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PLK1 phosphorylation of Epstein-Barr virus nuclear antigen 2

ABSTRACT: The Epstein-Barr virus nuclear antigen 2 (EBNA2) initiates and maintains the proliferation of infected B cells. In search of additional cellular strategies, that control EBNA2 function, we have performed a label-free mass spectrometry-based quantification of cellular proteins in EBNA2 immuno-precipitates and found polo-like kinase 1 (PLK1) to be bound to EBNA2. EBNA2/PLK1 complex formation is strongly enforced by EBNA2 S379 phosphorylation catalyzed by the mitotic CYCLIN B/CDK1 complex.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Human Herpesvirus 4 Strain B95-8

SUBMITTER: Piero Giansanti

LAB HEAD: Bernhard Kuster

PROVIDER: PXD022970 | Pride | 2021-08-22

REPOSITORIES: Pride

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PLK1-dependent phosphorylation restrains EBNA2 activity and lymphomagenesis in EBV-infected mice.

Zhang Xiang X Schuhmachers Patrick P Mourão André A Giansanti Piero P Murer Anita A Thumann Sybille S Kuklik-Roos Cornelia C Beer Sophie S Hauck Stefanie M SM Hammerschmidt Wolfgang W Küppers Ralf R Kuster Bernhard B Raab Monika M Strebhardt Klaus K Sattler Michael M Münz Christian C Kempkes Bettina B

EMBO reports 20211004 12

While Epstein-Barr virus (EBV) establishes a life-long latent infection in apparently healthy human immunocompetent hosts, immunodeficient individuals are at particular risk to develop lymphoproliferative B-cell malignancies caused by EBV. A key EBV protein is the transcription factor EBV nuclear antigen 2 (EBNA2), which initiates B-cell proliferation. Here, we combine biochemical, cellular, and in vivo experiments demonstrating that the mitotic polo-like kinase 1 (PLK1) binds to EBNA2, phosphor ...[more]

PMID: 34605140

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