The kinases Mst1 and Mst2 positively regulate phagocyte ROS induction and bactericidal activity

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The kinases Mst1 and Mst2 positively regulate phagocyte ROS induction and bactericidal activity

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Title: The kinases Mst1 and Mst2 positively regulate phagocyte ROS induction and bactericidal activity
Author: Geng, Jing; Sun, Xiufeng; Wang, Ping; Zhang, Shihao; Wang, Xiaozhen; Wu, Hongtan; Hong, Lixin; Xie, Changchuan; Li, Xun; Zhao, Hao; Liu, Qingxu; Jiang, Mingting; Chen, Qinghua; Zhang, Jinjia; Li, Yang; Song, Siyang; Wang, Hong-Rui; Zhou, Rongbin; Johnson, Randy L.; Chien, Kun-Yi; Lin, Sheng-Cai; Han, Jiahuai; Avruch, Joseph; Chen, Lanfen; Zhou, Dawang

Note: Order does not necessarily reflect citation order of authors.

Citation: Geng, J., X. Sun, P. Wang, S. Zhang, X. Wang, H. Wu, L. Hong, et al. 2015. “The kinases Mst1 and Mst2 positively regulate phagocyte ROS induction and bactericidal activity.” Nature immunology 16 (11): 1142-1152. doi:10.1038/ni.3268. http://dx.doi.org/10.1038/ni.3268.
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Abstract: Summary Mitochondria need to be juxtaposted to phagosomes to synergistically produce ample reactive oxygen species (ROS) in phagocytes for pathogens killing. However, how phagosomes transmit signal to recruit mitochondria remains unclear. Here, we report that the kinases Mst1 and Mst2 function to control ROS production by regulating mitochondrial trafficking and mitochondrion-phagosome juxtaposition. Mst1 and Mst2 activate Rac GTPase to promote Toll-like receptor (TLR)-triggered assembly of the TRAF6-ECSIT complex that is required for mitochondrial recruitment to phagosomes. Inactive forms of Rac, including the human Rac2D57N mutant, disrupt the TRAF6-ECSIT complex by sequestering TRAF6, and severely dampen ROS production and greatly increase susceptibility to bacterial infection. These findings demonstrate the TLR-Mst1-Mst2-Rac signalling axis to be critical for effective phagosome-mitochondrion function and bactericidal activity.
Published Version: doi:10.1038/ni.3268
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4618176/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:27320323
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