Target type: molecularfunction
Binding to a BAT3 complex. [GOC:bf, GOC:PARL, GOC:TermGenie, PMID:23246001]
The BAT3 complex, also known as the BAG6-BAT3-TRIM33 complex, plays a crucial role in the ubiquitination and subsequent degradation of misfolded proteins in the endoplasmic reticulum (ER). This complex functions through several key molecular activities:
1. **Protein Recognition:** BAT3 serves as a scaffold protein, recognizing and binding misfolded proteins within the ER lumen. Its interaction with these substrates is often mediated by the C-terminal domain, which contains a conserved domain known as the BAG domain. This domain interacts with the chaperone protein Hsc70, facilitating the initial recognition and capture of misfolded proteins.
2. **Ubiquitination:** The BAT3 complex recruits the E3 ubiquitin ligase TRIM33, which is responsible for attaching ubiquitin chains to the misfolded proteins. This ubiquitination event signals the targeted protein for degradation.
3. **ER-Associated Degradation (ERAD):** Once ubiquitinated, the misfolded proteins are extracted from the ER lumen and transported to the cytoplasm. The BAT3 complex, in collaboration with other ERAD components, aids in this extraction process, ensuring the misfolded proteins are delivered to the proteasome for degradation.
4. **Quality Control:** Through its role in ERAD, the BAT3 complex contributes to the overall quality control of protein folding in the ER. By removing misfolded proteins, the complex prevents the accumulation of potentially harmful molecules that could disrupt cellular function.
5. **Cellular Stress Response:** The BAT3 complex is also implicated in the cellular response to stress conditions, such as ER stress. It can act as a sensor for ER stress and contribute to the unfolded protein response (UPR), a complex signaling pathway that aims to restore ER homeostasis.
In summary, the BAT3 complex plays a vital role in protein quality control within the ER by recognizing, ubiquitinating, and targeting misfolded proteins for degradation via the ERAD pathway. It is a crucial player in maintaining cellular homeostasis and responding to cellular stress.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase 13 | A ubiquitin carboxyl-terminal hydrolase 13 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q92995] | Homo sapiens (human) |
| Transitional endoplasmic reticulum ATPase | A transitional endoplasmic reticulum ATPase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P55072] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| clotrimazole | conazole antifungal drug; imidazole antifungal drug; imidazoles; monochlorobenzenes | antiinfective agent; environmental contaminant; xenobiotic | |
| Methylenedioxycinnamic acid | hydroxycinnamic acid | ||
| 3,4-methylenedioxy-beta-nitrostyrene | 3,4-methylenedioxy-beta-nitrostyrene: tyrosine kinase inhibitor that prevents platelet glycoprotein IIb/IIIa activation; structure in first source | ||
| 4-(4-(4-chloro-phenyl)thiazol-2-ylamino)phenol | substituted aniline | ||
| ML240 | ML240 : A member of the class of quinazolines that is quinazoline which is substituted at positions 2, 5 and 8 by 2-amino-1H-benzimidazol-1-yl, benzylnitrilo and methoxy groups, respectively. It is a ATP-competetive inhibitor of AAA ATPase p97, also known as valosin-containing protein (VCP). | aromatic amine; aromatic ether; benzimidazoles; primary amino compound; quinazolines; secondary amino compound | antineoplastic agent |
| spautin-1 | |||
| ganciclovir | 2-aminopurines; oxopurine | antiinfective agent; antiviral drug |