LUZP1 antibody
- Known as:
- LUZP1 (anti-)
- Catalog number:
- orb35009
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- LUZP1 antibody
Related genes to: LUZP1 antibody
- Gene:
- LUZP1 NIH gene
- Name:
- leucine zipper protein 1
- Previous symbol:
- -
- Synonyms:
- LUZP
- Chromosome:
- 1p36.12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-27
- Date modifiied:
- 2016-10-05
Related products to: LUZP1 antibody
Related articles to: LUZP1 antibody
- Head and neck squamous cell carcinoma (HNSCC) remains a highly aggressive malignancy with poor prognosis driven by metastasis and therapeutic resistance. Through comparative proteomic profiling of tumor specimens from patients with long‑ and short‑term survival, the present study identified leucine zipper protein 1 (LUZP1) as one of the most upregulated proteins in tumors from short‑term survivors. Functional assays revealed that LUZP1 knockdown impaired migration, invasion, invadopodia formation and epithelial‑mesenchymal transition, while enhancing sensitivity to docetaxel and cisplatin. Analysis of paired primary and metastatic tumors further confirmed elevated LUZP1 expression in metastatic sites. Mechanistically, NF‑κB inhibition markedly reduced LUZP1 expression, whereas stimulation with IL‑1β or TNF‑α induced its upregulation and rescued the migration defect caused by LUZP1 depletion, implicating NF‑κB as a key upstream regulator. Immunohistochemical analysis of clinical samples demonstrated that high LUZP1 expression was associated with shorter overall and progression‑free survival. Collectively, these findings identify LUZP1 as a novel NF‑κB‑regulated effector that promotes metastasis and chemoresistance and highlight its potential as a prognostic biomarker and therapeutic target in HNSCC. - Source: PubMed
Publication date: 2026/04/09
Lin Chen-YuanHsieh Ching-YunLan Hsin-ChiLin Ching-ChanChen Tzu-TingTseng Wei-ChiTsou Yung-AnChang Wei-Chao - Colorectal cancer liver metastasis (CRLM) and chemotherapy resistance remain major clinical challenges, with the underlying molecular mechanisms yet to be fully elucidated. In this study, based on analyses of five initial clinical cohorts from FUSCC, the E3 ubiquitin ligase COP1 was identified as a critical driver of CRLM and resistance to oxaliplatin-based chemotherapy. Using an organoid biobank derived from paired primary colorectal tumors and liver metastases, integrated multi-omics analyses (WES, bulk RNA-seq, scRNA-seq) of patient-derived organoids (PDOs) from CRLM revealed significantly elevated COP1 expression in liver metastases compared to primary tumors. High COP1 levels were associated with poor prognosis, increased liver metastatic burden, and resistance to oxaliplatin-based chemotherapy. In vitro and in vivo functional experiments demonstrated that COP1 facilitates CRLM progression by ubiquitinating and degrading LUZP1, thereby releasing DAPK3 from LUZP1-mediated suppression. This process leads to enhanced MYL9 phosphorylation and activation of epithelial-mesenchymal transition (EMT) as well as the JAK2-STAT3-CCND2 signaling axis-pathways crucial for liver metastasis and resistance to oxaliplatin-based chemotherapy. These findings establish the COP1-LUZP1-MYL9 axis as a therapeutic target for CRLM and oxaliplatin-based chemoresistance. Clinically, COP1 expression profiling in PDOs from postoperative specimens enables a precision strategy for managing oxaliplatin-based chemoresistance, especially in the context of FOLFOX. - Source: PubMed
Publication date: 2026/04/05
Zhang RuijiaLuo WenqinZhou QikaiLiang DongguoHao YuankaiChen FanQiu YulinCao YixianShan ZezhiZhang YuLi QingguoCai SanjunLuo DakuiMo ShaoboMa BinLi Xinxiang - Dysfunction at the centrosome-cilium interface underlies a broad range of ciliopathies. Here, we identify biallelic variants in , encoding a centrosomal protein, in eight unrelated individuals presenting with neurodevelopmental, ocular, and variable additional multisystem features. Proband-derived fibroblasts and CEP76-depleted RPE1 cells display ciliary deficits, including impaired cilium formation and length, disrupted transition zone architecture, and impaired IFT88-mediated anterograde intraflagellar transport. Zebrafish mutants recapitulate key clinical phenotypes, and in vitro complementation assays confirm pathogenicity for all tested human disease-associated variants. Proteomics analysis identifies CEP76 interactors, including known partners CCP110 and CEP97, and highlights clinically and functionally relevant candidates, including ALMS1 and LUZP1. Together, these findings expand the role of CEP76 beyond centriole duplication to include ciliary assembly and trafficking, establishing it as a ciliopathy gene. This work provides mechanistic insights into -related disease and broadens our understanding of centrosome-cilium biology. - Source: PubMed
Publication date: 2025/10/17
Khan KamalTavares ErikaBishara KatherineOzanturk AysegulQebibo LeilaFrangakis StephanCalame Daniel GMeunier IsabelleBocquet BéatricePloski RafalAl Khateeb Mohammad AymanMarafi DanaMansard LukeDamaj LenaLewis Richard AUllah FaridArbogast ThomasOgden Jackson PHarion MadeleineWillems MarjolaineZaki Maha SBartolomaeus TobiasRoux Anne-FrançoiseLupski James RRydzanicz MalgorzataJamra Rami AbouRamond FrancisHeon EliseBurglen LydieDavis Erica E - Animal cells adapt to the stiffness of their environment through mechanotransduction, a process in which mechanical signals are converted into biochemical responses, influencing key cellular processes such as growth and differentiation. We identified ubiquitin-conjugating enzymes E2 A and B (UBE2A/B) as mechanosensitive proteins that translocate between the nucleus and cytoplasm depending on force and substrate stiffness. Here, we hypothesized that UBE2A/B nuclear translocation on stiff substrates triggers gene expression via UBE2A/B-mediated ubiquitination of histone H2B lysine 120 (H2BK120). Chromatin immunoprecipitation sequencing (ChIP-seq) revealed distinct DNA fragments bound to monoubiquitinated H2B in cells cultured on soft (0.2 kPa) versus stiff (64 kPa) substrates. We identified 2245 gene regions binding to ubiquitinated histones on stiff substrates and 294 on soft substrates and further integrated RNA-seq and UBE2A/B knockdown data to pinpoint 179 stiff-specific and 18 soft-specific genes. Among these, filamin C (FLNC), leucine zipper protein 1 (LUZP1), and glutamate-rich WD repeat-containing protein 1 (GRWD1) showed higher expression on stiff substrates, with GRWD1 known for its role in cancer progression through cell cycle and gene regulation. These findings highlight how substrate stiffness modulates gene expression via UBE2A/B-mediated H2B ubiquitination. - Source: PubMed
Publication date: 2025/04/09
Feng MingweiNakamura Fumihiko - Leucine zipper protein 1 (LUZP1) functions in the maintenance and dynamics of the cytoskeleton by interacting with actin and microtubules. Deficiency or mutation of LUZP1 is associated with brain developmental disorders; however, its precise role in brain function remains unclear. We showed that LUZP1 localizes to actin and is highly expressed in CaMKIIα-expressing neurons within the mouse hippocampal dentate gyrus. Depletion of LUZP1 impedes dendritic spine maturation, which is characterized by excess immature filopodia and loss of mature mushroom spines both in vitro and in vivo. LUZP1 knockdown reduces spontaneous electrical activity and synaptic plasticity in hippocampal neurons. Conditional deletion of LUZP1 in CaMKIIα-expressing neurons causes impaired learning and memory behavior in mice of both sexes. Mechanistically, LUZP1 control dendritic maturation by directly interacting with filamin A and modulating the Rac1-PAK1 signaling pathway. These findings shed light on the role of LUZP1 in regulating synaptic plasticity and brain function. - Source: PubMed
Publication date: 2025/05/14
Wang XiaojieWang LiangBu QianXiao YuzhouZhao YueJiang LinhongDai YanpingLi HongchunLiu HaxiaoyuChen YaxingFlores Angelo DZhao YinglanCen Xiaobo