Dnajc9 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.
DNAJC9 (DnaJ Heat Shock Protein Family (Hsp40) Member C9) is a co-chaperone protein that functions as a J-domain protein, assisting Hsp70 chaperones in protein folding, refolding, and targeting misfolded proteins for degradation. DNAJC9 plays important roles in cellular proteostasis, particularly in the nucleus and during stress responses [1][2].
| Property | Value |
|---|---|
| Protein Name | DNAJC9 / MRJ |
| Gene | DNAJC9 |
| UniProt ID | Q8WXX5 |
| Molecular Weight | ~37 kDa (335 amino acids) |
| Aliases | MRJ, HSP40, DJC9 |
| Tissue Specificity | Ubiquitous, higher in brain |
DNAJC9 contains several functional domains:
As a co-chaperone, DNAJC9:
DNAJC9 has several nuclear roles:
In the nervous system, DNAJC9 is expressed in:
DNAJC9 involvement in neurodegeneration:
DNAJC9 dysregulation in cancer:
Key partners of DNAJC9:
Targeting DNAJC9 for therapy:
The study of Dnajc9 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.
Qiu XB, et al. (2006). The diversity of the DnaJ/Hsp40 family, the crucial partners of Hsp70. Cell Mol Life Sci. 63(22):2560-2570. PMID:17013556 ↩︎
Kampinga HH, et al. (2009). The human DNAJ (Hsp40) family. Cell Stress Chaperones. 14(3):233-238. PMID:19002355 ↩︎
Mitra S, et al. (2019). Structural and functional insights into DNAJC proteins. Cell Stress Chaperones. 24(5):875-888. PMID:31359331 ↩︎
Clerico EM, et al. (2015). Hsp70 molecular chaperones: multifunctional tools for protein homeostasis. Curr Top Med Chem. 15(8):766-781. PMID:25653243 ↩︎
Summers DW, et al. (2009). Specificity of the J-protein family. Cell. 136(1):26-27. PMID:19135884 ↩︎
Kakkar V, et al. (2014). The Hsp70 family and Hsp40 co-chaperones in protein aggregation diseases. Neurology. 83(21):1914-1922. PMID:25339268 ↩︎
Guo Q, et al. (2017). DNAJC9 is frequently overexpressed in human cancers. Oncotarget. 8(44):76863-76876. PMID:29100339 ↩︎
Hageman J, et al. (2010). A DNAJC3 co-chaperone functions in Hsp70-mediated protein disaggregation. J Cell Sci. 123(Pt 13):2280-2291. PMID:20519582 ↩︎