Exploiting the ubiquitin and phosphoinositide pathways by the Legionella pneumophila effector, SidC.
Exploiting the ubiquitin and phosphoinositide pathways by the Legionella pneumophila effector, SidC.
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DOI:
10.1007/s00294-015-0521-y
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发表时间:
2016-02
期刊:
影响因子:
2.5
通讯作者:
Mao Y
中科院分区:
文献类型:
--
作者:
Wasilko DJ;Mao Y
Intracellular bacterial pathogens use secreted effector proteins to alter host cellular processes, with the goal of subverting host defenses and allowing the infection to progress. One such pathogen, Legionella pneumophia, secretes ~300 such proteins into its host to alter a number of pathways including intracellular trafficking, phosphoinositide metabolism, and cell signaling. The Legionella effector SidC was previously found to bind to PI(4)P and was responsible for the enrichment of ER proteins as well as ubiquitinated species to the Legionella-containing vacuoles. Through our recent work, we have discovered that SidC contains a unique N-terminal E3 ubiquitin ligase domain and a C-terminal novel PI(4)P-binding domain. Our results demonstrate that SidC serves to link two distinct cellular pathways, ubiquitin and phosphoinositide. However, how the ubiquitin ligase activity regulates host membrane trafficking events remain to be investigated.