MELK Protein, Human (Active)

MELK, a serine/threonine-protein kinase, orchestrates a diverse array of cellular processes encompassing cell cycle regulation, stem cell self-renewal, apoptosis, and splicing control. Exhibiting a broad substrate specificity, MELK phosphorylates key proteins such as BCL2L14, CDC25B, MAP3K5/ASK1, and ZNF622. As an activator of apoptosis, MELK phosphorylates and activates MAP3K5/ASK1. In the realm of cell cycle regulation, MELK assumes a pivotal role by mediating the phosphorylation of CDC25B, facilitating its localization to the centrosome and spindle poles during mitosis. This kinase is indispensable for the proliferation of both embryonic and postnatal multipotent neural progenitors. MELK's impact on carcinogenesis extends to the phosphorylation and inhibition of BCL2L14, potentially influencing mammary carcinogenesis by impeding the pro-apoptotic function of BCL2L14. Moreover, MELK contributes to the inhibition of spliceosome assembly during mitosis through the phosphorylation of ZNF622, redirecting its localization to the nucleus. Notably, MELK's involvement in primitive hematopoiesis underscores its multifaceted regulatory role in fundamental cellular processes.