BioID based proteomic analysis of the Bid interactome identifies novel proteins involved in cell cycle dependent apoptotic priming.

Robert Pedley, Louise King, Venkatesh Mallikarjun, Pengbo Wang, Joe Swift, Keith Brennan, Andrew Gilmore

Research output: Contribution to journalArticlepeer-review

Abstract

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 anti-mitotic 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.
Original languageEnglish
JournalCell Death and Disease
Publication statusAccepted/In press - 28 Sept 2020

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