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更新于：2025-05-07

NABP2

更新于：2025-05-07

基本信息

别名

hSSB1、MGC2731、NABP2

+ [10]

简介

Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint (PubMed:25249620). In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways.

关联

项与 NABP2 相关的药物

DKLS02

靶点

NABP2

作用机制

NABP2 inhibitors

在研机构

Princess Alexandra Hospital [+1]

原研机构

Queensland University of Technology [+1]

在研适应症

非小细胞肺癌

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

100 项与 NABP2 相关的临床结果

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100 项与 NABP2 相关的转化医学

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0 项与 NABP2 相关的专利（医药）

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项与 NABP2 相关的文献（医药）

2025-08-01·Cellular Signalling

Decoding the role of nucleic acid binding protein 2 in lipid dysregulation and hepatocellular carcinoma progression through LKB1-mediated mitochondrial dysfunction

Article

作者: Dai, Chengchen ; Zhou, Lihua ; Xu, Nuo ; Liu, Mingyu ; Li, Jinlong ; Chen, Yinqi ; Bian, Saiyan ; Bai, Nan ; Liu, Xiaoquan ; Zheng, Wenjie ; Tong, Yun ; Xu, Banglong ; Zhao, Xuying ; Tang, Zhangzhi ; Lin, Zhaoyi

Nucleic Acid Binding Protein 2 (NABP2), a crucial regulator in the single-stranded DNA-binding protein family, has been linked to the progression of hepatocellular carcinoma (HCC) and poor prognosis. However, the precise mechanisms by which NABP2 regulates HCC development, especially through metabolic pathways, remain unclear. In this study, we evaluated NABP2 expression in clinical HCC samples and analyzed its correlation with patient survival outcomes. Functional assays, including cell proliferation, migration, and lipid metabolism analyses, were performed in vitro and in vivo to investigate the role of NABP2 in tumorigenesis. Additionally, we examined the molecular interactions of NABP2 with the E3 ubiquitin ligase STUB1 and its impact on the LKB1/AMPK signaling pathway. Our results revealed that NABP2 was overexpressed in HCC tissues and associated with worse survival outcomes. NABP2 promoted tumor cell proliferation, migration, and disrupted lipid metabolism. Mechanistically, NABP2 regulated the proteostasis of liver kinase B1 (LKB1) by recruiting STUB1, leading to the inhibition of the LKB1/AMPK signaling axis and mitochondrial dysfunction. In conclusion, our findings suggest that NABP2 may serve as both a biomarker and a potential therapeutic target for HCC, offering novel insights into its role in metabolic reprogramming and tumor progression.

2024-11-27·Nucleic Acids Research

Tetrameric INTS6-SOSS1 complex facilitates DNA:RNA hybrid autoregulation at double-strand breaks

Article

作者: Shiekhattar, Ramin ; Valencia, Monica G ; Stefl, Richard ; Sedova, Katerina ; Dokaneheifard, Sadat ; Gullerova, Monika ; Sebesta, Marek ; Ajit, Kamal ; Beckedorff, Felipe ; Haluza, Vojtech ; Long, Qilin

AbstractDNA double-strand breaks (DSBs) represent a lethal form of DNA damage that can trigger cell death or initiate oncogenesis. The activity of RNA polymerase II (RNAPII) at the break site is required for efficient DSB repair. However, the regulatory mechanisms governing the transcription cycle at DSBs are not well understood. Here, we show that Integrator complex subunit 6 (INTS6) associates with the heterotrimeric sensor of ssDNA (SOSS1) complex (comprising INTS3, INIP and hSSB1) to form the tetrameric SOSS1 complex. INTS6 binds to DNA:RNA hybrids and promotes Protein Phosphatase 2A (PP2A) recruitment to DSBs, facilitating the dephosphorylation of RNAPII. Furthermore, INTS6 prevents the accumulation of damage-associated RNA transcripts (DARTs) and the stabilization of DNA:RNA hybrids at DSB sites. INTS6 interacts with and promotes the recruitment of senataxin (SETX) to DSBs, facilitating the resolution of DNA:RNA hybrids/R-loops. Our results underscore the significance of the tetrameric SOSS1 complex in the autoregulation of DNA:RNA hybrids and efficient DNA repair.

2024-09-01·iScience

Redox-dependent condensation and cytoplasmic granulation by human ssDNA-binding protein-1 delineate roles in oxidative stress response

Article

作者: Jezsó, Bálint ; Szakács, Gergely ; Harami-Papp, Hajnalka ; Kucsma, Nóra ; Kovács, Zoltán J ; Harami, Gábor M ; Pálinkás, János ; Mahmudova, Lamiya ; Kovács, Mihály ; Tóth, Szilárd ; Harami, Gábor M. ; Tárnok, Krisztián ; Kovács, Zoltán J. ; Hegedüs, József

Human single-stranded DNA binding protein 1 (hSSB1/NABP2/OBFC2B) plays central roles in DNA repair. Here, we show that purified hSSB1 undergoes redox-dependent liquid-liquid phase separation (LLPS) in the presence of single-stranded DNA or RNA, features that are distinct from those of LLPS by bacterial SSB. hSSB1 nucleoprotein droplets form under physiological ionic conditions in response to treatment modeling cellular oxidative stress. hSSB1's intrinsically disordered region is indispensable for LLPS, whereas all three cysteine residues of the oligonucleotide/oligosaccharide-binding fold are necessary to maintain redox-sensitive droplet formation. Proteins interacting with hSSB1 show selective enrichment inside hSSB1 droplets, suggesting tight content control and recruitment functions for the condensates. While these features appear instrumental for genome repair, we detected cytoplasmic hSSB1 condensates in various cell lines colocalizing with stress granules upon oxidative stress, implying extranuclear function in cellular stress response. Our results suggest condensation-linked roles for hSSB1, linking genome repair and cytoplasmic defense.

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