SARS-CoV-2 N binds to 14-3-3 proteins

Stable Identifier
R-HSA-9729500
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
ReviewStatus
5/5
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14-3-3 proteins directly shuttle SARS-CoV-1 N protein in a phosphorylation-dependent manner from nucleus to cytosol (Surjit et al, 2005). Polyphosphorylated SARS-CoV-2 N interacts with all seven human 14-3-3 isoforms via its phosphorylated S197. It is probable that this results in the shuttling of phosphorylated N from nucleus to cytosol. Moreover, 14-3-3 binding to p-N may present a cell immune-like response to the viral infection aimed at arresting or neutralizing N activities. On the other hand, in light of the abundance of N protein in the infected cell, p-N may instead arrest 14-3-3 proteins in the cytoplasm and indirectly disrupt cellular processes involving 14-3-3 (Tugaeva et al, 2021).
Literature References
PubMed ID Title Journal Year
33556408 The Mechanism of SARS-CoV-2 Nucleocapsid Protein Recognition by the Human 14-3-3 Proteins

Tugaeva, KV, Ker, DS, Bayfield, OW, Smith, JLR, Antson, AA, Sysoev, AA, Klychnikov, OI, Sluchanko, NN, Hawkins, DEDP

J Mol Biol 2021
16103198 The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation

Mishra, RN, Kumar, R, Reddy, MK, Chow, VT, Surjit, M, Lal, SK

J. Virol. 2005
Participants
Participates
Disease
Name Identifier Synonyms
COVID-19 DOID:0080600 2019 Novel Coronavirus (2019-nCoV), Wuhan seafood market pneumonia virus infection, 2019-nCoV infection, Wuhan coronavirus infection
Authored
Reviewed
Created
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