Modulation of host functions by bacterial serine/threonine protein kinase (STPK) effector proteins

Protein phosphorylation, one of the most ubiquitous and evolutionarily conserved post-translational modifications, serves as a master regulator of cellular signaling networks. In host-pathogen interactions, bacterial subversion of phosphorylation-dependent signaling pathways has emerged as a pivotal mechanism of microbial pathogenesis. Notably, recent advances in eukaryotic-like serine/threonine protein kinase (STPK) effector proteins have profoundly advanced our understanding of molecular pathogenesis through their ability to hijack host cell signaling. In this review, we will summarize the sophisticated strategies by which bacterial STPK effectors manipulate host phosphorylation networks to enhance virulence and promote infection.