Other
24 Authors
- Tang M,
- Bu CH,
- Su L,
- Fina M,
- Scott L,
- Kravchenko VV,
- Russell J,
- Wang Y,
- Chen D,
- Lyon S,
- Mathison JC,
- Moresco EM,
- Monson NL,
- Beutler B,
- Arnett S,
- Hildebrand S,
- Ulevitch RJ,
- Quan J,
- Shi H,
- Sun Q,
- Pratt D,
- Jurek P,
- Zhan X,
- Li X
| First Author | Shi H | Year | 2016 |
| Journal | Nat Immunol | Volume | 17 |
| Issue | 3 | Pages | 250-8 |
| PubMed ID | 26642356 | Mgi Jnum | J:226677 |
| Mgi Id | MGI:5698271 | Doi | 10.1038/ni.3333 |
| Citation | Shi H, et al. (2016) NLRP3 activation and mitosis are mutually exclusive events coordinated by NEK7, a new inflammasome component. Nat Immunol 17(3):250-8 |
| abstractText | The NLRP3 inflammasome responds to microbes and danger signals by processing and activating proinflammatory cytokines, including interleukin 1beta (IL-1beta) and IL-18. We found here that activation of the NLRP3 inflammasome was restricted to interphase of the cell cycle by NEK7, a serine-threonine kinase previously linked to mitosis. Activation of the NLRP3 inflammasome required NEK7, which bound to the leucine-rich repeat domain of NLRP3 in a kinase-independent manner downstream of the induction of mitochondrial reactive oxygen species (ROS). This interaction was necessary for the formation of a complex containing NLRP3 and the adaptor ASC, oligomerization of ASC and activation of caspase-1. NEK7 promoted the NLRP3-dependent cellular inflammatory response to intraperitoneal challenge with monosodium urate and the development of experimental autoimmune encephalitis in mice. Our findings suggest that NEK7 serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division. |
