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. 2017 Aug 28;36(50):6850–6862. doi: 10.1038/onc.2017.295

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Copyright © 2017 The Author(s)

This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/

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Vps34 induces PKC-δ-dependent phosphorylation of p62. (a), (b) PKC δ is a specific protein kinase to p62 in cells. Cell lysates from MCF-7 cells transfected as indicated were analyzed by western blotting with antibodies recognizing phosphorylated p62 at S349, Myc-tag, falg-tag and β-actin. (c) In vitro phosphorylation of p62 by PKC-δ. (d) Vps34 dose-dependently enhanced the formation of p62-PKC δ machinery, and consequently the phosphorylation of p62. MCF7 cells were cotransfected with myc-p62, F-PKC δ and increasing number of V5-Vps34 constructs for 48 h followed by immunoprecipitation assays for the formation of p62-PKC δ machinery and the phosphorylation of p62. (e) Ablation of Vps34 decreased PKC-δ-dependent phosphorylation of p62. Myc-p62 with or without F-PKC-δ was cotransfected into MCF-7 or Vps34 knockout MCF-7 cells for 48 h followed by the detection, as indicated.