MAD2L2 dimerization and TRIP13 control shieldin activity in DNA repair
MAD2L2 — a member of the shieldin complex — is known to play important roles in DNA repair. Here the authors demonstrate how MAD2L2 dimerization mediated through SHLD2 participates in shieldin assembly and function.
Saved in:
Main Authors: | Inge de Krijger, Bastian Föhr, Santiago Hernández Pérez, Estelle Vincendeau, Judit Serrat, Alexander Marc Thouin, Vivek Susvirkar, Chloé Lescale, Inés Paniagua, Liesbeth Hoekman, Simranjeet Kaur, Maarten Altelaar, Ludovic Deriano, Alex C. Faesen, Jacqueline J. L. Jacobs |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2021
|
Subjects: | |
Online Access: | https://doaj.org/article/ff52d6b334fd4c1a8c8a1c74813d0adb |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing
by: Melissa L. Brulotte, et al.
Published: (2017) -
Molecular basis for assembly of the shieldin complex and its implications for NHEJ
by: Ling Liang, et al.
Published: (2020) -
Acute systemic loss of Mad2 leads to intestinal atrophy in adult mice
by: Klaske M. Schukken, et al.
Published: (2021) -
Mad1's ability to interact with Mad2 is essential to regulate and monitor meiotic synapsis in C. elegans.
by: Alice Devigne, et al.
Published: (2021) - Revista MAD