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Details on Person Phosphorylation of SARS-Cov-2 nucleocapsid is catalyzed by g...

Class:IdSummation:9694680
_displayNamePhosphorylation of SARS-Cov-2 nucleocapsid is catalyzed by g...
_timestamp2022-01-25 08:39:50
created[InstanceEdit:9694660] Cook, Justin, 2020-07-07
literatureReference[LiteratureReference:9713210] Phosphorylation modulates liquid-liquid phase separation of the SARS-CoV-2 N protein
modified[InstanceEdit:9699090] Cook, Justin, 2020-09-10
[InstanceEdit:9713198] Stephan, Ralf, 2021-01-22
[InstanceEdit:9728917] Orlic-Milacic, Marija, 2021-04-23
[InstanceEdit:9729255] Stephan, Ralf, 2021-04-28
[InstanceEdit:9762455] Stephan, Ralf, 2022-01-25
textPhosphorylation 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).

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)..
(summation)[Reaction:9729260] GSK3 phosphorylates nucleoprotein [Homo sapiens]
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