Ask about this productRelated genes to: NUP153 antibody
- Gene:
- NUP153 NIH gene
- Name:
- nucleoporin 153
- Previous symbol:
- -
- Synonyms:
- HNUP153
- Chromosome:
- 6p22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-11
- Date modifiied:
- 2016-06-01
Related products to: NUP153 antibody
Related articles to: NUP153 antibody
- Before entering the nucleus, the HIV capsid core [composed of capsid (CA) proteins] must translocate through the Nuclear Pore Complex (NPC). This process relies on direct interactions between CA and the phenylalanine-glycine (FG) repeats in nucleoporins (NUPs) within the NPC. FG repeats are generally classified into three canonical motifs: FG, GLFG, and FxFG, which are differentially distributed along the NPC axis: FG and FxFG motifs are predominantly at the cytoplasmic periphery and in the nuclear basket, whereas GLFG motifs are primarily in the central channel of the NPC. We demonstrate that the capsid engages the diverse FG repeats with markedly different affinities. Notably, GLFGs of NUP98 located in the central channel display significantly increased affinity to CA than conventional FGs/FxFGs. NUP153, which is located at the nuclear basket, contains an atypical FxFG that is adjacent to a PSGV sequence, thus forming additional favorable interactions. We designate this nonconventional FxFG motif as an "FG super-motif." In addition, the C-terminus of NUP153 also contains a cluster of basic residues that serve as an enhancer of the NUP153 FG super-motif, dramatically increasing CA affinity by ~1,000-fold. Other binding enhancers for FG motifs were also identified in NUP58 and POM121 that are in the central channel and its nuclear boundary, respectively. Affinities of NUP58, POM121, and NUP153 enhancers to CA increase with proximity to the nuclear basket. Thus, we propose that the diverse FG repeats and their binding enhancers create an affinity gradient that potentiates HIV capsid translocation through the NPC. - Source: PubMed
Publication date: 2026/07/07
Melčák IvoSlack Ryan LLorson Zachary CEmanuelli Castaner AndresAmbrus KrisztinaWinkjer Jonathan SKirby Karen ADick Robert ASarafianos Stefan G - The nuclear envelope (NE) undergoes dynamic remodeling during both physiological and pathological processes. Nuclei in cells from people with accelerated aging diseases and from older individuals are often lobular and convoluted. Despite extensive study, the steps of phenotype acquisition and the co-factors required are not yet fully understood. Here, we focused on progerin, a variant form of lamin A that causes Hutchinson-Gilford progeria syndrome (HGPS). Using an inducible cell-based system, we characterized two distinct stages of NE remodeling. Correlative light and electron microscopy of interphase-arrested cells showed that prior to cell division, progerin primarily affects the inner nuclear membrane (INM), inducing focal expansion, invagination and the formation of multi-membranous structures, whereas the outer nuclear membrane remains largely unaffected. These focal regions of progerin accumulation are enriched for specific INM proteins and the nucleoporin NUP153 but largely exclude nuclear pore complexes. Live and fixed image analysis demonstrated that, upon cell division and NE reassembly, progerin-expressing cells develop pronounced nuclear lobulations characteristic of HGPS. Appreciation of this stepwise development of phenotype lends insight into cellular manifestations of aging in mitotic versus post-mitotic cell types and provides a system in which to study factors that contribute to these distinct stages in the disruption of nuclear morphology. Depletion of NUP153 reduced NE foci formation in interphase-arrested cells expressing GFP-progerin, suggesting that NUP153 promotes or stabilizes INM invagination. Aberrant nuclear architecture is just one cellular feature that changes during normal and accelerated aging, but its etiology provides a crucial framework for understanding accompanying consequences on chromatin packaging, DNA damage and the endoplasmic reticulum stress response. - Source: PubMed
Publication date: 2026/06/19
Turkmen Ayse MubineWang JingFrost AdamUllman Katharine S - The HIV-1 capsid (CA) is a validated antiviral target that plays critical roles in both the early and late stages of the viral life cycle. Using structure-based strategy, we designed and synthesized a series of phenylalanine derivatives containing a 4-quinazolinone scaffold as novel HIV-1 CA inhibitors. Among them, exhibited potent antiviral activity in MT-4 cells against HIV-1 NL4-3 (EC = 0.65 ± 0.27 nM) and effectively protected cells from HIV-1 IIIB infection. SPR revealed that interacts strongly with CA hexamers ( = 2.7 ± 0.5 nM) with an extended residence time and competes with host factors CPSF6 and NUP153, disrupting CA assembly and disassembly. retained activity against lenacapavir (LEN)-resistant strains, such as N74D (11-fold shift vs. 20-fold for LEN). Crystallographic analysis revealed that binds at the CA NTD-CTD interface and forms hydrogen bonds with Thr107 and Ser41 (NTD-NTD interface). Pharmacological evaluation demonstrated favorable properties, including good plasma stability, low toxicity (SI > 1571), and suitable pharmacokinetics with a prolonged half-life following subcutaneous administration ( = 19.9 h). Overall, this study identifies 4-quinazolinone-based phenylalanine derivatives as promising HIV-1 CA inhibitors and highlights as a potential long-acting therapeutic candidate for HIV-1 treatment. - Source: PubMed
Publication date: 2026/05/03
Zhang XujieSun LinWalsham LauraMa YuexiDing DangWang MeiZhao FabaoZhang JianWang ZhaoXu ShujingJiang XiangyiZhou YangDe Clercq ErikPannecouque ChristopheChen Chin-HoGoldstone David CLiu XinyongDick AlexejZhan Peng - Orthoflaviviruses are RNA viruses that cause serious diseases in humans, with currently no antivirals available. Targeting host factors is emerging as an attractive antiviral approach. However, as a first step, there is a need to understand which host proteins are hijacked and for what purpose. Here, using a combination of fluorescence microscopy, knock-down, crosslinking immunoprecipitation sequencing, mass spectrometry, and in vitro and biophysical assays, we identify nucleoporin-153 (NUP153) as a proviral factor during orthoflavivirus infection. We show that NUP153 is recruited to the virus amplification site on the endoplasmic reticulum to impact the structural to nonstructural viral protein ratios. We find that NUP153 interacts with both the viral proteins NS3 and NS5, and a highly conserved G-rich motif on the viral RNA. These interactions specifically promote the production of viral structural proteins, leading to an efficient virion assembly, virus release and spread to new cells. We propose that NUP153 acts as a key regulator in viral protein ratios, a mechanism that appears conserved among orthoflaviviruses. - Source: PubMed
Publication date: 2026/04/08
Peters Marie B ALindqvist RichardKassa EszterYau Wai-LokSengupta PallabiNiedermoser IsabellGerold GisaSabouri NasimIvarsson YlvaLundmark RichardÖverby Anna K - High-grade serous ovarian carcinoma (HGSOC) remains the most lethal gynecologic malignancy, with platinum resistance posing the major therapeutic barrier. Malignant ascites, a hallmark of advanced HGSOC, correlates with chemoresistance and poor prognosis, yet the contribution of ascites circRNAs in this process remains obscure. Here, we identify ASCOR, a circRNA upregulated in ascites small extracellular vesicles (sEVs) from platinum-resistant HGSOC patients, predicts poor survival. ASCOR promotes platinum resistance in vitro and in vivo by enhancing cell viability, reducing apoptosis, and alleviating DNA damage, with effects also transferred via sEVs. Mechanistically, ASCOR binds RPA1 and facilitates its NUP153-dependent nuclear translocation, which recruits the RNA helicase DDX18, suppressing R-loop formation. Meanwhile, the ASCOR-RPA1-DDX18 axis activates PI3K/Akt signaling to promote platinum resistance. Targeting ASCOR with antisense oligonucleotides reverses chemoresistance in mouse models. Our study unveils an ascites circRNA-driven pathway underlying platinum resistance in HGSOC, suggesting targeting ASCOR is a promising strategy for HGSOC treatment. - Source: PubMed
Publication date: 2026/02/12
Liu HanyuanZhu ChenchenYao XuelinLiu YiZhu JingLi YueboXu HanjiePeng ChengShan GeChen LiangZhou Ying