Control of APC/C-dependent ubiquitin chain elongation by reversible phosphorylation

Proceedings of the National Academy of Sciences of the United States of America
Allison CraneyMichael Rape

Abstract

Most metazoan E3 ligases contain a signature RING domain that promotes the transfer of ubiquitin from the active site of E2 conjugating enzymes to lysine residues in substrates. Although these RING-E3s depend on E2 enzymes for catalysis, how they turn on their E2s at the right time and place remains poorly understood. Here we report a phosphorylation-dependent mechanism that ensures timely activation of the E2 Ube2S by its RING-E3, the anaphase-promoting complex (APC/C); while phosphorylation of a specific serine residue in the APC/C coactivator Cdc20 prevents delivery of Ube2S to the APC/C, removal of this mark by PP2A(B56) allows Ube2S to bind the APC/C and catalyze ubiquitin chain elongation. PP2A(B56) also stabilizes kinetochore-microtubule attachments to shut off the spindle checkpoint, suggesting that cells regulate the E2-E3 interplay to coordinate ubiquitination with critical events during cell division.

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Citations

Apr 27, 2016·Proceedings of the National Academy of Sciences of the United States of America·Renping QiaoJan-Michael Peters
Aug 6, 2016·Frontiers in Genetics·Stefano Ferrari, Christian Gentili
Nov 15, 2017·Cold Spring Harbor Symposia on Quantitative Biology·Pablo Lara-GonzalezArshad Desai
Feb 10, 2019·Biomolecules·Margarida Moura, Carlos Conde
Apr 30, 2017·Cellular and Molecular Life Sciences : CMLS·Hazel F O'Connor, Jon M Huibregtse
Jul 25, 2019·Frontiers in Physiology·Kirandeep K DeolEric R Strieter
May 13, 2020·Nature Structural & Molecular Biology·Raquel C Martinez-ChacinNicholas G Brown
Apr 14, 2017·Journal of Cell Science·Sun Joo LeeEmily A Foley
Nov 18, 2018·The Journal of Cell Biology·Jakob Nilsson
Jul 13, 2017·Genes & Development·Taekyung KimArshad Desai
Jul 5, 2018·Frontiers in Cell and Developmental Biology·Adrian T Saurin
Dec 15, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Meenu MaanSrikumar P Chellappan

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