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A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair [RNA-seq]

ABSTRACT: A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair [RNA-seq]

PROVIDER: PRJNA756281 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15529500.fastq.gz	Fastqsanger.gz
	SRR15529501.fastq.gz	Fastqsanger.gz
	SRR15529502.fastq.gz	Fastqsanger.gz
	SRR15529503.fastq.gz	Fastqsanger.gz
	SRR15529504.fastq.gz	Fastqsanger.gz

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A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair [CNV-seq]

Project description:The BRCA1 tumor suppressor gene encodes a multi-domain protein for which several functions have been described. These include a key role in homologous recombination repair (HRR) of DNA double-strand breaks (DSBs), which is shared with two other high-risk hereditary breast cancer suppressors, BRCA2 and PALB2. Although both BRCA1 and BRCA2 interact with PALB2, BRCA1 missense variants affecting its PALB2-interacting coiled-coil domain are considered sequence variants of uncertain clinical significance (VUS). Using genetically engineered mice, we now show that a BRCA1 coiled-coil domain VUS, Brca1 p.L1363P, disrupting the interaction with PALB2 leads to embryonic lethality and loss of breast cancer suppression. Brca1 p.L1363P mammary tumors develop with a similar latency as Brca1-null tumors, but show different histopathological features and more stable DNA copy number profiles. Nevertheless, Brca1 p.L1363P mammary tumors are HRR-incompetent and responsive to cisplatin and PARP inhibition.

2022-02-01 | GSE182449 | GEO

A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair [RNA-seq]

2022-02-01 | GSE182448 | GEO

A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair.

Project description:A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair.

| PRJNA756277 | ENA

A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair [CNV-seq]

Project description:A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair [CNV-seq]

| PRJNA756282 | ENA

PALB2 and 53BP1 govern post-resection homologous recombination DNA repair

Project description:Homologous recombination (HR) requires the resection of DNA breaks and RAD51 filament formation. Protein complexes that control end resection have been characterized, but regulators of RAD51 loading are not well defined. PALB2 is a mediator of BRCA2-RAD51 DNA break localization; it can also bind BRCA1, or form homodimers with DNA binding activity, via its coiled-coil (CC) domain. Here, we created a CC mutated mouse allele (Palb2CC) that disrupts CC-mediated interactions. While Palb2CC/CC embryos were not viable; remarkably, intercrossing with mice lacking 53BP1, an inhibitor of PALB2-chromatin contacts, produced live-births. However, Palb2CC/CC53bp1-/- mice were tumor-prone and cells had limited RAD51 foci. HR remained inefficient because the CC domain was required for PALB2 to bind to single-stranded (ss)DNA overhangs and subsequently promote PALB2 and RAD51 accumulation. These findings underscore the role of ssDNA binding in localizing PALB2 to DNA breaks, while establishing genetic interactions that control post-end resection steps in mammalian HR.

2025-07-23 | GSE299657 | GEO

A BRCA1 coiled-coil domain variant disrupting PALB2 interaction predisposes to mammary tumors with a targetable defect in homologous recombination repair.

Project description:This SuperSeries is composed of the SubSeries listed below.

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Expression data from HT-1080 cells incubated or not in the presence of laminin111 coiled-coiled recombinant fragment (rLCC111)

Project description:Laminins are large heterotrimeric cross-shaped extracellular matrix (ECM) glycoproteins with terminal globular domains and a coiled-coil region. We have produced for the first time a recombinant laminin coiled-coil domain and studied the transcriptional profile of cells incubated in coiled-coil-coated wells. Cells were incubated in 24w plates, onto coiled-coil-coated wells or control BSA-coated wells (one each), 24h

2011-10-11 | E-GEOD-32896 | biostudies-arrayexpress

Expression data from HT-1080 cells incubated or not in the presence of laminin111 coiled-coiled recombinant fragment (rLCC111)

2011-10-12 | GSE32896 | GEO

A 36-base hairpin within lncRNA DRAIC interacts with the IKKα coiled-coil domain, weakening the IKK complex and inhibiting NF-kappaB activation

Project description:Long noncoding RNAs have diverse functions, but not enough is known about the molecular mechanisms underlying their cellular functions. The 1.7 kb long down-regulated non-coding RNA in cancers (DRAIC) slows tumor growth and inhibits the activation of the transcription factor NF-kappaB through interactions with IKK subunits. Starting with SHAPE-MaP-based structure-function studies of DRAIC we have now identified the minimal regions of DRAIC and IKK involved in the interactions and the anti-cancer function of DRAIC. A hairpin structure comprised of bases 705-722/741-758 (referred to as A+B) within DRAIC is responsible for inhibiting NF-kappaB activity. A+B binds specifically with the IKKα coiled-coil domain with a KD of ~1-5 nM. The coiled-coil domain of IKKα (the kinase subunit) and NEMO (the substrate recognition subunit,) mediate the dimerization of the subunits in the functional kinase complex. Consistent with its interaction with the coiled-coil domain of IKKα, A+B weakens the interaction between NEMO and the IKKα coiled-coil domain in an in vitro complex formation assay. The 36 nt A+B RNA was sufficient and necessary for DRAIC to inhibit tumor cell migration, invasion, and clonal growth in multiple cancer cell-lines. Therefore, this minimal hairpin fragment of the growth-suppressive DRAIC lncRNA inhibits NF-kappaB activation by interacting with high affinity with the coiled-coil domain of IKKα, weakening the interaction between the kinase subunit and the substrate recognition subunit of IKK, thereby inhibiting IB phosphorylation and NF-kappaB activation, and suppressing tumor phenotypes.

2025-07-01 | GSE279192 | GEO

Effects of depletion of Rho-associated, coiled-coil-containing protein kinase 2 in the kidney medullary tussue of murine model.

Project description:Rho and its effector Rho-associated, coiled-coil–containing protein kinase 2 (ROCK2) play crucial roles in a variety of cellular functions, such as cell adhesion and cytoskeletal rearrangement . We here investigated the role of ROCK2 in the kidney medullary tissue using tubular specific ROCK2 knockout mice.

2024-07-01 | GSE246069 | GEO

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