How microbes utilize host ubiquitination

Abstract

SummaryActivity, abundance and localization of eukaryotic proteins can be regulated through covalent attachment of ubiquitin and ubiquitin-like moieties.

A Moving View: Subcellular Trafficking Processes in Pattern Recognition Receptor–Triggered Plant Immunity

“…Ubiquitination of host targets is a prominent process utilized by pathogens to promote infection success (129). The bacterial effector AvrPtoB has similarities to eukaryotic E3 ligases and when secreted into host cells is able to interact with and ubiquitinate plant targets, including AtFLS2 (52, 114).…”

Ubiquitination of BST-2 Protein by HIV-1 Vpu Protein Does Not Require Lysine, Serine, or Threonine Residues within the BST-2 Cytoplasmic Domain

“…Although ubiquitination was initially characterized as a simple mechanism to target cellular proteins for degradation within the proteasome, it is now recognized as a far more complex mechanism that functions in a wide spectrum of processes. Perhaps not surprisingly, microbial (1) and viral (2,3) pathogens have learned to interfere with the host Ub machinery. The HIV-1 accessory proteins Vpu, Vif, and Vpr each interact with cullin E3 Ub ligase complexes, thereby allowing the virus to fine-tune and exploit the host Ub system for its own benefit (4).…”

Characterization and expression analysis of BCA2 gene in large yellow croaker, Larimichthys crocea

“…There are growing evidences showed that ubiquitination mediated by E3 ubiquitin ligase can not only regulate the development of immune system, but also initiate effective immune responses [4e6]. Furthermore, prokaryote may utilize the host ubiquitin system to invade, although prokaryote itself lacks classical ubiquitin system [7].…”