ArticleOncotarget2016
E2F1 interactions with hHR23A inhibit its degradation and promote DNA repair.
Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Role of Kindlin-2 in Cutaneous Squamous Carcinoma Cell Migration and Proliferation: Implications for Tumour Progression.International journal of molecular sciences · 2025Article
- Article
- β-arrestin 1 and integrin-linked kinase interact in epidermal keratinocytes and regulate cell motility.Tissue barriers · 2025Article
- The E2F1 transcription factor and RB tumor suppressor moonlight as DNA repair factors.Cell cycle (Georgetown, Tex.) · 2020Review
- Protective role of integrin-linked kinase against oxidative stress and in maintenance of genomic integrity.Oncotarget · 2018Article
- A reporter mouse model forBiology open · 2017Article
- CDH1 regulates E2F1 degradation in response to differentiation signals in keratinocytes.Oncotarget · 2017Article
- E2F1-directed activation of nc886 mediates drug resistance in cervical cancer cells via regulation of major vault protein.International journal of clinical and experimental pathology · 2017Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleotide excision repair (NER) is a major mechanism for removal of DNA lesions induced by exposure to UV radiation in the epidermis. Recognition of damaged DNA sites is the initial step in their repair, and requires multiprotein complexes that contain XPC and hHR23 proteins, or their orthologues. A variety of transcription factors are also involved in NER, including E2F1. In epidermal keratinocytes, UV exposure induces E2F1 phosphorylation, which allows it to recruit various NER factors to sites of DNA damage. However, the relationship between E2F1 and hHR23 proteins vis-à-vis NER has remained unexplored. We now show that E2F1 and hHR23 proteins can interact, and this interaction stabilizes E2F1, inhibiting its proteasomal degradation. Reciprocally, E2F1 regulates hHR23A subcellular localization, recruiting it to sites of DNA photodamage. As a result, E2F1 and hHR23A enhance DNA repair following exposure to UV radiation, contributing to genomic stability in the epidermis.
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Registered trials
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