Target type: biologicalprocess
Any process that activates or increases the frequency, rate or extent of supramolecular fiber organization. [GO_REF:0000058, GOC:PARL, GOC:rl, GOC:TermGenie, PMID:23921388]
Positive regulation of supramolecular fiber organization is a complex biological process that governs the formation, assembly, and maintenance of intricate, multi-component structures known as supramolecular fibers. These fibers are essential for various cellular functions, including cytoskeletal integrity, cell migration, cell signaling, and tissue morphogenesis. The process involves a precise interplay of different molecular components, including proteins, lipids, and nucleic acids.
Key aspects of positive regulation of supramolecular fiber organization include:
1. **Nucleation and Elongation:** The formation of supramolecular fibers begins with the nucleation of monomers or small oligomers. This nucleation event often involves specific protein-protein interactions, and the initial assembly may be influenced by factors such as concentration, pH, and temperature. Once the nucleus is formed, elongation occurs through the addition of further monomers or oligomers to the growing ends of the fiber.
2. **Assembly and Disassembly Dynamics:** The assembly and disassembly of supramolecular fibers is a dynamic process, with constant turnover of components. This dynamic nature allows for the adaptation of the fiber network to changing cellular needs. Factors such as post-translational modifications, chaperone proteins, and regulatory enzymes play crucial roles in modulating the assembly and disassembly rates of fibers.
3. **Fiber Bundling and Cross-linking:** In many cases, individual fibers associate with each other to form larger, more complex bundles. This bundling can be mediated by specific protein-protein interactions, or by the presence of cross-linking molecules that bridge between adjacent fibers. Fiber bundling significantly contributes to the mechanical strength and stability of the supramolecular fiber network.
4. **Spatial Organization and Alignment:** The spatial organization of supramolecular fibers is tightly regulated, ensuring that they are positioned correctly within the cell or tissue. This precise arrangement is often dictated by the cytoskeleton, which provides a framework for fiber assembly and orientation. Specialized proteins and signaling pathways also contribute to the precise spatial organization of these fibers.
5. **Regulation by External Stimuli:** The formation and organization of supramolecular fibers can be influenced by a variety of external stimuli, including changes in cell shape, mechanical stress, and extracellular signals. These stimuli often trigger signaling pathways that ultimately modulate the expression, activity, and interaction of the proteins involved in fiber assembly.
In summary, positive regulation of supramolecular fiber organization is a multifaceted process involving the controlled assembly, disassembly, and organization of protein and other macromolecular complexes into intricate, functionally essential supramolecular fibers. The precise orchestration of this process is essential for a wide range of cellular processes, underscoring its fundamental importance in maintaining cellular and tissue integrity.'
"
Protein | Definition | Taxonomy |
---|---|---|
Glutathione peroxidase 1 | A glutathione peroxidase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P07203] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
cefoperazone | cefoperazone : A semi-synthetic parenteral cephalosporin with a tetrazolyl moiety that confers beta-lactamase resistance. Cefoperazone: Semisynthetic broad-spectrum cephalosporin with a tetrazolyl moiety that is resistant to beta-lactamase. It may be used to treat Pseudomonas infections. | cephalosporin | antibacterial drug |
cefuroxime | 3-(carbamoyloxymethyl)cephalosporin; furans; oxime O-ether | drug allergen | |
ceftriaxone | 1,2,4-triazines; 1,3-thiazoles; cephalosporin; oxime O-ether | antibacterial drug; drug allergen; EC 3.5.2.6 (beta-lactamase) inhibitor | |
ceftizoxime | cephalosporin | antibacterial drug |