Ask about this productRelated genes to: KPNB1 antibody
- Gene:
- KPNB1 NIH gene
- Name:
- karyopherin subunit beta 1
- Previous symbol:
- -
- Synonyms:
- NTF97, IPOB, MGC2155, MGC2156, MGC2157, IMB1, Impnb, IPO1
- Chromosome:
- 17q21.32
- Locus Type:
- gene with protein product
- Date approved:
- 1997-04-21
- Date modifiied:
- 2016-02-01
Related products to: KPNB1 antibody
Related articles to: KPNB1 antibody
- As a frequently occurring malignant disorder in women, breast cancer (BC) is closely associated with circular RNAs (circRNAs) in mediating its pathological progression. Accumulating evidence suggests that hsa_circ_0001588 promotes BC via microRNA (miRNA) sponging. - Source: PubMed
Publication date: 2026/04/06
Wu WeiGao ZichenGao SijingBian YanZhong DengyuanMao Xiaoyun - Acute myeloid leukemia (AML) is a highly heterogeneous hematologic malignancy, with its pathogenesis closely associated with cellular states at various stages of differentiation. Existing clinical prognostic models often fail to account for this heterogeneity and lack integration of key molecular pathways. This study aimed to characterize AML differentiation-associated heterogeneity at the single-cell level, investigate the role of UNC13D in immune and dedifferentiation states, and develop a prognostic model integrating these features. - Source: PubMed
Publication date: 2026/02/25
Wang ZiqianZhou Daobin - Androgen deprivation and androgen receptor (AR) antagonists are essential treatments for prostate cancers in the clinic. However, after an initially effective response, most tumors become resistant to androgen deprivation therapies. Resistance often arises from AR mutations, resulting in ligand-independent activation and nuclear translocation of AR. - Source: PubMed
Publication date: 2026/02/25
Wang XuanXu XinFang ShengyunShi XiaoleiYang Yili - Nuclear protein homeostasis, including transcription factor turnover, critically depends on the nuclear proteasomes that must be imported after cell division. This dynamic process requires AKIRIN2, a small unstructured protein whose mechanistic role has remained elusive despite its essential function. Using an integrated approach combining protein-wide saturation mutagenesis screens, cryo-EM, and biochemical reconstitution, we characterize AKIRIN2 as a scaffold protein that coordinates the assembly of an importin cluster around the proteasome. AKIRIN2 binds in multiple copies to the 20S proteasome and simultaneously interacts with importin IPO9 and the KPNA2/KPNB1 heterodimer. In the nucleus, RanGTP triggers importin dissociation, releasing the proteasome, while AKIRIN2 undergoes ubiquitin-independent degradation. Our findings reveal how AKIRIN2's multivalency facilitates the recruitment of multiple importins to the proteasome, a critical adaptation for transporting this large macromolecular complex into the nucleus and maintaining the nuclear proteome. - Source: PubMed
Publication date: 2026/02/04
Brunner Hanna LKalis Robert WGrundmann LorenzHodáková ZuzanaKoskova ZuzanaGrishkovskaya Irinade Almeida MelanieHinterndorfer MatthiasKnaudt HannahHöfflin SimonAndersch FlorianKotisch HaraldDickmanns AchimCuylen-Haering SaraZuber JohannesHaselbach David - Neuronal cytoplasmic aggregation and nuclear depletion of the TAR DNA-binding protein 43 (TDP-43) is the most characteristic pathology of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), causing toxicity through cytoplasmic gain and nuclear loss of function mechanisms. In addition to its canonical role in nuclear cytoplasmic transport (NCT), the nuclear import receptor, importin-β1 (KPNB1) also acts as a molecular chaperone capable of preventing and reversing aberrant protein aggregation. Previous studies have demonstrated that increased expression of KPNB1 solubilizes TDP-43 aggregates and restores its nuclear localization. Here, we identify JRMS, a small molecule that enhances the chaperone activity of KPNB1 by increasing its cytoplasmic availability. JRMS treatment reduced cytoplasmic aggregation and promoted nuclear localization of full-length and pathological truncated TDP-43 variants across multiple experimental systems, including cell lines, primary neurons, iPSC-derived cortical neurons, organotypic brain slices and in vivo model. The effects of JRMS were KPNB1 dependent and occurred without inducing cytotoxicity or perturbing basal NCT. These findings identify JRMS as a promising therapeutic strategy for targeting TDP-43 pathology in ALS/FTD and other related TDP-43 proteinopathies. - Source: PubMed
Publication date: 2026/01/17
Shenouda MarcShenouda SandraKartono BryanEid ShehabCheng CherylRobertson Janice