The Shigella kinase effector OspG hijacks host ubiquitin signaling to escape septin-cage entrapment

ABSTRACT: We show by unbiased phosphoproteomics that a major target of OspG is CAND1, a regulatory protein controlling the assembly of cullin-RING ubiquitin ligases (CRLs). CAND1 phosphorylation weakens its interaction with cullins, which is expected to impact a large panel of CRL E3s. Indeed, global ubiquitome profiling reveals marked changes in the ubiquitination landscape when OspG is introduced. Notably, OspG promotes ubiquitination of a class of cytoskeletal proteins called septins, thereby inhibiting formation of cage-like structures encircling cytosolic bacteria.

ORGANISM(S): Homo Sapiens

SUBMITTER: Xiaoyun Liu  

PROVIDER: PXD048447 | iProX | Wed Jan 10 00:00:00 GMT 2024

REPOSITORIES: iProX