Target type: molecularfunction
Binding to catenin complex alpha subunit. [GOC:bf]
Alpha-catenin binding is a crucial molecular interaction that plays a pivotal role in cell-cell adhesion and the organization of the cytoskeleton. Alpha-catenin, a key component of adherens junctions, acts as a linker protein bridging the cadherin transmembrane adhesion receptors to the actin cytoskeleton. This binding event is critical for maintaining cell-cell adhesion and ensuring proper tissue integrity.
The molecular function of alpha-catenin binding involves a complex interplay of protein domains and interactions:
- **Cadherin Binding:** Alpha-catenin directly interacts with the cytoplasmic tail of cadherin proteins, specifically the juxtamembrane domain. This interaction is essential for anchoring the cadherin complex to the actin cytoskeleton.
- **Actin Binding:** Alpha-catenin also possesses an actin-binding domain, allowing it to interact with actin filaments. This interaction is crucial for linking the cadherin complex to the cytoskeleton, contributing to the formation of a stable adhesion structure.
- **Regulation of Actin Dynamics:** Alpha-catenin binding influences the organization and dynamics of the actin cytoskeleton. It can promote the assembly and stabilization of actin filaments, contributing to the formation of cell-cell junctions. Conversely, it can also regulate actin depolymerization, allowing for dynamic remodeling of cell-cell contacts.
- **Signal Transduction:** Alpha-catenin binding can participate in signal transduction pathways, mediating communication between the extracellular environment and the cell's interior. This can involve the regulation of gene expression, cell growth, and differentiation.
In summary, alpha-catenin binding is a multifaceted molecular event that underpins cell-cell adhesion and cytoskeletal organization. It involves a complex interplay of protein domains, interactions with cadherins and actin, and regulation of actin dynamics, contributing to the overall integrity and functionality of tissues.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Catenin beta-1 | A catenin beta-1 that is encoded in the genome of human. [PRO:WCB, UniProtKB:P35222] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| salvin | salvin: a biocyclic diterpenoid; from sage and rosemary (Lamiaceae) | abietane diterpenoid; carbotricyclic compound; catechols; monocarboxylic acid | angiogenesis modulating agent; anti-inflammatory agent; antineoplastic agent; antioxidant; apoptosis inducer; food preservative; HIV protease inhibitor; plant metabolite |
| toxoflavin | toxoflavin : A pyrimidotriazine that is 1,6-dimethyl-1,5,6,7-tetrahydropyrimido[5,4-e][1,2,4]triazine with oxo groups at positions 5 and 7. toxoflavin: azapteridine antibiotic; structure | carbonyl compound; pyrimidotriazine | antibacterial agent; antineoplastic agent; apoptosis inducer; bacterial metabolite; toxin; virulence factor; Wnt signalling inhibitor |
| cercosporin | cercosporin : An organic heterohexacyclic compound that is perylo[1,12-def][1,3]dioxepine-6,11-dione substituted by hydroxy groups at positions 5 and 12, by methoxy groups at positions 7 and 10, and by 2-hydroxypropyl groups at positions 8 and 9 (the R,R-stereoisomer). It is a phytotoxin which was first isolated from the pathogenic soybean fungus, Cercospora kikuchii and later found in multiple members of the genus Cercospora. cercosporin: phyytotoxin from Cercospora beticola Sacc; posses photodynamic action on mice, bacteria & plants | ||
| LSM-42773 | aromatic ketone | ||
| etodolac, (-)-isomer | (R)-etodolac : The R-enantiomer of etodolac. It is inactive, in contrast to the enantiomer, (S)-etodolac, which is a preferential inhibitor of cyclo-oxygenase 2 and a non-steroidal anti-inflammatory. The racemate is commonly used for the treatment of rheumatoid arthritis and osteoarthritis, and for the alleviation of postoperative pain. | etodolac | |
| ucn 1028 c | calphostin C: structure given in first source; isolated from Cladosporium cladosporioides |