Protein kinases are enzymes that play a critical role in regulating various cellular processes by adding phosphate groups to specific amino acids in proteins. Dual-specificity tyrosine phosphorylation refers to a specific type of kinase activity where the enzyme can phosphorylate a protein on both tyrosine and serine/threonine residues. DYRK1A (dual-specificity tyrosine phosphorylation-regulated kinase 1A) is a member of the DYRK family of proteins, characterized by their involvement in cellular signaling pathways, regulation of cell cycle, and processes related to neurodevelopment. In conclusion, DYRK1A is a multifaceted kinase that plays critical roles in both cancer metastasis and neuronal function. Its regulatory effects on cell migration, apoptosis, and synaptic plasticity present opportunities for targeted therapies in HCC and neurological disorders. Further research into the molecular mechanisms underlying DYRK1A's actions in these contexts will be essential for the development of specific interventions aimed at mitigating its pathological effects in cancer and neurodegeneration.