C-type lectins are a family of pattern recognition receptors that recognize microbial components and subsequently activate the signaling cascade to induce the production of proinflammatory cytokines. In the current study, the homologs of ERK (named as CgERK) and GSK3β (named as CgGSK3β) and a novel C-type lectin with a transmembrane domain (named as CgCLec-TM1) were identified from oyster Crassostrea gigas CgCLec-TM1 was able to bind Escherichia coli and Vibrio splendidus through its carbohydrate recognition domain and then activated CgERK by inducing its phosphorylation. The activated CgERK interacted with CgGSK3β to phosphorylate it at Ser9, which eventually induced the expressions of CgIL-17-1 and CgIL-17-5. The interaction between CgERK and CgGSK3β, as well as the phosphorylation of CgGSK3β, could be inhibited by ERK inhibitor (PD98059) to reduce the expressions of CgIL-17-1 and CgIL-17-5. CgGSK3β in oyster was proposed as a new substrate of CgERK. The results defined a CLec-TM1-ERK-GSK3β signaling pathway in oyster, which was activated by V. splendidus and then induced CgIL-17 productions.
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