Ask about this productRelated genes to: SEC22C antibody
- Gene:
- SEC22C NIH gene
- Name:
- SEC22 homolog C, vesicle trafficking protein
- Previous symbol:
- SEC22L3
- Synonyms:
- MGC13261, MGC5373
- Chromosome:
- 3p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-02-04
- Date modifiied:
- 2016-10-05
Related products to: SEC22C antibody
Related articles to: SEC22C antibody
- Although many studies have examined the relationship between host genetics and serum metabolites, it is still unclear to what extent host genetic variation contributes to growth-related serum metabolic patterns in chickens. To address this issue, we performed whole-genome resequencing, transcriptome sequencing, and untargeted metabolomics analyses on blood samples collected from a population of Chinese local chickens. The results showed that single-nucleotide polymorphisms (SNPs) significantly associated with growth performance were predominantly mapped the genomic regions of SEC22C, ABCD3, SRGAP2, and CDC42BPA. SEC22C, ABCD3, and SRGAP2 were significantly associated with both body weight (BW) and average daily gain (ADG), whereas CDC42BPA was significantly associated only with ADG. Comparative analysis of blood transcriptomes between high and low BW recombinant chickens revealed that SEC22C was more strongly associated with the low BW group, while CDC42BPA exhibited significantly higher expression levels in high-weight chickens. Five metabolites, including 1-myristoyl-sn-glycerol-3-phosphate choline, were significantly associated with 45 genes, including SRGAP2, PA2G4, TENM3, MAP2K6, and ADIPOR2. Furthermore, SRGAP2 may regulate the growth of the chickens through 1-myristoyl-sn-glycerol-3-phosphate choline. This study comprehensively elucidates the combined effects of host genetics and serum metabolites on growth traits, providing a robust scientific basis for studying the growth performance of local chickens. - Source: PubMed
Publication date: 2026/01/23
Yang XiaolingLong XiaoxiaYang YongxianWang LiqiWang Zhong - Uveal melanoma (UM) is the most common primary intraocular malignant tumor in adults; little is known about the contribution of non-coding RNAs (ncRNAs) to UM pathogenesis. Competitive endogenous RNA (ceRNA) networks based on RNA-RNA interactions regulate physiological and pathological processes. Through a combined approach of in silico and experimental biology, we investigated the expression of a set of long non-coding RNAs (lncRNAs) in patient biopsies, identifying as a potential oncogene in UM. The detection of dysregulation associated with several in vitro functional assays allowed us to investigate its ceRNA regulatory network and shed light on its potential involvement in cancer-related processes, such as epithelial to mesenchymal transition (EMT) and CoCl-induced hypoxia-like response. In vitro transient silencing of impaired cell proliferation and migration, and affected mRNA expression of , , , , and . A "miRNA sponge" and "miRNA protector" model have been hypothesized for -induced regulation of mRNAs. In vitro inhibition of suggested its role as a potential activator of expression. Comprehensively, may be considered a new oncogene in UM and a potential target for RNA-based therapeutic approaches. - Source: PubMed
Publication date: 2020/12/21
Barbagallo CristinaCaltabiano RosarioBroggi GiuseppeRusso AndreaPuzzo LidiaAvitabile TeresioLongo AntonioReibaldi MicheleBarbagallo DavideDi Pietro CinziaPurrello MicheleRagusa Marco - Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are a large protein complex that is involved in the membrane fusion in vesicle trafficking, cell growth, cytokinesis, membrane repair, and synaptic transmission. As one of the SNARE proteins, SEC22B functions in membrane fusion of vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus, antigen cross-presentation, secretory autophagy, and other biological processes. However, apart from not being SNARE proteins, there is little knowledge known about its two homologs (SEC22A and SEC22C). SEC22B alterations have been reported in many human diseases, especially, many mutations of SEC22B in human cancers have been detected. In this review, we will introduce the specific functions of SEC22B, and summarize the researches about SEC22B in human cancers and other diseases. These findings have laid the foundation for further studies to clarify the exact mechanism of SEC22B in the pathological process and to seek new therapeutic targets and better treatment strategies. - Source: PubMed
Publication date: 2020/08/31
Sun WeiTian Bi-XiaWang Shu-HongLiu Pei-JunWang Yao-Chun - Sec22c has been characterized as an endoplasmic reticulum (ER)-localized transmembrane protein involved in regulation of the vesicle transport between the ER and the Golgi. Sec22c has several isoforms generated by alternative splicing that changes the number of the C-terminal transmembrane domains (TMDs). However, the physiological significance of the splicing remains unknown. Here we show that the splicing isoforms containing four TMDs unexpectedly localized at cis-Golgi, whereas the splicing isoforms containing less than four TMDs localized at the ER. The C-terminal fragment containing the four TMDs was sufficient for the cis-Golgi localization and bound to ADP-ribosylation factor 4 (ARF4). ARF4 knockdown and overexpression of a constitutively active mutant of ARF4 decreased the cis-Golgi localization of the C-terminal fragment and the full-length protein, respectively. These results indicate that the splicing-dependent changes in the number of TMDs allow Sec22c to regulate the subcellular localization in cooperation with ARF4, implying that Sec22c will function at the Golgi as well as the ER. - Source: PubMed
Publication date: 2017/04/14
Yamamoto YasunoriYurugi ChisatoSakisaka Toshiaki - Yeast Sec22p participates in both anterograde and retrograde vesicular transport between the endoplasmic reticulum (ER) and the Golgi apparatus by functioning as a v-SNARE (soluble N-ethylmaleimide-sensitive factor [NSF] attachment protein receptor) of transport vesicles. Three mammalian proteins homologous to Sec22p have been identified and are referred to as Sec22a, Sec22b/ERS-24, and Sec22c, respectively. The existence of three homologous proteins in mammalian cells calls for detailed cell biological and functional examinations of each individual protein. The epitope-tagged forms of all three proteins have been shown to be primarily associated with the ER, although functional examination has not been carefully performed for any one of them. In this study, using antibodies specific for Sec22b/ERS-24, it is revealed that endogenous Sec22b/ERS-24 is associated with vesicular structures in both the perinuclear Golgi and peripheral regions. Colabeling experiments for Sec22b/ERS-24 with Golgi mannosidase II, the KDEL receptor, and the envelope glycoprotein G (VSVG) of vesicular stomatitis virus (VSV) en route from the ER to the Golgi under normal, brefeldin A, or nocodazole-treated cells suggest that Sec22b/ERS-24 is enriched in the pre-Golgi intermediate compartment (IC). In a well-established semi-intact cell system that reconstitutes transport from the ER to the Golgi, transport of VSVG is inhibited by antibodies against Sec22b/ERS-24. EGTA is known to inhibit ER-Golgi transport at a stage after vesicle/transport intermediate docking but before the actual fusion event. Antibodies against Sec22b/ERS-24 inhibit ER-Golgi transport only when they are added before the EGTA-sensitive stage. Transport of VSVG accumulated in pre-Golgi IC by incubation at 15 degreesC is also inhibited by Sec22b/ERS-24 antibodies. Morphologically, VSVG is transported from the ER to the Golgi apparatus via vesicular intermediates that scatter in the peripheral as well as the Golgi regions. In the presence of antibodies against Sec22b/ERS-24, VSVG is seen to accumulate in these intermediates, suggesting that Sec22b/ERS-24 functions at the level of the IC in ER-Golgi transport. - Source: PubMed
Zhang TWong S HTang B LXu YHong W