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. 2014 Jul 31;5(7):e1358. doi: 10.1038/cddis.2014.316

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Copyright © 2014 Macmillan Publishers Limited

Cell Death and Disease is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported 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/3.0/

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Bid is protected from caspase-8 cleavage to tBid by phosphorylation at a threonine residue. (a) Cleavage of endogenous Bid (the lysate of PC-3 cells expressing ALDH1L1) to tBid by recombinant caspase-8 before and after pretreatment with λ protein phosphatase (PPase). Control, lysate from PC-3 cells transfected with ‘empty' vector. (b) Cleavage of recombinant Bid exposed to lysate from ALDH1L1-expressing PC-3 cells by caspase-8 with and without PPase pretreatment. Control, recombinant Bid exposed to lysate from PC-3 cells transfected with ‘empty' vector. (c) In vitro phosphorylation of recombinant Bid by JNK1-3 (band corresponding to Bid is detected by phospho-threonine antibody). (d) Cleavage of recombinant Bid before and after in vitro kinase reaction in the presence of JNK2. (e) Mass-spectrometry identification of phosphorylated Bid peptides after in vitro kinase assay with JNK1-3 (numbers on the plot indicate the abundance of the phosphopeptide upon phosphorylation with each JNK)