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RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response

Academic Article
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Overview

authors

  • Groocock, L. M.
  • Nie, M.
  • Prudden, J.
  • Moiani, D.
  • Wang, T.
  • Cheltsov, Anton Vladislav
  • Rambo, R. P.
  • Arvai, A. S.
  • Hitomi, C.
  • Tainer, John
  • Luger, K.
  • Perry, J. J. P.
  • Lazzerini Denchi, Eros
  • Boddy, Michael

publication date

  • May 2014

journal

  • EMBO Reports  Journal

abstract

  • The post-translational modification of DNA repair and checkpoint proteins by ubiquitin and small ubiquitin-like modifier (SUMO) critically orchestrates the DNA damage response (DDR). The ubiquitin ligase RNF4 integrates signaling by SUMO and ubiquitin, through its selective recognition and ubiquitination of SUMO-modified proteins. Here, we define a key new determinant for target discrimination by RNF4, in addition to interaction with SUMO. We identify a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones. Furthermore, RNF4 nucleosome-targeting is crucially required for the repair of TRF2-depleted dysfunctional telomeres by 53BP1-mediated non-homologous end joining.

subject areas

  • Amino Acid Motifs
  • Animals
  • Cell Line
  • Chromosomal Proteins, Non-Histone
  • Crystallography, X-Ray
  • DNA Damage
  • DNA Repair
  • DNA-Binding Proteins
  • Gene Knockout Techniques
  • Mice
  • Nuclear Proteins
  • Nucleosomes
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Small Ubiquitin-Related Modifier Proteins
  • Tamoxifen
  • Telomere
  • Telomeric Repeat Binding Protein 2
  • Transcription Factors
  • Ubiquitin
  • Ubiquitination
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Research

keywords

  • RNF4
  • SUMO-targeted E3 ubiquitin ligase (STUbL)
  • small ubiquitin-like modifier
  • telomere
  • ubiquitin
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Identity

PubMed Central ID

  • PMC4210088

International Standard Serial Number (ISSN)

  • 1469-221X

Digital Object Identifier (DOI)

  • 10.1002/embr.201338369

PubMed ID

  • 24714598
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Additional Document Info

start page

  • 601

end page

  • 608

volume

  • 15

issue

  • 5

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