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title: DNAJC31 Gene
DNAJC31 Gene
Overview
DNAJC31 (DnaJ Heat Shock Protein Family (Hsp40) Member C31) is a member of the DnaJ/Hsp40 family of co-chaperones involved in cellular protein quality control pathways. The DNAJC31 protein contains the characteristic J domain that enables interaction with Hsp70 [heat shock proteins](/entities/heat-shock-proteins), facilitating protein folding, refolding of stress-damaged proteins, and targeting of misfolded proteins for degradation. This gene is expressed in various tissues, with expression in the brain suggesting potential roles in neuronal protein homeostasis. The protein quality control functions of DNAJC31 may be particularly relevant to neurodegenerative disease mechanisms, where proteostasis failure is a key pathological feature. [@klaips2018]
Gene Information
<div class="infobox infobox-gene"> [@hipp2019]
| Property | Value | [@balchin2016] |----------|-------| [@kim2013] | Gene Symbol | DNAJC31 | [@hartl2011] | Full Name | DnaJ Heat Shock Protein Family (Hsp40) Member C31 | [@mayer2005] | Chromosomal Location | 17q25.3 | [@liberek2008] | Gene ID | 345222 | | RefSeq | NM_001012506 | | Protein Length | 298 amino acids | | Molecular Weight | ~32 kDa | | Alternative Names | DNAJC31, DJC31 |
</div>
Protein Structure and Domains
DNAJC31 contains the canonical DnaJ protein domain architecture:
...
title: DNAJC31 Gene
DNAJC31 Gene
Overview
DNAJC31 (DnaJ Heat Shock Protein Family (Hsp40) Member C31) is a member of the DnaJ/Hsp40 family of co-chaperones involved in cellular protein quality control pathways. The DNAJC31 protein contains the characteristic J domain that enables interaction with Hsp70 [heat shock proteins](/entities/heat-shock-proteins), facilitating protein folding, refolding of stress-damaged proteins, and targeting of misfolded proteins for degradation. This gene is expressed in various tissues, with expression in the brain suggesting potential roles in neuronal protein homeostasis. The protein quality control functions of DNAJC31 may be particularly relevant to neurodegenerative disease mechanisms, where proteostasis failure is a key pathological feature. [@klaips2018]
Gene Information
<div class="infobox infobox-gene"> [@hipp2019]
| Property | Value | [@balchin2016] |----------|-------| [@kim2013] | Gene Symbol | DNAJC31 | [@hartl2011] | Full Name | DnaJ Heat Shock Protein Family (Hsp40) Member C31 | [@mayer2005] | Chromosomal Location | 17q25.3 | [@liberek2008] | Gene ID | 345222 | | RefSeq | NM_001012506 | | Protein Length | 298 amino acids | | Molecular Weight | ~32 kDa | | Alternative Names | DNAJC31, DJC31 |
</div>
Protein Structure and Domains
DNAJC31 contains the canonical DnaJ protein domain architecture:
J domain: The N-terminal domain (approximately 70 amino acids) contains the highly conserved HPD (His-Pro-Asp) motif essential for stimulating Hsp70 ATPase activity. This domain mediates the interaction with Hsp70 family proteins.
Glycine-rich flexible region: A flexible linker region between the J domain and C-terminal regions that facilitates protein-protein interactions and provides structural flexibility.
C-terminal client-binding domain: The C-terminal region is predicted to be involved in recognizing and binding unfolded or misfolded client proteins, containing regions that may form coiled-coil structures.
The domain organization follows the typical DnaJ family pattern, with the catalytic J domain at the N-terminus connected to the client-binding region through a flexible glycine-rich linker.
Expression Pattern
DNAJC31 shows broad expression across tissues:
Brain: Expressed in various brain regions including the cerebral [cortex](/brain-regions/cortex), [hippocampus](/brain-regions/hippocampus), basal ganglia, and cerebellum. Both neuronal and glial cell expression has been detected.
Peripheral tissues: Moderate expression in heart, liver, kidney, and skeletal muscle.
Cellular localization: Primarily cytosolic localization, consistent with roles in general protein quality control throughout the cell.
The widespread expression pattern suggests DNAJC31 serves general protein homeostasis functions that are essential across multiple tissue types, with particular importance in cells with high protein synthesis rates.
Molecular Functions
Co-chaperone Activity
DNAJC31 functions as a co-chaperone in protein quality control:
Hsp70 recruitment and activation: The J domain interacts with and stimulates Hsp70 ATPase activity, enabling client protein processing.
Substrate recognition: The C-terminal domains recognize hydrophobic regions in misfolded or partially unfolded proteins.
Protein folding support: DNAJC29 can stabilize folding intermediates and prevent aggregation during the folding process.
Targeted degradation: DNAJC31 can direct misfolded proteins to the [ubiquitin-proteasome system](/mechanisms/ubiquitin-proteasome-system) (UPS) or [autophagy](/entities/autophagy) pathways for degradation.
Cellular Pathways
DNAJC31 participates in several cellular processes:
Cytosolic protein quality control
Targeting proteins to the proteasome for degradation
Coordination with autophagy pathways
Response to proteotoxic stress conditions
Role in Neurodegenerative Diseases
Based on its protein quality control functions, DNAJC31 may play roles in neurodegenerative diseases:
Alzheimer's Disease
Potential involvement in [amyloid-beta](/proteins/amyloid-beta) and [tau protein](/proteins/tau) quality control
General support of neuronal proteostasis
May help maintain synaptic protein homeostasis
Parkinson's Disease
Could assist in [alpha-synuclein](/proteins/alpha-synuclein) aggregate management
May help maintain dopaminergic neuron protein homeostasis
Potential role in mitochondrial protein quality control
Amyotrophic Lateral Sclerosis
May participate in managing ALS-associated protein aggregates ([TDP-43](/mechanisms/tdp-43-proteinopathy), FUS, SOD1)
Could contribute to ER stress response pathways
Potential involvement in RNA-protein complex dynamics
Other Neurodegenerative Conditions
Huntington's disease: Potential management of mutant [huntingtin](/proteins/huntingtin) aggregates
Frontotemporal dementia: Protein quality control in FTD
General neurodegeneration: Age-related proteostasis decline
Therapeutic Implications
DNAJC31 represents a potential therapeutic target:
Chaperone enhancement: Small molecules that enhance DNAJC31 function could improve protein clearance in neurodegeneration.
Expression modulation: Increasing DNAJC31 expression may bolster cellular protein quality control capacity.
Combination therapy: Targeting DNAJC31 with other proteostasis components may provide synergistic benefits.
Biomarker potential: DNAJC31 expression levels could serve as indicators of proteostatic stress.
Research Methods
Investigating DNAJC31 involves:
Gene expression analysis: qRT-PCR, RNA-seq
Protein detection: Western blotting, immunohistochemistry
DNAJC31 is a DnaJ/Hsp40 family co-chaperone involved in cellular protein quality control. Through its J domain-mediated interaction with Hsp70 proteins, DNAJC31 facilitates protein folding, prevents protein aggregation, and targets misfolded proteins for degradation. The expression of DNAJC31 in the brain suggests potential relevance to neuronal protein homeostasis, which is critical for neuronal survival given their post-mitotic nature. While specific roles in neurodegenerative diseases require further investigation, the fundamental importance of protein quality control in neurodegeneration makes DNAJC31 a protein of interest. Understanding DNAJC31's specific functions, client proteins, and regulatory mechanisms may provide insights into therapeutic strategies for enhancing neuronal proteostasis in disease states.
See Also
[Hsp40 Family](/entities/hsp40-family) — DnaJ/Hsp40 co-chaperone family
[Hsp70 Family](/entities/hsp70-family) — Hsp70 molecular chaperone family
[Protein Homeostasis](/mechanisms/protein-homeostasis) — Protein quality control mechanisms
[Unfolded Protein Response](/mechanisms/endoplasmic-reticulum-stress)mechanisms/er-stress-unfolded-protein-response) — Cellular stress response
[Molecular Chaperones](/mechanisms/molecular-chaperones) — Protein folding assistants
[DNAJC Gene Family](/genes) — Other DNAJC genes in NeuroWiki
[Alzheimer's Disease](/diseases/alzheimers-disease) — Protein aggregation in AD
[Parkinson's Disease](/diseases/parkinsons-disease) — Protein homeostasis in PD
[PubMed: DNAJC16](https://pubmed.ncbi.nlm.nih.gov/?term=DNAJC16+neurodegeneration) — Literature search
References
[Kampinga HH et al., Guidelines for the nomenclature of the Hsp70 molecular chaperone family (2009) (2009)](https://pubmed.ncbi.nlm.nih.gov/19765564/)
[Rosenthal LA et al., The DNAJ/Hsp40 family: Key regulators of protein folding and quality control (2011) (2011)](https://pubmed.ncbi.nlm.nih.gov/21693579/)
[Cox D et al., Protein homeostasis in neurodegenerative disease: A strategic opportunity for drug discovery (2020) (2020)](https://pubmed.ncbi.nlm.nih.gov/32744208/)
[Klaips CL et al., Cellular pathways that protect neurons from proteostasis failure (2018) (2018)](https://pubmed.ncbi.nlm.nih.gov/29415856/)
[Hipp MS et al., Proteostasis failure in neurodegenerative diseases: Towards new therapeutic strategies (2019) (2019)](https://pubmed.ncbi.nlm.nih.gov/30605869/)
[Balchin D et al., In vivo aspects of protein folding and quality control (2016) (2016)](https://pubmed.ncbi.nlm.nih.gov/27230645/)
[Kim YE et al., Molecular chaperone functions in protein folding and proteostasis (2013) (2013)](https://pubmed.ncbi.nlm.nih.gov/23650619/)
[Hartl FU et al., Molecular chaperones in protein folding and proteostasis (2011) (2011)](https://pubmed.ncbi.nlm.nih.gov/21616445/)
[Mayer MP et al., Hsp70 chaperones: Cellular functions and molecular mechanism (2005) (2005)](https://pubmed.ncbi.nlm.nih.gov/15893391/)
[Liberek K et al., The DnaJ/DnaK chaperone system in protein quality control (2008) (2008)](https://pubmed.ncbi.nlm.nih.gov/18650913/)