Ask about this productRelated genes to: ANP32B antibody
- Gene:
- ANP32B NIH gene
- Name:
- acidic nuclear phosphoprotein 32 family member B
- Previous symbol:
- -
- Synonyms:
- SSP29, PHAPI2, APRIL
- Chromosome:
- 9q22.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-02-13
- Date modifiied:
- 2016-10-05
Related products to: ANP32B antibody
Related articles to: ANP32B antibody
- Triple-negative breast cancer (TNBC) exhibits pronounced intratumoral heterogeneity, and cancer stem cells (CSCs) are thought to play a pivotal role in this process. However, the molecular regulatory mechanisms linking CSC-associated stemness features to tumor progression remain insufficiently elucidated. - Source: PubMed
Publication date: 2026/03/23
Huo ZhenzhongSun WeiboLou ChunYang Tiansong - Alcohol consumption can have harmful effects on health, depending on the quantity and frequency. Understanding the underlying molecular mechanisms is essential to grasp its health consequences. The study aimed to assess the association between alcohol consumption and blood DNA methylation, an epigenetic mechanism that controls gene expression. - Source: PubMed
Publication date: 2025/07/07
Dragic DzevkaArtaud FannyKarimi MojganTruong ThérèseBaglietto LauraDeleuze Jean-FrançoisDiorio CarolineSeveri Gianluca - Bourbon virus (BRBV) is a tick-borne virus in the genus in the family. BRBV was initially identified as the presumptive causative agent of a fatal human infection in 2014 and has since been identified in ticks in the Midwest, Northeast, and Southern United States, with occasional spillovers into humans. However, little is known about how virus-host interactions impact their large host range. Here, we show that BRBV polymerase activity in human cells is completely dependent on cellular ANP32 proteins. BRBV polymerase activity was completely lost in cells lacking ANP32A and ANP32B, resulting in failed infections. BRBV polymerase activity was restored in the presence of ANP32 proteins from diverse hosts. Dhori virus and Thogoto virus, other related members, retained high activity in the absence of ANP32 proteins, showing reduced dependence on these host factors. Interaction studies revealed that the BRBV polymerase trimer binds human ANP32A or ANP32B. Genetic analysis revealed that tick vectors for BRBV encode a single locus corresponding to . Tick produces multiple protein variants through alternative splicing and start-site selection, all of which enhance polymerase activity for . Unexpectedly, the BRBV polymerase was highly sensitive to changes at the N-terminus of ANP32, while it was insensitive to changes in the body of ANP32 that restrict the activity of influenza virus polymerases. Thus, ANP32A is a deeply conserved pro-viral cofactor, and show remarkable plasticity utilizing ANP32 homologs from different hosts separated by almost 1 billion years of evolution.IMPORTANCEViral polymerases rely on cellular cofactors to support efficient transcription of viral genes and replication of the viral genome. The RNA-dependent RNA polymerase of influenza virus, an orthomyxovirus, requires the cellular ANP32A or ANP32B proteins for genome replication. However, little is known about whether ANP32 proteins are required by other orthomyxovirus family members, like the tick-borne thogotoviruses. We show that thogotoviruses use ANP32 proteins from diverse hosts to enhance polymerase activity, including that encoded by the single gene found in ticks. However, thogotovirus polymerase showed varying levels of dependence on ANP32 proteins, with some polymerases functioning at near full activity even in the absence of ANP32 proteins. Thus, ANP32 proteins are deeply conserved viral cofactors, with each virus displaying distinct patterns of ANP32 usage and requirements for function. - Source: PubMed
Publication date: 2025/05/14
Zhang ZhenyuAziati Ishmael DNipper ThomasBoon Adrianus C MMehle Andrew - Gene duplication has allowed protein evolution toward novel functions and mechanisms. The differences between paralogous genes frequently rely on the sequence of disordered regions. For instance, in mammals, the chaperones ANP32A and ANP32B share a common evolutionary line and have some exchangeable functions based on their similar N-terminal domains. Nevertheless, their C-terminal low-complexity-acidic-regions (LCARs) display substantial sequence differences, unveiling some degree of variability between them, in agreement with their different tissue-specific expression patterns. These structural and computational results indicate that a substitution in the vicinity of the nuclear localization signal (NLS), of Pro in ANP32A for Thr in ANP32B, determines the overall compactness of the C-terminal LCAR. The different structural properties of the disordered region affect the binding mode of ANP32 members to their targets. This type of divergent binding mode is exemplified with the extra-mitochondrial cytochrome c (Cc), a well-known ANP32B partner and which now determine also binds to ANP32A; and with the RNA binding protein HuR, whose export to the cytoplasm is mediated by ANP32 proteins under stress. Therefore, differential expression patterns of ANP32A or ANP32B may affect the regulation of Cc and HuR and can help to explain the distinct roles of these proteins in diseases. - Source: PubMed
Publication date: 2025/01/31
Baños-Jaime BlancaUceda-Mayo Ana BRivero-Rodríguez FranciscoCasado-Combreras Miguel ÁVelázquez-Cruz AlejandroVelázquez-Campoy AdriánCorrales-Guerrero LauraDe la Rosa Miguel ADíaz-Moreno Irene - Human ANP32A/B (huANP32A/B) poorly support the polymerase activity of avian influenza viruses (AIVs), thereby limiting interspecies transmission of AIVs from birds to humans. The SUMO-interacting motif (SIM) within NS2 promotes the adaptation of AIV polymerase to huANP32A/B via a yet undisclosed mechanism. Here we show that huANP32A/B are SUMOylated by the E3 SUMO ligase PIAS2α, and deSUMOylated by SENP1. SUMO modification of huANP32A/B results in the recruitment of NS2, thereby facilitating huANP32A/B-supported AIV polymerase activity. Such a SUMO-dependent recruitment of NS2 is mediated by its association with huANP32A/B via the SIM-SUMO interaction module, where K68/K153-SUMO in huANP32A or K68/K116-SUMO in huANP32B interacts with the NS2-SIM. The SIM-SUMO-mediated interactions between NS2 and huANP32A/B function to promote AIV polymerase activity by positively regulating AIV vRNP-huANP32A/B interactions and AIV vRNP assembly. Our study offers insights into the mechanism of NS2-SIM in facilitating AIVs adaptation to mammals. - Source: PubMed
Publication date: 2024/12/30
Sun LiukeGuo XingYu MengmengWang Xue-FengRen HuilingWang Xiaojun