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LIR motifs and the membrane-targeting domain are complementary in the function of RavZ
Sang-Won Park1,#, Yong-Woo Jun1,#, Purem Jeon2, You-Kyung Lee2, Ju-Hui Park1, Seung-Hwan Lee1, Jin-A Lee2,#, Deok-Jin Jang1,*,#
1Department of Ecological Science, Kyungpook National University,
22Department of Biological Sciences and Biotechnology, Hannam University
The bacterial effector protein RavZ is secreted by the intracellular pathogen, Legionella pneumophila, and inhibits host autophagy through an irreversible deconjugation of mammalian ATG8 (mATG8) proteins from autophagosome membranes. However, the roles of the LC3 interacting region (LIR) motifs in RavZ function remain unclear. In this study, we show that a membrane-targeting (MT) domain or the LIR motifs of RavZ play major or minor roles in RavZ function. A RavZ mutant that does not bind to mATG8 delipidated all forms of mATG8-phosphatidylethanolamine (PE) as efficiently as wild-type RavZ. However, a RavZ mutant with a deletion of the MT domain selectively delipidated mATG8-PE less efficiently than wild-type RavZ. Taken together, our results suggest that the effects of LIR motifs and the MT domain on RavZ activity are complementary and work through independent pathways.
Abstract, Accepted Manuscript(in press) [Submitted on August 19, 2019, Accepted on October 17, 2019]
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