To cope with attacks by diverse pathogenic microbes, plants have evolved cytoplasmic immune receptors and cell surface immune receptors to detect various danger signals during the infection. Cytoplasmic immune receptors, typically NOD-like receptors (NLRs), perceive pathogen effector proteins inside the plant cell. The cell surface immune receptors, also called pattern-recognition receptors (PRRs), are consisted of a variety of receptor-like kinases (RLKs) and receptor-like proteins (RLPs) that sense conserved microbial signatures termed Pathogen/Microbe-Associated Molecular Patterns (PAMPs), such as proteins and cell wall fragments derived from microbes. PRRs also perceive damage-associated molecular patterns (DAMPs), which are plant-derived molecules such as plant cell wall fragments and peptides produced specifically during pathogen infection. One important player linking various immune pathways is BIK1, a receptor-like cytoplasmic kinase. We have shown previously that BIK1 directly associates with multiple PAMP receptors to mediate immune signaling and that BIK1 is attacked by at least two different bacterial type III effectors. BIK1 has also been reported to mediate ethylene (ET) signaling, but the underlying mechanism remains unknown. Our recent data showed that BIK1mediates ET signaling by associating with PEPR1 and PEPR2, two closely related DAMP receptors perceiving a family of endogenous peptides Pep1- Pep6. Our data indicate that ET and the DAMP signaling pathway act in concert to amplify plant defenses. In addition to PRRs, we found that BIK1 also interacts with proteins implicated in the regulation of oxidative burst, visicle trafficking, and stomatal opening. Together the results indicate that BIK1 fulfills multiple roles in plant immune signaling.