Nucleocytoplasmic Shuttling of Geminivirus C4 Protein Mediated by Phosphorylation and Myristoylation Is Critical for Viral Pathogenicity

文献类型： 外文期刊

第一作者： Wang, Yaqin

作者： Wang, Yaqin;Hu, Tao;Zhou, Xueping;Yang, Xiuling;Zhou, Xueping;Lozano-Duran, Rosa;Sunter, Garry

作者机构：

关键词： Geminivirus; C4; phosphorylation; myristoylation; pathogenicity; nucleocytoplasmic shuttling

期刊名称：MOLECULAR PLANT （ 影响因子：13.164； 五年影响因子：16.357 ）

ISSN： 1674-2052

年卷期： 2018 年 11 卷 12 期

页码：

收录情况： SCI

摘要： Many geminivirus C4 proteins induce severe developmental abnormalities in plants. We previously demonstrated that Tomato leaf curl Yunnan virus (TLCYnV) C4 induces plant developmental abnormalities at least partically by decreasing the accumulation of NbSK eta, an ortholog of Arabidopsis BIN2 kinase involved in the brassinosteroid signaling pathway, in the nucleus through directing it to the plasma membrane. However, the molecular mechanismby which the membrane-associated C4 modifies the localization of NbSKh in the host cell remains unclear. Here, we show that TLCYnV C4 is a nucleocytoplasmic shuttle protein, and that C4 shuttling is accompanied by nuclear export of NbSKh. TLCYnV C4 is phosphorylated by NbSKh in the nucleus, which promotes myristoylation of the viral protein. Myristoylation of phosphorylated C4 favors its interaction with exportin-alpha (XPO I), which in turn facilitates nuclear export of the C4/NbSK eta complex. Supporting this model, chemical inhibition of N-myristoyltransferases or exportin-alpha enhanced nuclear retention of C4, and mutations of the putative phosphorylation or myristoylation sites in C4 resulted in increased nuclear retention of C4 and thus decreased severity of C4-induced developmental abnormalities. The impact of C4 on development is also lessened when a nuclear localization signal or a nuclear export signal is added to its C-terminus, restricting it to a specific cellular niche and therefore impairing nucleocytoplasmic shuttling. Taken together, our results suggest that nucleocytoplasmic shuttling of TLCYnV C4, enabled by phosphorylation by NbSKh, myristoylation, and interaction with exportin-alpha, is critical for its function as a pathogenicity factor.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序