was previously assumed that HSP70 paralogs possess similar functions and are largely redundant.

Purpose of the Study:

  • To investigate the functional diversity of highly homologous HSP70 paralogs, HSPA1A and HSPA1L, in human cells.
  • To determine the mechanisms underlying differential substrate handling by HSPA1A and HSPA1L.
  • To explore the role of co-chaperone interactions in modulating HSP70 function.

Main Methods:

  • Expression of HSPA1A and HSPA1L in human cells.
  • Analysis of substrate aggregation, focusing on the amyotrophic lateral sclerosis-associated protein variant superoxide dismutase 1 (SOD1)-A4V.
  • Co-immunoprecipitation assays to assess interactions between HSP70s and co-chaperones, including Hsp70/Hsp90-organizing protein (HOP) and HSPH2.

Main Results:

  • HSPA1A reduced SOD1-A4V aggregation, while HSPA1L enhanced it, demonstrating opposing effects.
  • Differences in substrate handling were not attributed to variations in the substrate-binding domain.
  • Differential co-chaperone binding determined substrate fate; HOP preferentially bound HSPA1L, and HSPH2 preferred HSPA1A.
  • HSPH2 played a critical role in the HSPA1A-mediated reduction of SOD1-A4V aggregation.

Conclusions:

  • Human HSP70 paralogs exhibit significant functional diversity, contrary to previous assumptions of redundancy.
  • Differential affinities for specific co-chaperones, such as HSPH2, define the distinct cellular roles of HSP70s.
  • This highlights the importance of co-chaperone interactions in fine-tuning protein quality control pathways.