MELK

Description

The MELK (maternal embryonic leucine zipper kinase) is a protein-coding gene located on chromosome 9.

Maternal embryonic leucine zipper kinase (MELK) is an enzyme encoded by the MELK gene in humans. It is a serine/threonine kinase belonging to the AMPK/Snf1 protein kinase family. MELK was initially identified as a maternal mRNA in mouse embryos. Its expression is elevated in numerous cancers, making it a target for pharmacological inhibition. Previously, MELK was thought to be essential for cancer cell proliferation. However, recent research using CRISPR has demonstrated that MELK is dispensable for cancer cell growth, questioning the rationale for targeting this protein in patients. The findings depend on the experimental design, highlighting the need for further research.

MELK, a serine/threonine kinase, is involved in various cellular processes including cell cycle regulation, stem cell renewal, apoptosis and splicing regulation. Its broad substrate specificity allows it to phosphorylate BCL2L14, CDC25B, MAP3K5/ASK1, and ZNF622. Notably, it activates apoptosis by phosphorylating and activating MAP3K5/ASK1. As a regulator of the cell cycle, it mediates phosphorylation of CDC25B, promoting its localization to the centrosome and spindle poles during mitosis. MELK plays a crucial role in cell proliferation and carcinogenesis. It is essential for the proliferation of embryonic and postnatal neural progenitors. Phosphorylation and inhibition of BCL2L14 by MELK may impact mammary carcinogenesis by inhibiting the pro-apoptotic function of BCL2L14. Furthermore, MELK participates in the inhibition of spliceosome assembly during mitosis by phosphorylating ZNF622, leading to its redirection to the nucleus. Additionally, MELK might play a role in primitive hematopoiesis.

MELK is also known as HPK38.

Associated Diseases

WES Whole Exome Sequencing