ArticleBiochemistry2018
Antiparallel Coiled-Coil Interactions Mediate the Homodimerization of the DNA Damage-Repair Protein PALB2.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- Specifications of the ACMG/AMP variant curation guidelines for the analysis of germline PALB2 sequence variants.American journal of human genetics · 2025Article
- PALB2 and 53BP1 govern post-resection homologous recombination DNA repair.Molecular cell · 2025Article
- Review
- Structural analysis of genetic variants of the human tumor suppressor PALB2 coiled-coil domain.Bioscience reports · 2025Article
- Proline variants in the BRCA1 coiled-coil domain disrupt folding and binding to PALB2.Protein science : a publication of the Protein Society · 2025Article
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.iScience · 2024Article
- Installation of an Indole on the BRCA1 Disordered Domain Using Triazine Chemistry.Biomolecules · 2024Article
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.bioRxiv : the preprint server for biology · 2024Article
- Splicing Analysis of 16Cancers · 2022Article
- BRCA1-Dependent and Independent Recruitment of PALB2-BRCA2-RAD51 in the DNA Damage Response and Cancer.Cancer research · 2022Review
- Functional assessment of missense variants of uncertain significance in the cancer susceptibility gene PALB2.NPJ breast cancer · 2022Article
- Splicing predictions, minigene analyses, and ACMG-AMP clinical classification of 42 germline PALB2 splice-site variants.The Journal of pathology · 2022Article
- The roles and targeting options of TRIM family proteins in tumor.Frontiers in pharmacology · 2022Review
- Poly(ADP-ribose) binding and macroH2A mediate recruitment and functions of KDM5A at DNA lesions.The Journal of cell biology · 2021Article
- A Validated Functional Analysis of Partner and Localizer of BRCA2 Missense Variants for Use in Clinical Variant Interpretation.The Journal of molecular diagnostics : JMD · 2021Article
- Structural characterization of the self-association domain of swallow.Protein science : a publication of the Protein Society · 2021Article
- Making Connections: Integrative Signaling Mechanisms Coordinate DNA Break Repair in Chromatin.Frontiers in genetics · 2021Review
- Molecular Mechanisms of PALB2 Function and Its Role in Breast Cancer Management.Frontiers in oncology · 2020Review
- A global functional analysis of missense mutations reveals two major hotspots in the PALB2 tumor suppressor.Nucleic acids research · 2019Article
- Article
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8 authors at 1 institution in 1 country.
Funding
Abstract
Deficits in DNA damage-repair pathways are the root cause of several human cancers. In mammalian cells, DNA double-strand break repair is carried out by multiple mechanisms, including homologous recombination (HR). The partner and localizer of BRCA2 (PALB2), which is an essential factor for HR, binds to the breast cancer susceptibility 1 (BRCA1) protein at DNA double-strand breaks. At the break site, PALB2 also associates with the breast cancer susceptibility 2 (BRCA2) protein to form a multiprotein complex that facilitates HR. The BRCA1-PALB2 interaction is mediated by association of predicted helical coiled-coil regions in both proteins. PALB2 can also homodimerize through the formation of a coiled coil by the self-association of helical elements at the N-terminus of the PALB2 protein, and this homodimerization has been proposed to regulate the efficiency of HR. We have produced a segment of PALB2, designated PALB2cc (PALB2 coiled coil segment) that forms α-helical structures, which assemble into stable homodimers. PALB2cc also forms heterodimers with a helical segment of BRCA1, called BRCA1cc (BRCA1 coiled coil segment). The three-dimensional structure of the homodimer formed by PALB2cc was determined by solution NMR spectroscopy. This PALB2cc homodimer is a classical antiparallel coiled-coil leucine zipper. NMR chemical-shift perturbation studies were used to study dimer formation for both the PALB2cc homodimer and the PALB2cc/BRCA1cc heterodimer. The mutation of residue Leu24 of PALB2cc significantly reduces its homodimer stability, but has a more modest effect on the stability of the heterodimer formed between PALB2cc and BRCA1cc. We show that mutation of Leu24 leads to genomic instability and reduced cell viability after treatment with agents that induce DNA double-strand breaks. These studies may allow the identification of distinct mutations of PALB2cc that selectively disrupt homodimeric versus heterodimeric interactions, and reveal the specific role of PALB2cc homodimerization in HR.
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