@article{FischerHarrisonRamirezetal.2017,
  author    = {Fischer, Annette and Harrison, Kelly S and Ramirez, Yesid and Auer, Daniela and Chowdhury, Suvagata Roy and Prusty, Bhupesh K and Sauer, Florian and Dimond, Zoe and Kisker, Caroline and Hefty, P Scott and Rudel, Thomas},
  title     = {Chlamydia trachomatis-containing vacuole serves as deubiquitination platform to stabilize Mcl-1 and to interfere with host defense},
  series = {eLife},
  volume    = {6},
  journal   = {eLife},
  number    = {e21465},
  doi       = {10.7554/eLife.21465},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-171073},
  year      = {2017},
  abstract  = {Obligate intracellular Chlamydia trachomatis replicate in a membrane-bound vacuole called inclusion, which serves as a signaling interface with the host cell. Here, we show that the chlamydial deubiquitinating enzyme (Cdu) 1 localizes in the inclusion membrane and faces the cytosol with the active deubiquitinating enzyme domain. The structure of this domain revealed high similarity to mammalian deubiquitinases with a unique α-helix close to the substrate-binding pocket. We identified the apoptosis regulator Mcl-1 as a target that interacts with Cdu1 and is stabilized by deubiquitination at the chlamydial inclusion. A chlamydial transposon insertion mutant in the Cdu1-encoding gene exhibited increased Mcl-1 and inclusion ubiquitination and reduced Mcl-1 stabilization. Additionally, inactivation of Cdu1 led to increased sensitivity of C. trachomatis for IFNγ and impaired infection in mice. Thus, the chlamydial inclusion serves as an enriched site for a deubiquitinating activity exerting a function in selective stabilization of host proteins and protection from host defense.},
  language  = {en}
}