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Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination.
Open accessAbstract
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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“In template switching, the monoubiquitin moiety added to K164 of PCNA is instead further ubiquitinated by the HLTF E3 ubiquitin ligase, to form a K63-linked ubiquitin chain (Motegi et al., 2008; Unk et al., 2008).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Unk et al., 2008
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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)
- 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
- 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
- green
- www.ncbi.nlm.nih.gov
- 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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