Page last updated: 2024-10-24

positive regulation of proteolysis involved in protein catabolic process

Definition

Target type: biologicalprocess

Any process that activates or increases the frequency, rate or extent of proteolysis involved in protein catabolic process. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:18307834]

Positive regulation of proteolysis involved in protein catabolic process is a complex and multifaceted biological process essential for cellular homeostasis and function. It involves the coordinated action of various regulatory mechanisms that control the breakdown of proteins, a critical aspect of protein catabolism. This regulation ensures that proteolysis occurs in a controlled and specific manner, preventing the accumulation of damaged or misfolded proteins, and enabling the timely degradation of proteins that are no longer required. The process involves a series of steps: 1. **Target Protein Recognition and Selection:** Specific signals on the target protein, such as ubiquitination, phosphorylation, or specific amino acid sequences, mark it for degradation. These signals are recognized by dedicated protein complexes or proteolytic enzymes. 2. **Proteolytic Machinery Activation:** The recognition of target proteins triggers the activation of the proteolytic machinery, often involving the assembly of specific protein complexes. 3. **Protein Degradation:** Once activated, the proteolytic machinery breaks down the target protein into smaller peptides or amino acids, which can then be recycled or further processed. 4. **Regulation of Proteolysis:** Positive regulation of proteolysis ensures that the breakdown of proteins occurs at the appropriate time and in the appropriate location within the cell. This regulation involves a complex interplay of various factors, including: - **Ubiquitin-Proteasome System (UPS):** The UPS is a major pathway for protein degradation. Ubiquitination, the covalent attachment of ubiquitin to a target protein, signals for its degradation by the proteasome, a multi-protein complex that unfolds and breaks down proteins. - **Lysosomal Degradation:** Lysosomes are cellular organelles containing hydrolytic enzymes that degrade various macromolecules, including proteins. Proteins destined for lysosomal degradation are often targeted by specific receptors or sorting signals. - **Caspase-mediated Proteolysis:** Caspases are cysteine proteases involved in apoptosis (programmed cell death). During apoptosis, caspases are activated and cleave specific target proteins, leading to the dismantling of the cell. - **Other Proteolytic Pathways:** In addition to the UPS and lysosomal degradation, other proteolytic pathways, such as those involving calpains and cathepsins, also contribute to protein degradation. 5. **Cellular Consequences:** Positive regulation of proteolysis plays a crucial role in various cellular processes, including: - **Protein Quality Control:** Removal of misfolded or damaged proteins prevents the accumulation of toxic proteins and maintains cellular integrity. - **Cell Cycle Regulation:** Proteolysis controls the degradation of key regulatory proteins, ensuring proper progression through the cell cycle. - **Signal Transduction:** Degradation of signaling molecules fine-tunes cellular responses to external stimuli. - **Development and Differentiation:** Proteolysis is essential for the breakdown of specific proteins during developmental processes and tissue differentiation. - **Response to Stress:** During stress conditions, proteolysis is often upregulated to remove damaged proteins and maintain cellular function. In conclusion, positive regulation of proteolysis is an intricate and essential biological process that governs the breakdown of proteins within cells. This regulation ensures the timely removal of damaged or unwanted proteins, allowing cells to maintain their integrity, adapt to changing environments, and execute critical cellular functions.'
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Proteins (1)

ProteinDefinitionTaxonomy
Dipeptidyl peptidase 1A dipeptidyl peptidase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P53634]Homo sapiens (human)

Compounds (11)

CompoundDefinitionClassesRoles
Pyrrolidine-1-carbonitrilepyrrolidines
e 64E 64: cysteine protease inhibitor of microbial origin, which inhibits cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.-)dicarboxylic acid monoamide;
epoxy monocarboxylic acid;
guanidines;
L-leucine derivative;
zwitterion
antimalarial;
antiparasitic agent;
protease inhibitor
canertinibmonochlorobenzenes;
morpholines;
organofluorine compound;
quinazolines
antineoplastic agent;
tyrosine kinase inhibitor
odanacatibodanacatib: a selective inhibitor of cathepsin K for the treatment of post-menopausal osteoporosis; structure in first source
bibw 2992aromatic ether;
enamide;
furans;
monochlorobenzenes;
organofluorine compound;
quinazolines;
secondary carboxamide;
tertiary amino compound
antineoplastic agent;
tyrosine kinase inhibitor
6-(3,5-difluoroanilino)-9-ethyl-2-purinecarbonitrile6-aminopurines
6-(3,5-difluoroanilino)-9-(2,2-difluoroethyl)-2-purinecarbonitrile6-aminopurines
9-(3,5-difluorophenyl)-6-(ethylamino)-2-purinecarbonitrileimidazoles
grassystatin agrassystatin A: isolated from a cyanobacterium, identified as Lyngbya cf.; structure in first source
thiopental sodiumorganochlorine compound;
piperazines;
pyrimidines
antineoplastic agent;
tyrosine kinase inhibitor
osimertinibosimertinib : A member of the class of aminopyrimidines that is 4-(1-methylindol-3-yl)pyrimidin-2-amine in which one of the amino hydrogens is replaced by a 2-methoxy-4-[2-(dimethylamino)ethyl](methyl)amino-5-acrylamidophenyl group. Used (as the mesylate salt) for treatment of EGFR T790M mutation positive non-small cell lung cancer.

osimertinib: an EGFR tyrosine kinase inhibitor
acrylamides;
aminopyrimidine;
biaryl;
indoles;
monomethoxybenzene;
secondary amino compound;
secondary carboxamide;
substituted aniline;
tertiary amino compound
antineoplastic agent;
epidermal growth factor receptor antagonist