Legionella effector LpPIP recruits protein phosphatase 1 to the mitochondria to induce dephosphorylation of outer membrane proteins.

ABSTRACT: Legionella pneumophila utilizes a type IVB secretion system (T4SS) to translocate over 300 effector proteins into host cells, hijacking cellular processes, including those within the mitochondrion. Currently, no Legionella effectors have been identified at the mitochondrial outer membrane, a critical interface between the organelle and the rest of the cell. We screened the Legionella effector repertoire for features of mitochondrial tail-anchored (TA) proteins and identified four putative TA effectors. Among them, LpPIP (Lpg1625) localizes to the mitochondrial outer membrane and interacts with all three isoforms of protein phosphatase 1 (PP1) via an RVxF motif, functioning as a PP1-interacting protein (PIP). Importantly, PP1 remains catalytically active upon interaction with LpPIP to depho

SUBMITTER: Yek KQ 

PROVIDER: S-EPMC12313075 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature