Pannexin1 (Pnx1) is a channel-forming transmembrane protein involved in nucleotide permeation and adenosine triphosphate release, playing a crucial role in intercellular communication. The level of Pnx1 degradation may have an impact on intercellular communication. However these mechanisms remain largely unexplored. Accordingly, the main goal of this pilot study was to evaluate the potential role of a lysosomal pathway called chaperone-mediated autophagy (CMA) on the degradation of Pnx1. In this study we demonstrate that CMA activation leads to an increase in Pnx1 degradation with a concomitant increase in the interaction between Pnx1 and CMA components. We also demonstrate that a

mutation in a putative KFERQ motif, which is necessary for degradation by CMA, hampers Pnx1 degradation. Altogether, these results suggest that degradation of Pnx1 is to some extent dependent on CMA, however further experiments are necessary to strength this conclusion.