BioID-based proteomic analysis of the Bid interactome identifies novel proteins involved in cell-cycle-dependent apoptotic priming
AuthorsPedley, Robert; orcid: 0000-0002-0801-7240
King, Louise E.
Gilmore, Andrew P.; orcid: 0000-0002-9988-0436; email: firstname.lastname@example.org
MetadataShow full item record
AbstractAbstract: Apoptotic priming controls the commitment of cells to apoptosis by determining how close they lie to mitochondrial permeabilisation. Variations in priming are important for how both healthy and cancer cells respond to chemotherapeutic agents, but how it is dynamically coordinated by Bcl-2 proteins remains unclear. The Bcl-2 family protein Bid is phosphorylated when cells enter mitosis, increasing apoptotic priming and sensitivity to antimitotic drugs. Here, we report an unbiased proximity biotinylation (BioID) screen to identify regulators of apoptotic priming in mitosis, using Bid as bait. The screen primarily identified proteins outside of the canonical Bid interactome. Specifically, we found that voltage-dependent anion-selective channel protein 2 (VDAC2) was required for Bid phosphorylation-dependent changes in apoptotic priming during mitosis. These results highlight the importance of the wider Bcl-2 family interactome in regulating the temporal control of apoptotic priming.
CitationCell Death & Disease, volume 11, issue 10, page 872
PublisherNature Publishing Group UK
DescriptionFrom Springer Nature via Jisc Publications Router
History: received 2020-05-13, rev-recd 2020-09-24, accepted 2020-09-28, collection 2020-10, registration 2020-10-07, online 2020-10-16, pub-electronic 2020-10-16
Publication status: Published
Funder: John and Janet Hartley