Page last updated: 2024-10-24

negative regulation of protein polymerization

Definition

Target type: biologicalprocess

Any process that stops, prevents, or reduces the frequency, rate or extent of the process of creating protein polymers. [GOC:mah]

Negative regulation of protein polymerization is a fundamental cellular process that controls the assembly and disassembly of protein complexes. It involves a diverse array of regulatory mechanisms that act to inhibit or reduce the rate of protein polymerization. These mechanisms play critical roles in maintaining cellular homeostasis, regulating cellular processes, and preventing the formation of harmful protein aggregates.

One key mechanism involves the binding of inhibitory proteins to monomeric subunits or oligomers, preventing their further association. These inhibitors can act by sterically hindering the interaction sites required for polymerization or by inducing conformational changes that disrupt the assembly process. Another strategy involves the modification of protein subunits, such as phosphorylation or acetylation, which can alter their affinity for polymerization or their ability to interact with other subunits.

In addition to protein-protein interactions, the cellular environment also plays a significant role in regulating protein polymerization. Factors like pH, temperature, and the presence of specific ions can influence the stability and aggregation of protein subunits. For instance, some proteins require specific ionic conditions for their assembly, while others may be destabilized by high salt concentrations.

The regulation of protein polymerization is crucial for various cellular processes, including cytoskeletal dynamics, signal transduction, and the formation of functional protein complexes. For example, the polymerization of tubulin into microtubules is tightly regulated to ensure proper cell division and migration. Similarly, the assembly of actin filaments is essential for cell motility and the maintenance of cell shape.

Dysregulation of protein polymerization can have serious consequences for cellular function and organismal health. Uncontrolled polymerization can lead to the formation of protein aggregates, which can disrupt cellular processes and contribute to diseases like Alzheimer's and Parkinson's. Conversely, insufficient polymerization can result in the loss of essential cellular structures and functions.

Therefore, the negative regulation of protein polymerization is a complex and essential cellular process that involves a diverse array of molecular mechanisms. Understanding these mechanisms is crucial for comprehending normal cellular function and for developing therapeutic strategies for diseases associated with protein aggregation.'
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Proteins (2)

ProteinDefinitionTaxonomy
Cell division inhibitor SulAA cell division inhibitor SulA that is encoded in the genome of Escherichia coli K-12. [PRO:DNx, UniProtKB:P0AFZ5]Escherichia coli K-12
Voltage-dependent anion-selective channel protein 2A voltage-dependent anion-selective channel protein 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P45880]Homo sapiens (human)

Compounds (3)

CompoundDefinitionClassesRoles
erastinerastin : A member of the class of quinazolines that is quinazolin-4(3H)-one in which the hydrogens at positions 2 and 3 are replaced by 1-{4-[(4-chlorophenoxy)acetyl]piperazin-1-yl}ethyl and 2-ethoxyphenyl groups, respectively. It is an inhibitor of voltage-dependent anion-selective channels (VDAC2 and VDAC3) and a potent ferroptosis inducer.

erastin: an antineoplastic agent; structure in first source
aromatic ether;
diether;
monochlorobenzenes;
N-acylpiperazine;
N-alkylpiperazine;
quinazolines;
tertiary carboxamide
antineoplastic agent;
ferroptosis inducer;
voltage-dependent anion channel inhibitor
novobiocinnovobiocin : A coumarin-derived antibiotic obtained from Streptomyces niveus.

Novobiocin: An antibiotic compound derived from Streptomyces niveus. It has a chemical structure similar to coumarin. Novobiocin binds to DNA gyrase, and blocks adenosine triphosphatase (ATPase) activity. (From Reynolds, Martindale The Extra Pharmacopoeia, 30th ed, p189)
carbamate ester;
ether;
hexoside;
hydroxycoumarin;
monocarboxylic acid amide;
monosaccharide derivative;
phenols
antibacterial agent;
antimicrobial agent;
EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitor;
Escherichia coli metabolite;
hepatoprotective agent
clorobiocinclorobiocin: chlorine-containing antibiotic related to novobiocin