Target type: biologicalprocess
Any process that affects the structure and integrity of a protein complex by altering the likelihood of its assembly or disassembly. [GOC:dph]
Regulation of protein complex stability is a fundamental process in cellular life, ensuring the proper assembly, function, and disassembly of these essential molecular machines. It involves a complex interplay of various factors, including:
**1. Protein-Protein Interactions:** The stability of protein complexes is primarily determined by the strength and specificity of interactions between their constituent proteins. These interactions can be mediated by various forces, including:
* **Hydrophobic interactions:** Non-polar amino acid residues tend to cluster together, excluding water molecules and contributing to complex stability.
* **Electrostatic interactions:** Oppositely charged amino acid residues can form salt bridges, enhancing complex stability.
* **Hydrogen bonding:** Polar amino acid residues can form hydrogen bonds, contributing to the overall stability of the complex.
**2. Post-Translational Modifications:** Modifications to proteins after translation, such as phosphorylation, acetylation, and ubiquitination, can significantly impact complex stability. These modifications can:
* **Alter protein-protein interactions:** Modifications can create or disrupt binding sites, affecting complex assembly or disassembly.
* **Induce conformational changes:** Modifications can alter the conformation of a protein, influencing its interaction with other proteins.
* **Recruit chaperones:** Modifications can act as signals for chaperones to assist in complex assembly or disassembly.
**3. Chaperones:** Chaperones are a diverse group of proteins that play crucial roles in protein folding and assembly. They can:
* **Assist in folding:** Chaperones help proteins adopt their correct conformation, facilitating complex formation.
* **Prevent aggregation:** Chaperones can prevent misfolded proteins from aggregating, maintaining the integrity of protein complexes.
* **Mediate complex disassembly:** Chaperones can facilitate the release of specific subunits from a complex, regulating its stability.
**4. Ligands and Cofactors:** The binding of ligands or cofactors can also modulate protein complex stability. Ligands can:
* **Stabilize complexes:** Ligands can bind to specific sites on proteins, increasing the affinity between subunits and stabilizing the complex.
* **Induce conformational changes:** Ligands can induce changes in the conformation of proteins, influencing their interactions with other subunits.
* **Promote complex disassembly:** Ligands can bind to specific sites on proteins, triggering the release of subunits and leading to complex disassembly.
**5. Cellular Environment:** The cellular environment plays a significant role in regulating protein complex stability. Factors such as:
* **Temperature:** Elevated temperatures can destabilize protein complexes, promoting their disassembly.
* **pH:** Changes in pH can disrupt protein interactions, affecting complex stability.
* **Ionic strength:** Changes in ionic strength can influence electrostatic interactions, impacting complex stability.
**6. Ubiquitination and Proteasomal Degradation:** Ubiquitination is a post-translational modification that targets proteins for degradation by the proteasome. Ubiquitination can:
* **Destabilize complexes:** Ubiquitination can tag specific subunits within a complex for degradation, leading to complex disassembly.
* **Promote complex assembly:** Ubiquitination can also regulate the levels of specific proteins, influencing the availability of subunits for complex formation.
**7. Autophagy:** Autophagy is a cellular process that involves the degradation of cellular components within lysosomes. Autophagy can:
* **Remove damaged complexes:** Autophagy can selectively target damaged or misassembled protein complexes for degradation.
* **Regulate complex stability:** Autophagy can contribute to the turnover of specific proteins, indirectly influencing the stability of protein complexes.
The regulation of protein complex stability is a dynamic and intricate process, essential for maintaining cellular homeostasis and function. By understanding the mechanisms that govern complex stability, we can gain insights into the underlying causes of disease and develop novel therapeutic strategies.'
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Protein | Definition | Taxonomy |
---|---|---|
Heat shock cognate 71 kDa protein | A heat shock cognate 71 kDa protein that is encoded in the genome of human. [PRO:DAN] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
adenosine diphosphate | Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. | adenosine 5'-phosphate; purine ribonucleoside 5'-diphosphate | fundamental metabolite; human metabolite |
tubercidin | tubercidin : An N-glycosylpyrrolopyrimidine that is adenosine in which the in the 5-membered ring that is not attached to the ribose moiety is replaced by a carbon. Tubercidin is produced in the culture broth of Streptomyces tubericidus. Tubercidin: An antibiotic purine ribonucleoside that readily substitutes for adenosine in the biological system, but its incorporation into DNA and RNA has an inhibitory effect on the metabolism of these nucleic acids. | antibiotic antifungal agent; N-glycosylpyrrolopyrimidine; ribonucleoside | antimetabolite; antineoplastic agent; bacterial metabolite |
toyocamycin | toyocamycin : An N-glycosylpyrrolopyrimidine that is tubercidin in which the hydrogen at position 5 of the pyrrolopyrimidine moiety has been replaced by a cyano group. Toyocamycin: 4-Amino-5-cyano-7-(D-ribofuranosyl)-7H- pyrrolo(2,3-d)pyrimidine. Antibiotic antimetabolite isolated from Streptomyces toyocaensis cultures. It is an analog of adenosine, blocks RNA synthesis and ribosome function, and is used mainly as a tool in biochemistry. | antibiotic antifungal agent; N-glycosylpyrrolopyrimidine; nitrile; ribonucleoside | antimetabolite; antineoplastic agent; apoptosis inducer; bacterial metabolite |
nsc 65346 | sangivamycin : A nucleoside analogue that is adenosine in which the nitrogen at position 7 is replaced by a carbamoyl-substituted carbon. It is a potent inhibitor of protein kinase C. sangivamycin: RN given refers to parent cpd | nucleoside analogue | protein kinase inhibitor |
adenosine | quinquefolan B: isolated from roots of Panax quinquefolium L.; RN not in Chemline 10/87; RN from Toxlit | adenosines; purines D-ribonucleoside | analgesic; anti-arrhythmia drug; fundamental metabolite; human metabolite; vasodilator agent |
8-aminoadenosine | |||
5'-deoxyadenosine | 5'-deoxyadenosine : A 5'-deoxyribonucleoside compound having adenosine as the nucleobase. 5'-deoxyadenosine: main heading DEOXYADENOSINE refers to the 3' cpd | 5'-deoxyribonucleoside; adenosines | Escherichia coli metabolite; human metabolite; mouse metabolite |
ver 155008 | VER 155008: structure in first source | purine nucleoside | |
nms-e973 | NMS-E973: structure in first source |