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Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay

Matsushita, Kazufumi, Takeuchi, Osamu, Standley, Daron M., Kumagai, Yutaro, Kawagoe, Tatsukata, Miyake, Tohru, Satoh, Takashi, Kato, Hiroki, Tsujimura, Tohru, Nakamura, Haruki, Akira, Shizuo·2009·Nature
DOI 10.1038/nature07924
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Abstract

Toll-like receptors (TLRs) recognize microbial components, and evoke inflammation and immune responses. TLR stimulation activates complex gene expression networks that regulate the magnitude and duration of the immune reaction. Here we identify the TLR-inducible gene Zc3h12a as an immune response modifier that has an essential role in preventing immune disorders. Zc3h12a-deficient mice suffered from severe anaemia, and most died within 12 weeks. Zc3h12a(-/-) mice also showed augmented serum immunoglobulin levels and autoantibody production, together with a greatly increased number of plasma cells, as well as infiltration of plasma cells to the lung. Most Zc3h12a(-/-) splenic T cells showed effector/memory characteristics and produced interferon-gamma in response to T-cell receptor stimulation. Macrophages from Zc3h12a(-/-) mice showed highly increased production of interleukin (IL)-6 and IL-12p40 (also known as IL12b), but not TNF, in response to TLR ligands. Although the activation of TLR signalling pathways was normal, Il6 messenger RNA decay was severely impaired in Zc3h12a(-/-) macrophages. Overexpression of Zc3h12a accelerated Il6 mRNA degradation via its 3'-untranslated region (UTR), and destabilized RNAs with 3'-UTRs for genes including Il6, Il12p40 and the calcitonin receptor gene Calcr. Zc3h12a contains a putative amino-terminal nuclease domain, and the expressed protein had RNase activity, consistent with a role in the decay of Il6 mRNA. Together, these results indi…

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Research works printed but not linked: 20

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Metadata

Authors
Matsushita, K., Takeuchi, O., Standley, D. M., Kumagai, Y., Kawagoe, T., Miyake, T., Satoh, T., Kato, H., Tsujimura, T., Nakamura, H., & Akira, S.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2009-03-25
Volume
458
Issue
7242
Pages
1185-1190
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature07924
Cited by
649
References
2
Language
en
Licence
www.springer.com/tdm (tdm)

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