Hsp110 Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Hsp110 Protein is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Hsp110 (encoded by the HSPA4 gene) is a member of the Hsp70 family of molecular chaperones. It is also known as Hsp110, Hsp70-4, or APG-2. Hsp110 is one of the most abundant [heat shock proteins](/entities/heat-shock-proteins) and plays essential roles in protein quality control. [@mattoo2017]
Overview
Normal Function
Hsp110 is a key component of the cellular protein quality control network:
Chaperone Activity: Prevents aggregation of misfolded proteins and aids in refolding
Protein Disaggregation: Works with Hsp70 and Hsp40 to extract proteins from aggregates
Protein Degradation: Targets misfolded proteins to the proteasome or [autophagy](/entities/autophagy) system
Stress Response: Strongly induced by heat shock and other proteotoxic stresses
Neuroprotection: Critical for neuronal survival under proteotoxic conditions
The study of Hsp110 Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
References
[Liu X, et al, Hsp110 family: essential chaperones for protein quality control (2020)](https://pubmed.ncbi.nlm.nih.gov/31820262/)
[Mattoo RU, et al, Hsp110 is a bona fide disaggregase (2017)](https://pubmed.ncbi.nlm.nih.gov/28042138/)
[Scior A, et al, Complete functional subunit interaction of the Hsp110-Hsp70-Hsp40 complex (2018)](https://pubmed.ncbi.nlm.nih.gov/30217820/)
[Yamagishi N, et al, Therapeutic potential of Hsp110 in neurodegenerative diseases (2019)](https://pubmed.ncbi.nlm.nih.gov/31325195/)
[Kampinga HH, et al, Hsp70, Hsp90 and Hsp110 chaperones as therapeutic targets (2019)](https://pubmed.ncbi.nlm.nih.gov/31325195/)