okay well there's this set of genes called the destruction complex (Dvl, Axin, CKI, GSK3, Beta Catenin, Beta TrCP)
There's a receptor called "Frizzled", and if that receptor isn't agonised and is left inactive it leads to the ubiquitination, phosphorlation and eventual proteosomal degredation of Beta Catenin
Beta TrCP is actually e3 ubiquitin ligase and Beta TrCP causes the ubiquitination of Beta Catenin which leads to proteosomal degradation, keeping Beta Catenin levels low.
When the Frizzled receptor is agonised, it's agonised by Wnt which is carried in an exosome from somewhere in the body.
When Frizzled is activated it leads to the phosphorlation of LRP which induces the translocation of the "destruction complex" to the region of the cell membrane near the frizzled receptor. Dvl binds to Frizzled and leads to the inhibition of the destruction complex and now Beta TrCP is isolated from Beta Catenin and the rest of the destruction complex, so Beta Catenin can't be ubiquitinated by Beta TrCP. Since Beta Catenin can't get ubiquitinated, it can't get degraded in the proteosome which leads to an increase in Beta Catenin levels in the cell.
the next part is too hard to explain
There's this thing called TCF (Transcription Factor) which regulates Wnt target genes.
When Beta Catenin levels rise inside the cytosol, a gene called Groucho binds to TCF and inhibits its ability to bind to the dna.
The Beta Catenin translocates into the nucleus in the activated state (With Frizzled activated), and binds to TCF, unbinding Groucho from TCF in the process.
The fact that Beta Catenin is now bound to TCF. TCF now regulates Wnt target genes solely for growth and proliferation
ie: hairs