APC6 antibody
- Known as:
- APC6 (anti-)
- Catalog number:
- orb100448
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- APC6 antibody
Related genes to: APC6 antibody
- Gene:
- CDC16 NIH gene
- Name:
- cell division cycle 16
- Previous symbol:
- -
- Synonyms:
- APC6, ANAPC6, CUT9
- Chromosome:
- 13q34
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-07
- Date modifiied:
- 2015-09-11
Related products to: APC6 antibody
Related articles to: APC6 antibody
- Brucella is an intracellular Gram-negative bacterium that primarily infects the host reproductive and immune systems, inducing autophagy and facilitating pathogen replication. TBC (Tre2-Bub2-Cdc16) domain-containing proteins is important in membrane trafficking, cell polarity, and signal transduction as regulators of Rab small GTPases. Previously, we demonstrated that B. melitensis M5-90 modulates the expression of miR-146b-5p, which targets TBC1D14, in RAW264.7 cells. In this study, CRISPR-Cas9 was used to generate TBC1D14-knockout (KO) Sheep Leydig cells (SLCs), and B.melitensis BA0711 treatment experiment was conducted at a multiplicity of infection (MOI) of 100. After confirming that SLCs retain autophagic activity, western blot, autophagy flux assays, transmission electron microscopy (TEM), and quantitative RT-PCR were performed to identify the function of TBC1D14. We found that fluorescence of autolysosome was significantly enhanced in NC-SLCs compared with TBC1D14-KO-SLCs following BA0711 treatment at 8 and 12 hpi. Notably, autophagy flux in NC-SLCs remained consistently higher than that in KO-SLCs from 8 hpi onwards. Consistently, Western blot revealed a decreased LC3-II/LC3-I ratio, and TEM confirmed a reduced number of autolysosomes in KO-SLCs at 12 hpi. These results indicate that TBC1D14 regulates autophagy positively in SLCs upon BA0711 stimulation. Although transcriptomic and proteomic analyses indicated activation of autophagy- and phagocytosis-related pathways during BA0711 exposure, this response was significantly attenuated in TBC1D14-deficient cells. Furthermore, TBC1D14 knockout led to down-regulation of phagosome-related proteins and altered chemotaxis pathways, whereas re-expression of TBC1D14 in KO cells upregulated RAB28. In conclusion, this study demonstrates that TBC1D14 positively regulates autophagy and provides insights into the response reaction of SLCs treated by B.melitensis BA0711, in addition to this, suggesting RAB28 may serve as a downstream effector of TBC1D14. - Source: PubMed
Publication date: 2026/07/16
Cheng YiwenNiu ShihuaZhang ZitongQian HejieHuang ZijingJing HuiLiao LianjieMan ChurigaGao HongyanChen QiaolingDu LiChen SiWang Fengyang - Melasma is a common acquired pigmented dermatosis, which seriously affects the appearance and quality of life of patients. Calreticulin (CALR) is a pleiotropic protein existing in nucleated cells, which mediates cellular immunity, and cellular immunity is closely related to the occurrence of melasma. In this study, 55 differentially expressed genes (31 up-regulated and 24 down-regulated) were screened by bioinformatics analysis of GSE72140 data set, and it was found that CALR was significantly highly expressed in melasma lesions. Functional enrichment analysis showed that CALR was associated with biological processes such as the localization and regulation of ribonucleoprotein complex and the assembly of MHC-I complex, and participated in the progression of melasma through KEGG pathway (such as cell cycle and progesterone-mediated oocyte maturation). Single cell analysis further revealed that CALR was highly expressed in Langerhans cells, macrophages and other immune cells, suggesting that CALR may promote melanin production through immune inflammatory reaction. Correlation analysis showed that CALR was strongly associated with PPDPF, CDC16 and PAPOLA, suggesting that CALR may regulate the function of melanocytes by influencing cell signal transduction, cell cycle regulation and mRNA metabolism. Protein interaction network analysis showed that CALR interacted with TET2, TP2 and STYX, suggesting that CALR may affect melasma through epigenetic regulation. This study provides the preliminary bioinformatics-based evidence for a potential role of CALR in melasma and proposes the 'immune-melanin axis' as an exploratory framework. However, these findings are only hypotheses and need to be experimentally validated through and studies in the future. - Source: PubMed
Publication date: 2026/06/20
Jia WeixueYang DejuanYu Shanshan - : Hyperthermia coupled with temperature-triggered drug delivery systems, including drug-loaded thermosensitive liposomes, that exhibit increased membrane permeability at hyperthermia-relevant temperatures is a promising therapeutic strategy for cancer treatment. Our previous study revealed that nitrogen-doped carbon dots (CD) partially interact with the phospholipids of liposomes, increasing the membrane permeability of an encapsulated anticancer drug. In vitro cell experiments indicated that their presence in the culture medium, albeit at relatively high concentrations, also affect cell membrane permeability, enhancing drug internalization in cancer cells. This study aims to introduce either hydrophilic or lipophilic carbon dots into liposomes and evaluate them as thermosensitive drug delivery systems. : Alkylated carbon dots (CD-C16) were synthesized and liposomal systems with either the lipophilic CD-C16 or the parent hydrophilic CD were prepared and efficiently loaded with doxorubicin (DOX). Following physicochemical characterization, their thermosensitivity was studied vs. time and temperature, while their effect on cell survival at 37 and 40 °C was evaluated against HEK293 and PC3 cells. : At 40 °C, for CD containing liposomes 50% DOX release is observed, whereas for CD-C16 containing liposomes 95% DOX is released within 5 min. Against PC3 cells at 40 °C, both DOX-loaded CD containing liposomes and CD-C16 containing liposomes are more potent compared to the parent drug-loaded liposomes, whereas CD-C16 containing liposomes are equally potent to free DOX. Against HEK293 cells the thermosensitive formulations at 40 °C prove even more cytotoxic, with CD-C16 containing liposomes being more potent than free DOX, but CD containing liposomes are advantageous for being less toxic than free DOX at 37 °C. : Although work is needed to elucidate the mechanism at the molecular level, the results suggest that it is possible to adjust liposomal membrane permeability through the incorporation of carbon dots in order to optimize performance for hyperthermia-based applications. - Source: PubMed
Publication date: 2026/04/25
Mavroidi BarbaraLyra Kyriaki MarinaSideratou ZiliTsiourvas Dimitris - TBC (Tre2/Bub2/Cdc16) domain-containing proteins constitute the widespread family of GTPase-activating proteins (GAPs). They interact with the Rab superfamily of small GTPases, stimulate GTP hydrolysis, and regulate vesicle trafficking. TBC1D17, involved in Shiga toxin trafficking, autophagy and glucose metabolism regulation, constitutes an example of GAP interacting with Rabs. Here we present the first crystal structures of the murine and human TBC domains of TBC1D17 proteins determined at 2.20 and 3.34 Å resolution, respectively. The TBC domain in both structures represents a heart-like shape. Our analyses revealed dimerization of the TBC domain through a fragment located near residues participating in GTP hydrolysis, a result we observed also in structures of closely related homologs. Furthermore, we tested Rab5a interactions with various fragments of TBC1D17. Interestingly, this protein contains an annotated, yet uncharacterized, Rab-binding domain (RBD) and our studies revealed strong interactions of Rab5a with TBC1D17 fragments containing RBD, while interactions with the TBC domain alone are much weaker. These results provide the first direct evidence for the critical role of the TBC1D17 RBD in interactions with Rab5a. - Source: PubMed
Nielipińska DominikaOrlikowska MartaNielipiński MaciejSekuła BartoszBłażewska Katarzyna MGendaszewska-Darmach EdytaPietrzyk-Brzezińska Agnieszka J - Lysosomes are highly dynamic organelles that serve antagonistic functions as terminal catabolic stations for the degradation of macromolecules and as central metabolic decision centers for anabolic growth signaling. Lysosome dysfunction is implicated in various human diseases. The physiological roles of lysosomes are linked to the control of lysosome position and dynamics via the activity of the kinesin-activating small GTPase ARL8. How the activity of ARL8 is regulated remains poorly understood. Here, we identify the GTPase-activating Tre-2/Bub2/Cdc16 (TBC) domain protein TBC1D9B as a critical negative regulator of ARL8B function. We demonstrate that TBC1D9B is associated with the lysosomal membrane protein TMEM55B, directly binds to ARL8B-GTP, and stimulates its GTPase activity. Knockout of TBC1D9B or its binding partner TMEM55B causes lysosome dispersion, defective autophagic flux, and impairs the adaptive degradative response of cells to limiting nutrient supply. These lysosomal phenotypes of TBC1D9B loss are occluded by concomitant depletion of ARL8 in cells. Collectively, our data unravel a key role for TBC1D9B in controlling lysosome function by serving as a negative regulator of ARL8 activity. - Source: PubMed
Publication date: 2026/03/14
Duhay ValentinTian MiaomiaoKosieradzka KlaudiaEbner MichaelLo Wen-TingKrauss MichaelSprengel Henner-LinusVoss MatthiasRiechmann MaraSavas Jeffrey NSchwake MichaelHaucke VolkerDamme Markus