Hspa14 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.
HSPA14 (Heat Shock Protein Family A (Hsp70) Member 14) is a member of the Hsp70 family of molecular chaperones. It is also known as HSP70L1 or Hsp70-like protein. HSPA14 is involved in protein folding, assembly of protein complexes, and cellular stress responses. The gene is located on chromosome 2p22.2 and encodes a protein of approximately 517 amino acids.
| Property |
Value |
| Gene Symbol |
HSPA14 |
| Gene Name |
Heat Shock Protein Family A (Hsp70) Member 14 |
| Alternative Names |
HSP70L1, Hsp70L1, HSP70-14 |
| Chromosomal Location |
2p22.2 |
| NCBI Gene ID |
51282 |
| UniProt ID |
Q9NSE4 |
| Ensembl ID |
ENSG00000174177 |
| Protein Family |
Hsp70 family |
| Molecular Weight |
~56 kDa |
| Amino Acids |
~517 |
HSPA14 contains the conserved Hsp70 domain structure:
- N-terminal ATPase domain (~45 kDa): Binds and hydrolyzes ATP
- Substrate binding domain (~25 kDa): Binds unfolded polypeptides
- C-terminal EEVD motif: Conserved in cytosolic Hsp70s
HSPA14 functions as a molecular chaperone:
- Binds unfolded or misfolded proteins
- Uses ATP hydrolysis for conformational changes
- Facilitates protein refolding
- Prevents protein aggregation
- Assists in protein complex assembly
- Protein quality control
- Stress response
- Cytoprotection
- Immune response modulation
- Antigen processing
- Participates in ribosome-associated quality control
- Involved in mitochondrial protein import
- May have specialized functions in immune cells
HSPA14 in AD:
- May help clear Aβ aggregates
- Chaperone activity can be overwhelmed
- Stress-induced upregulation observed
- Therapeutic potential as co-chaperone target
In PD:
- Assists in α-synuclein clearance
- Protects dopaminergic neurons
- Mitochondrial protein quality control
- LRRK2 interactions studied
- Gene variants under investigation
In ALS:
- Handles misfolded SOD1, FUS, TDP-43
- Protein quality control compromised
- Can be overwhelmed by aggregation
- Hsp70 family as therapeutic target
- Co-chaperone interactions important
¶ Cancer and Neurodegeneration
- HSPA14 elevated in some cancers
- Different expression patterns in cancer vs neurodegeneration
- Potential dual therapeutic targeting
| Strategy |
Approach |
Status |
| Hsp70 activators |
Enhance chaperone activity |
Preclinical |
| Co-chaperone modulators |
Alter Hsp70 complex |
Research |
| Combination therapy |
With Hsp90 inhibitors |
Research |
- Small-molecule Hsp70 activators
- Natural product derivatives
- Peptide-based modulators
- Gene therapy approaches
- Ubiquitous: Expressed in most tissues
- High in: Liver, kidney, brain
- Inducible: Stress-responsive
- Cell-type specific: Higher in dividing cells
- Understanding neuronal-specific functions
- Developing brain-penetrant modulators
- Biomarker potential
- Gene therapy applications
- Combination with protein degradation
The study of Hspa14 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.
- Takayama S, et al. (2003). Hsp70 family in apoptosis. Cell Death Differ. 10(1):26-35.
- Bukau B, et al. (2006). Molecular chaperones and protein quality control. Cell. 125(3):443-451.
- Morimoto RI. (2008). Proteotoxic stress and protein homeostasis. Genes Dev. 22(11):1427-1438.
- Young JC. (2010). Hsp70: functions and applications. J Biosci. 35(3):369-374.
- Hartl FU, et al. (2009). Molecular chaperones in protein folding. Science. 323(5915):821-823.
- Vabulas RM, et al. (2010). Hsp70 in protein aggregation. Cold Spring Harb Perspect Biol. 2(12):a004390.