These aforementioned results led us to a potential mechanism that upon the stimuli of hyperglycemia, Rac1/PAK1 signaling was activated in podocyte; β-catenin was then modified, either dephosphorylated at N-terminus or phosphorylated at C-terminus, leading to elevated level of active β-catenin; the downstream p38 further ensured β-catenin transcriptional activities via activating MEF2c; and active β-catenin contributed to the dysregulation of a series of target genes, and imbalanced expression of SD proteins such as p-cadherin, as reported here. This evidence concerns the gene RAC1 and Hyperglycemia.