NEK7 is a core component required for the assembly and activation of the NLRP3 inflammasome, yet the mechanisms governing its protein stability and turnover remain largely unclear. Here, we explored the possibility that chaperone-mediated autophagy (CMA) selectively regulates NEK7 degradation. CMA is a selective autophagic pathway in which Hsc70 recognizes substrate proteins bearing a KFERQ-like motif and delivers them into the lysosome through the lysosomal membrane receptor LAMP2A. As NEK7 contains a putative KFERQ-like motif, we hypothesized that it may serve as a CMA substrate, and that reduced LAMP2A expression would impair its lysosomal translocation, resulting in cytosolic NEK7 accumulation. Such accumulation is expected to drive excessive NLRP3 inflammasome assembly and activation, thereby aggravating hepatic inflammation. Together, our findings identify CMA-mediated degradation of NEK7 as a novel regulatory mechanism underlying hepatic inflammatory responses and highlight its potential as a therapeutic target for inflammatory liver disease.