text: Current research regarding Botrytis-induced kinase1 aims to determine how BIK1 interacts with MAPK pathway proteins as well as with the OXI1 kinase. Also, studies are being conducted to determine the relationship between BIK1 and the phosphorylizing homolog kinases PEPR1 and PEPR2. Though it is believed that PEPR1 and PEPR2 act as enzymes toward BIK1 and phosphorylate the kinase, research is still being done to examine the effects of the interaction on a broader scale. Previously published research suggests that PEPR1 and PEPR2 work with the ET signal pathway and Botrytis-induced kinase1 in order to amplify the defense mechanism in immune response. Additionally, future research may explore the mechanism that allows BIK1 and BAK1 to cooperate with the FLS2 receptor to initiate defense response. While it is known that the three work together and each is required for the process to occur efficiently, but the exact relationship between the three remains unknown and the specific binding residues for each component have yet to be determined in vivo.