P21-activated kinase 1 (PAK1) is a serine/threonine protein kinase that plays a crucial role in cardiomyocyte survival in response to various stresses. However, the underlying cardioprotective mechanisms of PAK1 remain unclear. Autophagy is a lysosome degradation pathway essential for cellular homeostasis. In the present study, we showed the ability of PAK1 to regulate autophagy in cardiomyocytes and identified p62 as a potential downstream mediator. PAK1 is silenced in H9c2 cardiac myoblasts by siRNA or overexpressed by adenovirus. Autophagy flux was determined by LC3-II protein levels and a fluorescent autophagy reporter with and without the lysosomal protease inhibitors Pepstatin A (pepA) and Aloxistatin (E64d). Downregulation of PAK1 reduced LC3-II levels in whole cell lysates, which was not affected by pepA and E64d, suggesting that PAK1 knockdown reduced autophagy flux. Conversely, PAK1 overexpression increased LC3-II levels, which were further elevated by pepA and E64d, suggesting that PAK1 is sufficient to promote autophagy. Interestingly, the protein expression of p62, a ubiquitin-binding autophagy adaptor, was increased by PAK1 overexpression and reduced by PAK1 knockdown. Importantly, overexpression of p62 rescued the defective autophagy flux in the absence of PAK1, suggesting that p62 may mediate PAK1-dependent autophagy. RT-qPCR assay showed that the p62 mRNA levels were unchanged by either overexpression or knockdown of PAK1 in vitro and in vivo. The cells were treated with the protein synthesis inhibitor cycloheximide (CHX) and p62 protein levels were measured over time in both PAK1-silencing and overexpressing conditions. The results showed that p62 degradation was mitigated by PAK1 overexpression and accelerated by PAK1 knockdown. Together, these results suggest that PAK1 is sufficient and necessary to maintain autophagy in cardiomyocytes, which is likely mediated by its ability to affect p62 protein stability.