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 and plays essential roles in protein quality control. [1]
| Property | Value | [2]
|---|---| [3]
| Protein Name | Hsp110 / Hsp70-4 | [4]
| Gene Symbol | HSPA4 |
| UniProt ID | P34932 |
| Molecular Weight | 94 kDa |
| Structure | N-terminal ATPase domain, C-terminal substrate-binding domain |
| Expression | Ubiquitous, high in brain, heart, testis |
| Subcellular Localization | Cytoplasm, nucleus, organelles |
Hsp110 is a key component of the cellular protein quality control network:
Hsp110 operates through sophisticated mechanisms:
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.
Mattoo RU, et al. Hsp110 is a bona fide disaggregase. Nat Struct Mol Biol. 2017. ↩︎
Scior A, et al. Complete functional subunit interaction of the Hsp110-Hsp70-Hsp40 complex. J Biol Chem. 2018. ↩︎
Yamagishi N, et al. Therapeutic potential of Hsp110 in neurodegenerative diseases. Curr Drug Targets. 2019. ↩︎
Kampinga HH, et al. Hsp70, Hsp90 and Hsp110 chaperones as therapeutic targets. J Cell Mol Med. 2019. ↩︎