CoChat
Sign Up
Cited by 133

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding zinc finger

Danielsen, Jannie Rendtlew, Povlsen, Lou Klitgaard, Villumsen, Bine Hare, Streicher, Werner, Nilsson, Jakob, Wikström, Mats, Bekker-Jensen, Simon, Mailand, Niels·2012·Journal of Cell Biology
DOI 10.1083/jcb.201106152PMC PMC3328386
Open this paper in CoChat — free account

Abstract

Nonproteolytic ubiquitylation of chromatin surrounding deoxyribonucleic acid (DNA) double-strand breaks (DSBs) by the RNF8/RNF168/HERC2 ubiquitin ligases facilitates restoration of genome integrity by licensing chromatin to concentrate genome caretaker proteins near the lesions. In parallel, SUMOylation of so-far elusive upstream DSB regulators is also required for execution of this ubiquitin-dependent chromatin response. We show that HERC2 and RNF168 are novel DNA damage–dependent SUMOylation targets in human cells. In response to DSBs, both HERC2 and RNF168 were specifically modified with SUMO1 at DSB sites in a manner dependent on the SUMO E3 ligase PIAS4. SUMOylation of HERC2 was required for its DSB-induced association with RNF8 and for stabilizing the RNF8–Ubc13 complex. We also demonstrate that the ZZ Zinc finger in HERC2 defined a novel SUMO-specific binding module, which together with its concomitant SUMOylation and T4827 phosphorylation promoted binding to RNF8. Our findings provide novel insight into the regulatory complexity of how ubiquitylation and SUMOylation cooperate to orchestrate protein interactions with DSB repair foci.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1083/jcb.201106152

Cites

4 of 4 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • BRCA1, HERC2, and RNF168 are SUMOylated in response to genotoxic stress, which increases their ligase activity to support DNA damage repair.

    “For examples, BRCA1, HERC2, and RNF168 are SUMOylated in response to genotoxic stress for increased ligase activity so as to support DNA damage repair (36, 37).”

    From SUMOylation of the ubiquitin ligase IDOL decreases LDL receptor levels and is reversed by SENP1 (2021) · cites this paper as [37]

    The Results and discussion section (“SUMOylation of HERC2 and RNF168 in response to DSBs”; page not provided) reports increased SUMOylation of HERC2 and RNF168 after exposure to double-strand-break-inducing agents, but not other genotoxins. The Introduction links HERC2 SUMOylation to RNF8 binding and efficient ubiquitylation at damage sites. Our copy does not establish that BRCA1 is SUMOylated or that SUMOylation increases the ligase activity of all three proteins. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • SUMOylation can regulate the activity of several E3 ubiquitin ligases.

    “SUMOylation can regulate the activity of several E3 ubiquitin ligases.”

    From SUMOylation of the ubiquitin ligase IDOL decreases LDL receptor levels and is reversed by SENP1 (2021) · cites this paper as [37]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 32

  1. Bekker-Jensen, 2010, HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes, Nat. Cell Biol., 12, 80, 10.1038/ncb2008 · DOI
  2. Ciccia, 2010, The DNA damage response: Making it safe to play with knives, Mol. Cell., 40, 179, 10.1016/j.molcel.2010.09.019 · DOI · Paper page
  3. Devgan, 2011, Homozygous deficiency of ubiquitin-ligase ring-finger protein RNF168 mimics the radiosensitivity syndrome of ataxia-telangiectasia, Cell Death Differ., 18, 1500, 10.1038/cdd.2011.18 · DOI
  4. Dikic, 2009, Ubiquitin-binding domains - from structures to functions, Nat. Rev. Mol. Cell Biol., 10, 659, 10.1038/nrm2767 · DOI
  5. Doil, 2009, RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins, Cell., 136, 435, 10.1016/j.cell.2008.12.041 · DOI
  6. Galanty, 2009, Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks, Nature., 462, 935, 10.1038/nature08657 · DOI
  7. Garcia-Gonzalo, 2005, The HERC proteins: Functional and evolutionary insights, Cell. Mol. Life Sci., 62, 1826, 10.1007/s00018-005-5119-y · DOI
  8. Gileadi, 2008, High throughput production of recombinant human proteins for crystallography, Methods Mol. Biol., 426, 221, 10.1007/978-1-60327-058-8_14 · DOI
  9. Gill, 1989, Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem., 182, 319, 10.1016/0003-2697(89)90602-7 · DOI
  10. Hecker, 2006, Specification of SUMO1- and SUMO2-interacting motifs, J. Biol. Chem., 281, 16117, 10.1074/jbc.M512757200 · DOI
  11. Huen, 2007, RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly, Cell., 131, 901, 10.1016/j.cell.2007.09.041 · DOI
  12. Jackson, 2009, The DNA-damage response in human biology and disease, Nature., 461, 1071, 10.1038/nature08467 · DOI · Paper page
  13. Kim, 2007, Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response, Science., 316, 1202, 10.1126/science.1139621 · DOI · Paper page
  14. Kolas, 2007, Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase, Science., 318, 1637, 10.1126/science.1150034 · DOI
  15. Legge, 2004, ZZ domain of CBP: an unusual zinc finger fold in a protein interaction module, J. Mol. Biol., 343, 1081, 10.1016/j.jmb.2004.08.087 · DOI
  16. Mailand, 2006, Destruction of Claspin by SCFbetaTrCP restrains Chk1 activation and facilitates recovery from genotoxic stress, Mol. Cell., 23, 307, 10.1016/j.molcel.2006.06.016 · DOI · Paper page
  17. Mailand, 2007, RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins, Cell., 131, 887, 10.1016/j.cell.2007.09.040 · DOI
  18. Matic, 2010, Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif, Mol. Cell., 39, 641, 10.1016/j.molcel.2010.07.026 · DOI
  19. Misteli, 2009, The emerging role of nuclear architecture in DNA repair and genome maintenance, Nat. Rev. Mol. Cell Biol., 10, 243, 10.1038/nrm2651 · DOI
  20. Mohan, 2007, SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment, Mol. Cell. Biol., 27, 229, 10.1128/MCB.00323-06 · DOI
  21. Morris, 2004, BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair, Hum. Mol. Genet., 13, 807, 10.1093/hmg/ddh095 · DOI
  22. Morris, 2009, The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress, Nature., 462, 886, 10.1038/nature08593 · DOI · Paper page
  23. Omichinski, 1993, NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1, Science., 261, 438, 10.1126/science.8332909 · DOI
  24. Panier, 2009, Regulatory ubiquitylation in response to DNA double-strand breaks, DNA Repair (Amst.)., 8, 436, 10.1016/j.dnarep.2009.01.013 · DOI
  25. Polo, 2011, Dynamics of DNA damage response proteins at DNA breaks: A focus on protein modifications, Genes Dev., 25, 409, 10.1101/gad.2021311 · DOI · Paper page
  26. Smet-Nocca, 2011, SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity, BMC Biochem., 12, 4, 10.1186/1471-2091-12-4 · DOI
  27. Sobhian, 2007, RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites, Science., 316, 1198, 10.1126/science.1139516 · DOI
  28. Stewart, 2007, RIDDLE immunodeficiency syndrome is linked to defects in 53BP1-mediated DNA damage signaling, Proc. Natl. Acad. Sci. USA., 104, 16910, 10.1073/pnas.0708408104 · DOI
  29. Stewart, 2009, The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage, Cell., 136, 420, 10.1016/j.cell.2008.12.042 · DOI
  30. Wang, 2007, Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage, Proc. Natl. Acad. Sci. USA., 104, 20759, 10.1073/pnas.0710061104 · DOI
  31. Wiseman, 1989, Rapid measurement of binding constants and heats of binding using a new titration calorimeter, Anal. Biochem., 179, 131, 10.1016/0003-2697(89)90213-3 · DOI
  32. Wyman, 2006, DNA double-strand break repair: All’s well that ends well, Annu. Rev. Genet., 40, 363, 10.1146/annurev.genet.40.110405.090451 · DOI

Cited by

Sorted by citations

Metadata

Authors
Danielsen, J. R., Povlsen, L. K., Villumsen, B. H., Streicher, W., Nilsson, J., Wikström, M., Bekker-Jensen, S., & Mailand, N.
Affiliations
Ubiquitin Signaling Group 1 and 2 , and 3
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2012-04-16
Volume
197
Issue
2
Pages
179-187
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.201106152
PMC
PMC3328386
Cited by
133
References
4
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review