The ubiquitin system targets translocated EspH to proteasomal degradation.

ABSTRACT: EspH is an effector protein secreted by the type III secretion system of various pathogenic Escherichia coli strains, including enteropathogenic E. coli (EPEC). The ability of EspH to inhibit host RhoGTPases, disrupt the actin cytoskeleton, and induce host cell cytotoxicity has been well-documented. Mass spectrometry analysis of EspH translocated into EPEC-infected cells revealed that a lysine at position 106 (K106) is modified with ubiquitin. Immunoblotting using the FK2 anti-ubiquitin antibodies has confirmed these results, suggesting that EspH undergoes polyubiquitylation. Prediction algorithms have identified a single ubiquitylation site at K106 and a phosphodegron in EspH. Moreover, we show that wild-type (EspH_wt), but not the EspH_K106R

SUBMITTER: Nandi I 

PROVIDER: S-EPMC12688225 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature