GSK3 phosphorylates nucleoprotein

Phosphorylation of SARS-Cov-2 nucleocapsid is catalyzed by glycogen synthase kinase 3 (GSK3) and several other host cell kinases. Phosphorylated N forms a liquid-like compartment, possibly suited for viral genome processing (Carlson et al, 2020). GSK3 phosphorylations depend on priming phosphorylations on at least two sites by SRPK1/2 protein kinases (Heaton et al, 2020).<br><br>Three proteomics papers show varying sites for phosphorylations on N that can be explained by specific phosphorylation catalyzed by GSK3 when primed by phosphorylations on S188 and S206. The sites S176, S180, S184, S194, T198 and S202 are supported by at least two of the three papers (Bouhaddou et al, 2020; Davidson et al, 2020; Klann et al, 2020). Another analysis found S176 phosphorylated in about half of the cases (Supekar et al, 2021)..

SARS-CoV-2 核衣壳的磷酸化作用由糖原合成酶激酶3（GSK3）以及多种宿主细胞激酶催化。磷酸化的N形成类似液体的细胞器，可能适合于病毒基因组处理（Carlson等，2020年）。GSK3的磷酸化作用依赖于SRPK1/2蛋白激酶在至少两个位点上的启动磷酸化（Heaton等，2020年）。三篇蛋白质组学论文展示了N上磷酸化的不同位点，这些差异可通过GSK3在S188和S206位点磷酸化启动下的特定磷酸化作用来解释。位点S176、S180、S184、S194、T198和S202至少被三篇论文中的两篇所支持（Bouhaddou等，2020年；Davidson等，2020年；Klann等，2020年）。另一项分析发现，约有一半的情况下S176发生磷酸化（Supekar等，2021年）。