MINK1 (misshapen like kinase 1) is a serine/threonine protein kinase that regulates diverse cellular processes through phosphorylation of multiple substrates. MINK1 functions as a key regulator of cell migration and cytoskeletal organization by phosphorylating proteins involved in focal adhesion dynamics, including LL5β (PHLDB2), which promotes microtubule anchoring at the cell cortex through CLASP proteins 1. The kinase also phosphorylates PRICKLE1, a Wnt/PCP pathway component, contributing to cancer cell motility and invasiveness in triple-negative breast cancer 1. MINK1 participates in mechanotransduction pathways, where it can be stimulated by RAP2 under low ECM stiffness conditions to activate LATS1/2 and inhibit YAP/TAZ signaling 2. In neuronal contexts, MINK1 interacts with CNKSR scaffold proteins and can be displaced by SAMD12, affecting synapse development 3. MINK1 also regulates immune responses by activating JNK/c-Jun signaling, which upregulates ULBP2 expression and enhances NK cell-mediated cytotoxicity against breast cancer cells 4. Additionally, MINK1 phosphorylates the glucocorticoid receptor at Thr524, inducing 14-3-3 protein interactions that modulate inflammatory responses 5. Clinically, MINK1 deficiency is associated with increased pyroptosis in intervertebral disc degeneration 6 and may be involved in multiple sclerosis pathogenesis through EBV interactions 7.