ArticleNucleic acids research2017
A novel TPR-BEN domain interaction mediates PICH-BEND3 association.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 34 citations in OpenAlex.
- ERCC6L-mediated stabilization of HIF-1α enhances glycolysis and stemness properties of lung adenocarcinoma cells.Cell death & disease · 2025Article
- Article
- The interplay of the translocase activity and protein recruitment function of PICH in ultrafine anaphase bridge resolution and genomic stability.Nucleic acids research · 2025Article
- Integrated Pan-Cancer Profiling and Breast Cancer Validation Identify BEND3 as a Potential Prognostic and Immune Biomarker.Breast cancer (Dove Medical Press) · 2025Article
- A dual-function SNF2 protein drives chromatid resolution and nascent transcripts removal in mitosis.EMBO reports · 2023Article
- ERCC6L facilitates the onset of mammary neoplasia and promotes the high malignance of breast cancer by accelerating the cell cycle.Journal of experimental & clinical cancer research : CR · 2023Article
- Review
- PLK-1 Interacting Checkpoint Helicase, PICH, Mediates Cellular Oxidative Stress Response.Epigenomes · 2022Article
- BEND3 safeguards pluripotency by repressing differentiation-associated genes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Distinct structural bases for sequence-specific DNA binding by mammalian BEN domain proteins.Genes & development · 2022Article
- Interaction between BEND5 and RBPJ suppresses breast cancer growth and metastasis via inhibiting Notch signaling.International journal of biological sciences · 2022Article
- Regulation of mitotic chromosome architecture and resolution of ultrafine anaphase bridges by PICH.Cell cycle (Georgetown, Tex.) · 2021Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PICH is a DNA translocase required for the maintenance of chromosome stability in human cells. Recent data indicate that PICH co-operates with topoisomerase IIα to suppress pathological chromosome missegregation through promoting the resolution of ultra-fine anaphase bridges (UFBs). Here, we identify the BEN domain-containing protein 3 (BEND3) as an interaction partner of PICH in human cells in mitosis. We have purified full length PICH and BEND3 and shown that they exhibit a functional biochemical interaction in vitro. We demonstrate that the PICH-BEND3 interaction occurs via a novel interface between a TPR domain in PICH and a BEN domain in BEND3, and have determined the crystal structure of this TPR-BEN complex at 2.2 Å resolution. Based on the structure, we identified amino acids important for the TPR-BEN domain interaction, and for the functional interaction of the full-length proteins. Our data reveal a proposed new function for BEND3 in association with PICH, and the first example of a specific protein-protein interaction mediated by a BEN domain.
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