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A novel phosphorylation site in SARS-CoV-2 nucleocapsid regulates its RNA-binding capacity and phase separation in host cells
Junyu Wu1,†,* , Yongheng Zhong1 , Xue Liu1 , Xiaoyu Lu1 , Weijie Zeng1 , Chunyan Wu1 , Fan Xing1 , Liu Cao1 , Fuxiang Zheng1 , Panpan Hou1 , Hong Peng1 , Chunmei Li1 , Deyin Guo1,*
1Centre for Infection and Immunity Study (CIIS), School of Medicine, Shenzhen Campus of Sun Yat-sen University, Shenzhen 518197, China
These authors contributed equally to this work.
*Correspondence to:Junyu Wu , Email:wujy68@mail.sysu.edu.cn Deyin Guo , Email:guodeyin@mail.sysu.edu.cn
J Mol Cell Biol, Volume 14, Issue 2, February 2022, mjac003,  https://doi.org/10.1093/jmcb/mjac003

Dear Editor,

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel emerging coronavirus that has spread worldwide since breaking out in late 2019 and has led to hundreds of millions of infections and millions of human deaths (Zhou et al., 2020). The genome of SARS-CoV-2 encodes 29 viral proteins, including four structural proteins: spike (S), envelope (E), membrane (M), and nucleocapsid (N) (Kim et al., 2020). N protein is essential for viral genomic RNA replication and packaging and it also plays an important role in the virus‒host interactions (Lang et al., 2021). The amino acid sequences of N protein are highly conserved among coronaviruses (Supplementary Figure S1). Accumulating evidence indicates that N protein is a phosphoprotein and its phosphorylation state is important for its proper function (Peng et al., 2008Wu et al., 2014).