DNAJC23 (DnaJ Heat Shock Protein Family Member C23), also known as ERdj5, is a co-chaperone protein critically involved in protein folding and quality control mechanisms within the cell. It belongs to the DNAJ/Hsp40 family which assists Hsp70 chaperones in protein refolding and degradation pathways[1].
| Property | Value |
|---|---|
| Gene Symbol | DNAJC23 |
| Gene Name | DnaJ Heat Shock Protein Family Member C23 |
| Aliases | ERdj5, TIMM44 |
| Chromosomal Location | 17q25.3 |
| NCBI Gene ID | 55829 |
| UniProt ID | Q8N5Z0 |
| Gene Type | Protein Coding |
DNAJC23 contains several functional domains essential for its chaperone activity:
The J domain is the defining feature of DNAJ proteins and is essential for interaction with Hsp70 family chaperones[2].
DNAJC23 performs critical cellular functions in protein homeostasis:
DNAJC23 is expressed in various tissues with high metabolic activity:
In neurons, DNAJC23 is particularly important due to:
DNAJC23 contributes to neurodegenerative disease pathogenesis through multiple interconnected mechanisms:
The ERAD pathway is crucial for clearing misfolded proteins that accumulate in neurodegenerative diseases:
Chronic ER stress is a hallmark of neurodegeneration:
DNAJC23's involvement in mitochondrial protein import affects:
| Disease | Evidence Level | Mechanism |
|---|---|---|
| Alzheimer's Disease | Moderate | ER stress, protein quality control |
| Parkinson's Disease | Moderate | Mitochondrial function, aggregation handling |
| Neurodegeneration (general) | Moderate | Protein homeostasis disruption |
DNAJC23 interacts with several key proteins:
| Protein | Interaction Type | Functional Role |
|---|---|---|
| BiP/GRP78 | Hsp70 partner | ER chaperone function |
| Hsp70 family | Chaperone recruitment | Protein folding |
| Derlin proteins | ERAD component | Retrotranslocation |
| PDI | Quality control | Protein folding |
DNAJC23 represents a potential therapeutic target:
Qiu XB et al. ERdj5 is a novel ER-resident DnaJ protein that regulates protein folding. 2006. ↩︎
Kampinga HH et al. The Hsp70 family: functions, structure, and clinical implications. 2009. ↩︎