A Dual Phosphorylation Switch Balances Rice Immunity: Nature Communications Study Shows OsPUB2 Degrades OsPUB12
A rice immunity study by Zhao and colleagues was published in Nature Communications on November 11. The paper was received on February 4, 2026 and accepted on October 10, 2026, with digital object identifier 10.1038/s41467-026-79063-x.
The study reveals that the ubiquitin E3 ligase OsPUB2 specifically interacts with OsPUB12 and targets it for ubiquitin-mediated degradation. In contrast to the immunity-suppressing role of OsPUB12, OsPUB2 positively regulates resistance to rice bacterial diseases and contributes to pathogen-associated molecular pattern induced reactive oxygen burst and defense gene expression.
Upon pathogen challenge, the calcium-dependent kinase OsCPK17 and the mitogen-activated protein kinase OsMPK6 phosphorylate OsPUB12 at threonine 154 and serine 460 in a temporally sequential manner.
These two phosphorylation events oppositely regulate the interaction of OsPUB12 with OsPUB2 and its subsequent ubiquitination, leading to divergent regulation of OsPUB12 stability and rice immunity, the paper said.
The authors said the distinct phosphorylation of OsPUB12 by the two immune-related kinases synergistically maintains OsPUB2-mediated OsPUB12 homeostasis, serving as a core mechanism to fine-tune rice immunity.
Published by GSM · USA (original Chinese edition)
Photo: 图：稻田里正在成熟的水稻植株与金黄稻穗特写。Undeka 11 摄，CC BY-SA 4.0，经 Wikimedia Commons / Photo: Ripening rice plants in paddy field, Indonesia. By Undeka 11, CC BY-SA 4.0, via Wikimedia Commons
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