Application of the Schroeder-Le Chatelier law of solubility to solutions of salts in organic liquids

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Abstract

SUMMARY

Herpesviruses encode conserved protein kinases to stimulate phosphorylation-sensitive processes during infection. How these kinases bind to cellular factors and how this impacts their regulatory functions is poorly understood. Here, we use quantitative proteomics to determine cellular interaction partners of human herpesvirus (HHV) kinases. We find that these kinases can target key regulators of transcription and replication. The interaction with Cyclin A and associated factors is identified as a specific signature of β-herpesvirus kinases. Cyclin A is recruited via RXL-motifs that overlap with nuclear localization signals (NLS) and locate in the non-catalytic N-terminal regions. This architecture is conserved for viral kinases of HHV6, HHV7 and rodent CMVs. Docking to Cyclin A competes with NLS function, enabling dynamic changes in kinase localization and substrate phosphorylation. The viral kinase redirects Cyclin A to the cytosol, which is essential for the inhibition of cellular DNA replication during infection. Our data highlight a fine-tuned and physiologically important interplay between a cellular cyclin and viral kinases.
Reference Key
openalex_W2332079989 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors C. E. Linebarger
Journal american journal of science
Year 1895
DOI
10.2475/ajs.s3-49.289.48
URL
https://ajsonline.org/article/63051.pdf
Keywords Keywords not found

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