Target type: biologicalprocess
Any process leading to the attainment of the full functional capacity of a ligand for an epidermal growth factor receptor. The ligand is functional when it can bind to and activate an epidermal growth factor receptor. [GOC:signaling, PMID:11672524, PMID:11672525]
Epidermal growth factor receptor (EGFR) ligand maturation is a complex process that involves the synthesis, processing, and activation of a family of polypeptide growth factors that bind to and activate EGFR. These ligands include epidermal growth factor (EGF), transforming growth factor alpha (TGFα), amphiregulin, heparin-binding EGF-like growth factor (HB-EGF), and epiregulin.
The process begins with the synthesis of the precursor proteins for each ligand as transmembrane proteins. These precursors are typically synthesized with a signal peptide, a transmembrane domain, and an extracellular domain that contains the mature ligand sequence.
**Proteolytic Processing:** The maturation of EGFR ligands involves proteolytic cleavage of the precursor protein, releasing the mature ligand from the cell surface. This cleavage can be mediated by a variety of proteases, including metalloproteases, furin, and ADAM (a disintegrin and metalloproteinase) family members. The specific protease involved in the cleavage of each ligand can vary depending on the cell type and the specific context.
**Activation:** Once cleaved from the cell surface, the mature EGFR ligands can bind to and activate EGFR. The binding of the ligand to EGFR triggers a cascade of intracellular signaling events that ultimately lead to cell growth, proliferation, and survival.
**Regulation of Ligand Maturation:** The maturation of EGFR ligands is tightly regulated. This regulation is important for ensuring that the ligands are only produced and activated when needed, and that their activity is appropriately controlled.
**Factors that can influence ligand maturation include:**
* **Cell type:** Different cell types express different levels of EGFR ligands and proteases, which can affect the rate of ligand maturation.
* **Growth factors and cytokines:** Certain growth factors and cytokines can induce the expression of EGFR ligands or their processing enzymes.
* **Cellular stress:** Stress conditions, such as hypoxia or DNA damage, can also influence the maturation of EGFR ligands.
* **Post-translational modifications:** The maturation of EGFR ligands can be further regulated by post-translational modifications, such as glycosylation and phosphorylation.
**In summary, the maturation of EGFR ligands is a complex process involving multiple steps, including synthesis, processing, and activation. The regulation of this process is critical for controlling EGFR signaling and maintaining cellular homeostasis.**'
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Protein | Definition | Taxonomy |
---|---|---|
Disintegrin and metalloproteinase domain-containing protein 10 | A disintegrin and metalloproteinase domain-containing protein 10 that is encoded in the genome of human. [PRO:WCB, UniProtKB:O14672] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
ilomastat | CS 610: matrix metalloproteinase inhibitor; structure in first source ilomastat : An N-acyl-amino acid obtained by formal condensation of the carboxy group of (2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoic acid with the amino group of N-methyl-L-tryptophanamide. A cell permeable broad-spectrum matrix metalloproteinase (MMP) inhibitor | hydroxamic acid; L-tryptophan derivative; N-acyl-amino acid | anti-inflammatory agent; antibacterial agent; antineoplastic agent; EC 3.4.24.24 (gelatinase A) inhibitor; neuroprotective agent |
bms-566394 | BMS-566394: structure in first source | ||
incb3619 | INCB3619: ADAM inhibitor; structure in first source | ||
grassystatin a | grassystatin A: isolated from a cyanobacterium, identified as Lyngbya cf.; structure in first source |