MYLK, also known as myosin light chain kinase, catalyzes the phosphorylation of myosin light chains (MLC). This function is crucial for regulating the contractility of smooth muscle cells and is involved in various cellular processes like cell migration. It participates in signaling pathways such as the transforming growth factor-β signaling pathway [1,2].

In aging-related aortic aneurysm and dissection (AAD) in mice, miR-1204 directly targets MYLK. This leads to the acquisition of a senescence-associated secretory phenotype (SASP) by vascular smooth muscle cells (VSMCs) and loss of their contractile phenotype, aggravating AAD. MYLK overexpression can reverse miR-1204-induced VSMC senescence and related phenotypic changes [1]. In heritable thoracic aortic disease, null variants in MYLK can result in aortic events. Missense pathogenic variant carriers have earlier-onset aortic events than null PV carriers [2].

In conclusion, MYLK is essential for maintaining the contractile function of smooth muscle cells. Mouse models with MYLK-related genetic manipulations have revealed its significance in age-related aortic diseases. Understanding MYLK's role through these models provides insights into the mechanisms of aortic diseases and may offer potential therapeutic targets for treatment.