negative regulation of supramolecular fiber organization
Definition
Target type: biologicalprocess
Any process that stops, prevents or reduces the frequency, rate or extent of fibril organization. [GO_REF:0000058, GOC:PARL, GOC:rl, GOC:TermGenie, PMID:23921388]
Negative regulation of supramolecular fiber organization is a complex biological process that involves the control of the assembly and disassembly of fibrous structures within cells. These fibers can be composed of various proteins, lipids, and carbohydrates and play crucial roles in maintaining cell shape, motility, and intracellular transport.
The process is tightly regulated by a diverse range of molecular mechanisms, including:
**1. Protein-Protein Interactions:** Specific proteins interact with components of the supramolecular fibers, either promoting or hindering their assembly. These interactions can involve direct binding, post-translational modifications, or the formation of multi-protein complexes.
**2. Post-Translational Modifications:** Modifications like phosphorylation, acetylation, and ubiquitination can alter the conformation and activity of proteins involved in fiber organization, leading to either inhibition or activation of fiber assembly.
**3. Signaling Pathways:** Various signaling pathways, such as the MAPK and PI3K pathways, can trigger downstream events that regulate fiber assembly and disassembly. These pathways often involve the activation of specific kinases or phosphatases that modify the activity of fiber-associated proteins.
**4. Scaffolding Proteins:** Scaffolding proteins can serve as platforms for the assembly of protein complexes involved in fiber organization. By interacting with multiple components, these proteins can facilitate the formation of functional units that regulate fiber dynamics.
**5. Chaperone Proteins:** Chaperone proteins assist in the proper folding and assembly of proteins, ensuring that they adopt the correct conformation necessary for their function in fiber organization. They can also prevent the aggregation of misfolded proteins that could disrupt fiber integrity.
**6. Microenvironment:** The cellular environment plays a crucial role in regulating fiber organization. Factors such as pH, ionic strength, and the presence of specific molecules can influence the stability and assembly of fibers.
**7. External Stimuli:** Cells can respond to external stimuli, like changes in temperature, mechanical stress, or the presence of hormones, by altering their fiber organization. These responses often involve the activation of signaling pathways that trigger downstream events that regulate fiber assembly.
In summary, negative regulation of supramolecular fiber organization involves a complex interplay of molecular mechanisms that fine-tune the assembly and disassembly of fibrous structures. This precise control is essential for maintaining cellular function and responding to diverse environmental cues.'
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Proteins (1)
| 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) |
Compounds (9)
| 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 |