Ask about this productRelated genes to: ANP32A Blocking Peptide
- Gene:
- ANP32A NIH gene
- Name:
- acidic nuclear phosphoprotein 32 family member A
- Previous symbol:
- C15orf1
- Synonyms:
- LANP, PP32, I1PP2A, PHAPI, MAPM, mapmodulin
- Chromosome:
- 15q23
- Locus Type:
- gene with protein product
- Date approved:
- 2002-02-13
- Date modifiied:
- 2015-11-05
Related products to: ANP32A Blocking Peptide
Related articles to: ANP32A Blocking Peptide
- Glioblastomas (GBMs) exhibit constitutive activation of oncogenic kinase signaling pathways, contributing to tumor aggressiveness and resistance to therapy. Kinase inhibitors have demonstrated limited efficacy against GBMs, primarily due to the tumors' ability to adapt to diverse stimuli and effectively rewiring critical downstream signaling networks. This remarkable adaptability underscores the pressing need for novel therapeutic strategies that sustain the inhibition of oncogenic kinase signaling in GBM. This study sought to elucidate the mechanisms by which GBMs maintain the constitutive activation of oncogenic kinase signaling under the surveillance of intact tumor suppressor protein phosphatase 2A (PP2A). We identify that GBMs inhibit PP2A activity through overexpression of endogenous inhibitors (EIPs), including ANP32A, CIP2A, and SET. Inhibition of these EIPs restores PP2A activity, disrupting oncogenic kinase activation and transcription factor signaling, reducing tumor formation. Furthermore, CRISPR-Cas9 EIP silencing enhances PP2A's ability to target DNA damage response kinases ATR and ATM, sensitizing tumors to radiation by impairing DNA repair and cell cycle checkpoint control. These findings reveal the therapeutic potential of activating PP2A in GBMs, both as a standalone strategy and in combination with radiation. - Source: PubMed
Publication date: 2026/02/20
Jacob John RyanNimjee Shahid MElder J BradleyChakravarti ArnabPalanichamy Kamalakannan - Groundwater contaminated with high fluoride levels poses a global public health concern. While fluoride exposure has been linked to hypertension, the role of genetic polymorphisms in bone metabolism-related genes in modulating this relationship remains unclear. - Source: PubMed
Publication date: 2026/02/17
Gao YueWang QingboYang ShuaifeiWu JunhuaQin MingWang XinLiu XiaonaJiang YutingOgutu JamesGao YanhuiYang Yanmei - In 2024, an unprecedented outbreak of H5N1 high pathogenicity avian influenza was detected in dairy cattle in the USA resulting in spillbacks into poultry, wild birds and other mammals including humans. Here, we present molecular and virological evidence that the cattle B3.13 genotype H5N1 viruses rapidly accumulated adaptations in polymerase genes that enabled better replication in bovine cells and tissues, as well as cells of other mammals including humans. We find evidence of several mammalian adaptations in cattle including PB2 M631L, which is found in all cattle sequences, and PA K497R, which is found in the majority. Structurally, PB2 M631L maps to the polymerase-ANP32 interface, an essential host factor for viral genome replication. We show that this mutation adapts the polymerase to better interact with bovine ANP32 proteins, particularly ANP32A, and thereby enhances virus replication in bovine mammary systems and primary human airway cultures. We show that ongoing evolution in the PB2 gene, including E627K and a convergently arising D740N substitution, further increase polymerase activity and virus replication in a range of mammalian cells. Thus, circulation of H5N1 in dairy cattle allows virus adaption improving replicative ability in cattle and poses a continued risk of zoonotic spillover. - Source: PubMed
Publication date: 2026/01/16
Dholakia VidhiQuantrill Jessica LRichardson Samuel A SPankaew NuntichaBrown Maryn DYang JiayunCapelastegui FernandoMasonou TerezaCase Katie-MarieAjeian JilaWoodall Maximillian N JMagill CallumFreimanis GrahamMcCarron AmyStaller EccoSheppard Carol MBrown Ian HMurcia Pablo RSmith Claire MIqbal MunirDigard PaulBarclay Wendy SPinto Rute MPeacock Thomas PGoldhill Daniel H - Avian influenza virus cross-species infection in humans poses a major threat to global public health. Species-specific differences between avian ANP32A and mammalian ANP32 proteins create a natural barrier against viral cross-species infection by directly impairing the functional interaction between the avian-origin viral RNA polymerase and mammalian ANP32 proteins, thereby restricting viral genome replication. The key to overcoming this barrier lies in the adaptation of viral RNA polymerase to host ANP32 family proteins. This mini-review summarizes the mechanisms and variations in influenza virus adaptation to ANP32 proteins across different species. Influenza viruses adapt to species-specific ANP32 proteins through various mutations and display distinct preferences for specific ANP32 family members within the same host. Additionally, alternative splicing variants of ANP32A within a single species further modulate viral RNA polymerase adaptability. Despite this diversity, the underlying interaction mechanism remains conserved: ANP32-polymerase binding is necessary but not sufficient for optimal polymerase activity. This interaction facilitates the formation of asymmetric polymerase dimers and specifically supports viral genome replication, while the step from cRNA to vRNA remains subject to species-specific restrictions. This explains the classic adaptive mechanism of the PB2 E627K mutation, which restores efficient viral genome replication through acid-base pairing with ANP32A. Furthermore, adaptive mutations in emerging strains such as H3N2 canine influenza virus and recent cases of H5N1 in dairy cows underscore the need for continuous viral surveillance and deeper mechanistic studies on virus-ANP32 interactions. Such research is strategically critical for advancing the One Health approach and mitigating future influenza pandemics. - Source: PubMed
Publication date: 2026/01/05
Bi Zhenwei - Drug resistance is a major challenge for the target therapy of KRAS-mutant non-small cell lung cancer (NSCLC). Here, we observe that ANP32A is tightly associated with KRAS-mutant NSCLC and serves as an unfavorable prognosis factor. ANP32A deficiency impaired cell proliferation, migration, invasion, and cell cycle progression and induced sotorasib (Sot) resistance in KRAS-mutant NSCLC cells, which were reversed by ANP32A reoverexpression in ANP32A-deficient cells. Mechanistically, ANP32A deficiency impaired histone 3 acetylation at lysine 27 (H3K27Ac). Particularly, ANP32A deficiency reduced H3K27Ac of the YEATS4 gene promoter and downregulated YEATS4 expression. ANP32A also interacted with YEATS4 and promoted its binding to H3K27Ac. Furthermore, YEATS4 overexpression partially restored ANP32A deficiency-impaired cell proliferation, H3K27Ac, and Sot sensitivity. Most importantly, trichostatin A mimicked the effect of ANP32A, which restored YEATS4 expression, antagonized Sot resistance, and resensitized ANP32A-deficient cells to Sot in vitro and in vivo, possibly by reactivating the p53 pathway. Our study identifies a new epigenetic mechanism involving the ANP32A that promotes KRAS-mutant lung cancer growth and affects Sot activity. The combination of Sot and histone deacetyltransferase inhibitors could be an effective treatment for KRAS-mutant lung cancer. ANP32A may serve as a biomarker for Sot treatment. - Source: PubMed
Publication date: 2025/12/29
Pan KailingDang MingjingXu BoHuang ZanChen Xianguo