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Cited by 250DNA Repair MechanismsUbiquitin and proteasome pathwaysCancer-related Molecular Pathways

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination.

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Unk, Ildiko, Hajdú, Ildikó, Fátyol, Károly, Hurwitz, Jerard, Yoon, Jung-Hoon, Prakash, Louise, Prakash, Satya, Haracska, Lajos·2008·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0800563105PMC PMC2268824
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Abstract

Human helicase-like transcription factor (HLTF) is frequently inactivated in colorectal and gastric cancers. Here, we show that HLTF is a functional homologue of yeast Rad5 that promotes error-free replication through DNA lesions. HLTF and Rad5 share the same unique structural features, including a RING domain embedded within a SWI/SNF helicase domain and an HIRAN domain. We find that inactivation of HLTF renders human cells sensitive to UV and other DNA-damaging agents and that HLTF complements the UV sensitivity of a rad5Delta yeast strain. Also, similar to Rad5, HLTF physically interacts with the Rad6-Rad18 and Mms2-Ubc13 ubiquitin-conjugating enzyme complexes and promotes the Lys-63-linked polyubiquitination of proliferating cell nuclear antigen at its Lys-164 residue. A requirement of HLTF for error-free postreplication repair of damaged DNA is in keeping with its cancer-suppression role.

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Metadata

Authors
Unk, I., Hajdú, I., Fátyol, K., Hurwitz, J., Yoon, J.-H., Prakash, L., Prakash, S., & Haracska, L.
Affiliations
  • *Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Temesvari Körút 62, H-6726, Szeged, Hungary;
  • HUN-REN Szegedi Biológiai Kutatóközpont (HU)
  • Memorial Sloan Kettering Cancer Center (US)
  • The University of Texas Medical Branch at Galveston (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2008-03-11
Volume
105
Issue
10
Pages
3768-3773
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0800563105
PMC
PMC2268824
OpenAlex
W2073294832
Cited by
250
References
26
Citations by year
2026: 7 · 2025: 11 · 2024: 15 · 2023: 14 · 2022: 14 · 2021: 11 · 2020: 17 · 2019: 17 · 2018: 13 · 2017: 17 · 2016: 16 · 2015: 12 · 2014: 9 · 2013: 10 · 2012: 15
FWCI
7.12
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Howard Hughes Medical Institute (55005612)
  • Wellcome Trust
  • Hungarian Scientific Research Fund
  • Nemzeti Kutatási és Technológiai Hivatal
  • Hungarian Science Foundation
  • National Institutes of Health
  • Medical Research Council
  • National Cancer Institute (T32CA117834)
  • National Institute of Environmental Health Sciences (R01ES012411, ES 012411)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Keywords
HLTF, Rad5, ubiquitin ligase, postreplication repair, DNA damage response, UV sensitivity, RING domain, tumor suppression, colorectal cancer, gastric cancer
MeSH terms
Adenosine Triphosphatases, Cell Line, DNA Helicases, DNA-Binding Proteins, Drug Resistance, Genetic Complementation Test, Humans, Ligases, Lysine, Methyl Methanesulfonate, Mutation, Protein Binding, Saccharomyces cerevisiae, Transcription Factors, Ultraviolet Rays, Proliferating Cell Nuclear Antigen, Polyubiquitin, Saccharomyces cerevisiae Proteins, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Ubiquitination

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