Essay on Components Of The Destruction Complex Function

Essay on Components Of The Destruction Complex Function

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Similar to other complexes observed, the components of the destruction complex function in cooperation. Binding interaction between APC and Axin helps to assemble the complex and facilitates phosphorylation (Fagotto & Henderson, 2002). Without the combined interactive force, β-catenin will not be effectively positioned since the phosphorylated site may not be oriented in the right direction. Free β-catenin is not normally recognized by GSK3 protein. Thus, only in the presence of APC and Axin is the kinase able to phosphorylate the amino acid (Orsulic & Peifer, 1996). Therefore, APC serves a dual role as part of the destruction complex and as an inducer for β-catenin phosphorylation (Valenta et al., 2012). Phosphorylation of β-catenin does not degrade it without the presence of the ubiquitin ligase complex (Vlad et al., 2008).
Different cellular signals prevent β-catenin degradation by inhibiting the β-catenin destruction complex (Valenta et al., 2012). The main regulator of this destruction complex is the activation and deactivation of Wnt signaling (Valenta et al., 2012). The disassembly of the destruction complex is initiated when a Wnt ligand binds to the transmembrane receptor belonging to the Frizzled family, and activates the LRP5/6 co-receptors (Alberts, 2002). This co-receptors function by either competing with GSK3β for binding site, or by localizing the kinase into specific vesicular bodies to prevent interaction, and thus phosphorylating with the free β-catenin (Huber et al., 1997). This receptor interaction promotes a cytoplasmic protein, disheveled, to directly bind to the receptor complex, multimerize, and subsequently induce conformational changes in the protein complex. Disheveled (Dlv), by allowing the formation o...

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... not even possess a binding domain for DNA. However different domains of β-catenin are recognized by different DNA binding proteins, in which, the interaction induces conformational shift on β-catenin that brings the protein in close proximity to the promoters of the target genes, thus playing its signaling role (Archbold et al., 2012). Simple interaction of β-catenin with TCF does not initiate transcription; it rather recruits different transcription factors that alter the chromatin configuration and functional state of the basal transcriptional machinery, to initiate transcription (Benchabane et al., 2011). Therefore, β-catenin simply provides a base for the interaction of different molecules to transcriptional co-activators, and only with the formed association, is it able to play its central signaling role in the nucleus (Huber et al., 1997 & Xing et al., 2008).

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