Hsp90Aa1 Gene is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
| HSP90AA1 - Heat Shock Protein 90 Alpha Family Class A Member 1 | |
|---|---|
| Full Name | Heat Shock Protein 90 Alpha Family Class A Member 1 |
| Chromosomal Location | 14q32.31 |
| NCBI Gene ID | 3320 |
| Ensembl ID | ENSG00000100425 |
| UniProt ID | P07900 |
| Associated Diseases | Alzheimer's Disease, Parkinson's Disease, ALS, Huntington's Disease |
The HSP90AA1 gene encodes Hsp90α, a molecular chaperone that constitutes approximately 1-2% of total cellular protein. Hsp90 is essential for the folding and stability of numerous client proteins, many of which are involved in signal transduction and neurodegeneration[1].
Hsp90 functions as a molecular chaperone:
Hsp90 contains multiple domains:
Hsp90 is expressed in all cell types:
The study of Hsp90Aa1 Gene 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.
HSP90AA1 (Heat Shock Protein 90 Alpha Family Class A Member 1) is a 854-amino acid molecular chaperone that constitutes ~1-2% of total cellular protein. As part of the Hsp90 family, it plays a crucial role in protein folding and quality control:
HSP90 clients relevant to neurodegeneration include:
Taipale M, et al. The Hsp90 chaperone. Cold Spring Harb Perspect Biol. 2014;6(8):a013920. PMID:25190254 ↩︎
Karagoz GE, Rutherford SL. Hsp90 and the proteostasis. Nat Rev Mol Cell Biol. 2014;15(8):507-511. PMID:25134683 ↩︎
Chen HJ, et al. Hsp90 and ALS. Nat Rev Neurol. 2015;11(7):383-384. PMID:26100736 ↩︎