CCNYL1 antibody
- Known as:
- CCNYL1 (anti-)
- Catalog number:
- orb101800
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- CCNYL1 antibody
Related genes to: CCNYL1 antibody
- Gene:
- CCNYL1 NIH gene
- Name:
- cyclin Y like 1
- Previous symbol:
- -
- Synonyms:
- FLJ40432
- Chromosome:
- 2q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 2007-02-09
- Date modifiied:
- 2015-11-12
Related products to: CCNYL1 antibody
Related articles to: CCNYL1 antibody
- Cyclin-dependent kinase 17 (CDK17) is an understudied member of the PCTAIRE family of CDKs, with phosphorylation-guided molecular mechanism being underexplored. In this study, an in-depth mass spectrometry-based phosphoproteomics data integration and harmonization, coupled with replicable statistical analysis, was performed to understand the phosphorylation landscape of CDK17. High-confidence phosphorylation sites of CDK17 were derived from 711 phosphoproteomics profiling studies, where 176 datasets showed differential phosphorylation of CDK17. Among 13 identified phosphorylation sites of CDK17, S180, S137, and S146 were prominently detected in 75% of all the datasets. Notably, sequence conservation of CDK17 (S146, S137, and S180) with CDK16 (S119, S110, and S153) and CDK18 (S98, S89, and S132), respectively, was observed, where CDK16 (S119) is a part of the binding motif for multiple upstream kinases, 14-3-3 protein, and CCNYL1. Furthermore, conserved co-regulatory patterns of other proteins were identified as compared with CDK17 phosphorylation, which revealed 19 upstream kinases, 164 downstream substrates, and several interactors of CDK17, which conserved co-regulatory patterns across diverse biological contexts. Statistical analysis revealed phosphoregulation of CDK17 through other kinases, regulation of CDK17 substrates, protein-protein interactions, and conserved co-differential regulation in multiple datasets. Specifically, this analysis derived through global data integration with a replicable analytical framework lays a groundwork for experimental validation of CDK17 phosphorylation in its functional regulation. - Source: PubMed
Publication date: 2026/03/18
Bangera AshikaLubaba FathimathulPerunelly Gopalakrishnan AthiraShivamurthy Prathik BasthikoppaRaju RajeshRamesh Poornima - Histone deacetylase inhibitors (HDACis) induce cell death in many chemoresistant cancer models, suggesting their potential as alternative treatments for these malignancies. However, their efficacy in solid tumors remains limited. Therefore, understanding the molecular mechanisms underlying HDACi-induced cell death is essential for developing targeted activators of these pathways, enabling the selective elimination of chemoresistant cancer cells while minimizing the widespread transcriptional effects of HDACis. In this study, we investigated HDACi-induced cell death across models of different cellular origins to determine whether a universal molecular mechanism triggers this process. Our findings demonstrate that HDACi-induced cell death is TP53-independent, resistant to caspase inhibitors, and sensitive to serine protease inhibitors. This form of cell death requires intracellular calcium mobilization to induce mitochondrial depolarization. Using DNA arrays, apoptosis protein arrays, and ELISA assays, combined with siRNA-mediated gene silencing, we identified genes with a causal relationship to TSA-induced cell death. These include dual-specificity phosphatases such as DUSP3 and DUSP10; endoplasmic reticulum stress-related genes such as XBP1, MBTPS1, MBTPS2, and RPS6KA5; and other genes like BAX, AIF, EAF2, NANOS1, and CCNYL1. Our findings reveal novel potential targets for developing antineoplastic agents designed to exploit HDACi-induced cell death pathways, providing a strategy to overcome chemoresistance in cancer therapy. - Source: PubMed
Publication date: 2025/09/12
Fuentes-Baile MaríaGarcía-Morales PilarPérez-Valenciano ElizabethMata-Balaguer TrinidadMenéndez-Gutiérrez María Pde Juan Romero CaminoRodríguez-Lescure ÁlvaroMartín-Orozco ElenaMallavia RicardoBarberá Víctor MSaceda Miguel - The function of dopamine receptor D2 (D2R) is well associated with sperm motility; however, the physiological role of D2R present on testicular cells remains elusive. The aim of the present study is to delineate the function of testicular D2R. Serum dopamine levels were found to decrease with age, whereas testicular D2R expression increased. In rat testicular sections, D2R immunolabeling was observed in interstitial cells, spermatogonia, spermatocytes and mature elongated spermatids, whereas tyrosine hydroxylase immunolabeling was selectively detected in Leydig cells. In vitro seminiferous tubule culture following bromocriptine (D2R agonist) treatment resulted in decreased cAMP levels. Microarray identified 1077 differentially expressed genes (511 up-regulated, 566 down-regulated). The majority of differentially expressed genes were present in post-meiotic cells including early and late spermatids, and sperm. Gene ontology elucidated processes related to extra-cellular matrix to be enriched and was supported by differential expression of various collagens and laminins, thereby indicating a role of dopamine in extra-cellular matrix integrity and transport of spermatids across the seminiferous epithelium. Gene ontology and enrichment map also highlighted cell/sperm motility to be significantly enriched. Therefore, genes involved in sperm motility functions were further validated by RT-qPCR. Seven genes (Akap4, Ccnyl1, Iqcf1, Klc3, Prss55, Tbc1d21, Tl18) were significantly up-regulated, whereas four genes (Dnah1, Dnah5, Clxn, Fsip2) were significantly down-regulated by bromocriptine treatment. The bromocriptine-stimulated reduction in seminiferous tubule cyclic AMP and associated changes in spermatid gene expression suggests that dopamine regulates both spermatogenesis and spermiogenesis within the seminiferous epithelium, and spermatozoa motility following spermiation, as essential processes for fertility. - Source: PubMed
Raut SanketaKhambata KushaanSingh DiptyBalasinor Nafisa H - Congenital hypothyroidism due to thyroid dysgenesis (TD), presented as thyroid aplasia, hypoplasia or ectopia, is one of the most prevalent rare diseases with an isolated organ malformation. The pathogenesis of TD is largely unknown, although a genetic predisposition has been suggested. We performed a genome-wide association study (GWAS) with 142 Japanese TD cases and 8380 controls and found a significant locus at 2q33.3 (top single nucleotide polymorphism, rs9789446: P = 4.4 × 10-12), which was replicated in a German patient cohort (P = 0.0056). A subgroup analysis showed that rs9789446 confers a risk for thyroid aplasia (per allele odds ratio = 3.17) and ectopia (3.12) but not for hypoplasia. Comprehensive epigenomic characterization of the 72-kb disease-associated region revealed that it was enriched for active enhancer signatures in human thyroid. Analysis of chromosome conformation capture data showed long-range chromatin interactions of this region with promoters of two genes, FZD5 and CCNYL1, mediating Wnt signaling. Moreover, rs9789446 was found to be a thyroid-specific quantitative trait locus, adding further evidence for a cis-regulatory function of this region in thyroid tissue. Specifically, because the risk rs9789446 allele is associated with increased thyroidal expression of FDZ5 and CCNYL1 and given the recent demonstration of perturbed early thyroid development following overactivation of Wnt signaling in zebrafish embryos, an enhanced Wnt signaling in risk allele carriers provides a biologically plausible TD mechanism. In conclusion, our work found the first risk locus for TD, exemplifying that in rare diseases with relatively low biological complexity, GWAS may provide mechanistic insights even with a small sample size. - Source: PubMed
Narumi SatoshiOpitz RobertNagasaki KeisukeMuroya KojiAsakura YumiAdachi MasanoriAbe KiyomiSugisawa ChihoKühnen PeterIshii TomohiroNöthen Markus MKrude HeikoHasegawa Tomonobu - The role of WNT/β-catenin signalling in mouse neocortex development remains ambiguous. Most studies demonstrate that WNT/β-catenin regulates progenitor self-renewal but others suggest it can also promote differentiation. Here we explore the role of WNT/STOP signalling, which stabilizes proteins during G2/M by inhibiting glycogen synthase kinase (GSK3)-mediated protein degradation. We show that mice mutant for cyclin Y and cyclin Y-like 1 (Ccny/l1), key regulators of WNT/STOP signalling, display reduced neurogenesis in the developing neocortex. Specifically, basal progenitors, which exhibit delayed cell cycle progression, were drastically decreased. Ccny/l1-deficient apical progenitors show reduced asymmetric division due to an increase in apical-basal astral microtubules. We identify the neurogenic transcription factors Sox4 and Sox11 as direct GSK3 targets that are stabilized by WNT/STOP signalling in basal progenitors during mitosis and that promote neuron generation. Our work reveals that WNT/STOP signalling drives cortical neurogenesis and identifies mitosis as a critical phase for neural progenitor fate. - Source: PubMed
Publication date: 2021/08/25
Da Silva FabioZhang KaiqingPinson AnnelineFatti EdoardoWilsch-Bräuninger MichaelaHerbst JessicaVidal ValerieSchedl AndreasHuttner Wieland BNiehrs Christof