Academic Journal

Temporal regulation of Lsp1 O-GlcNAcylation and phosphorylation during apoptosis of activated B cells

التفاصيل البيبلوغرافية
العنوان: Temporal regulation of Lsp1 O-GlcNAcylation and phosphorylation during apoptosis of activated B cells
المؤلفون: Wu, Jung-Lin, Wu, Hsin-Yi, Tsai, Dong-Yan, Chiang, Ming-Feng, Chen, Yi-Ju, Gao, Shijay, Lin, Chun-Cheng, Lin, Chun-Hung, Khoo, Kay-Hooi, Chen, Yu-Ju, Lin, Kuo-I.
المصدر: Nature Communications ; volume 7, issue 1 ; ISSN 2041-1723
بيانات النشر: Springer Science and Business Media LLC
سنة النشر: 2016
الوصف: Crosslinking of B-cell receptor (BCR) sets off an apoptosis programme, but the underlying pathways remain obscure. Here we decipher the molecular mechanisms bridging B-cell activation and apoptosis mediated by post-translational modification (PTM). We find that O -GlcNAcase inhibition enhances B-cell activation and apoptosis induced by BCR crosslinking. This proteome-scale analysis of the functional interplay between protein O -GlcNAcylation and phosphorylation in stimulated mouse primary B cells identifies 313 O -GlcNAcylation-dependent phosphosites on 224 phosphoproteins. Among these phosphoproteins, temporal regulation of the O -GlcNAcylation and phosphorylation of lymphocyte-specific protein-1 (Lsp1) is a key switch that triggers apoptosis in activated B cells. O -GlcNAcylation at S209 of Lsp1 is a prerequisite for the recruitment of its kinase, PKC-β1, to induce S243 phosphorylation, leading to ERK activation and downregulation of BCL-2 and BCL-xL. Thus, we demonstrate the critical PTM interplay of Lsp1 that transmits signals for initiating apoptosis after BCR ligation.
نوع الوثيقة: article in journal/newspaper
اللغة: English
DOI: 10.1038/ncomms12526
الاتاحة: http://dx.doi.org/10.1038/ncomms12526
https://www.nature.com/articles/ncomms12526.pdf
https://www.nature.com/articles/ncomms12526
Rights: https://creativecommons.org/licenses/by/4.0 ; https://creativecommons.org/licenses/by/4.0
رقم الانضمام: edsbas.159F9491
قاعدة البيانات: BASE