Ask about this productRelated genes to: RGS22 antibody
- Gene:
- RGS22 NIH gene
- Name:
- regulator of G protein signaling 22
- Previous symbol:
- -
- Synonyms:
- DKFZP434I092, PRTD-NY2, CT145
- Chromosome:
- 8q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-02-23
- Date modifiied:
- 2017-04-13
Related products to: RGS22 antibody
Related articles to: RGS22 antibody
- In metazoan epithelia, arrays of motile cilia beat in a tissue-wide coordinated manner to drive unidirectional fluid flow. Whether radial spokes (RSs), which mediate mechano-signal transduction between the central pair and axonemal dynein arms, acquire metazoa-specific subunit(s) in evolution to facilitate this function remains poorly known. Here we report that Gα-GTPase activating protein family member RGS22 is a metazoa-specific component of RS1/2 complexes. Mouse Rgs22-deficient motile cilia exhibit ultrastructural defects, including deformation of the RS1 and disorganization of outer dynein arms. These abnormalities correlate with impaired planar polarity, manifested as unsynchronized ciliary beating and disrupted rotational polarity of basal bodies across the ependyma. The motility deficits further lead to progressive ciliary loss and shortening, resulting in postnatal hydrocephalus. Together, our data identify RGS22 an animal-lineage RS1/2 component required for normal RS architecture and associated with tissue-level ciliary motility and coordination phenotypes. - Source: PubMed
Publication date: 2026/06/24
Fang AnxuanLuo JiajunXu HaomangPeng Ye-JunXu WeiCao HuiwenLi WeiDai JialeiShi ZhipengWang YongLi Xiao-MengZhao HuijieGui MiaoYu ChaoZhu XueliangZhang Qianting - Ependymal cells line the wall of cerebral ventricles and ensure the unidirectional cerebrospinal fluid (CSF) flow by beating their motile cilia coordinately. The ependymal denudation or ciliary dysfunction causes hydrocephalus. Here, we report that the deficiency of regulator of G-protein signaling 22 (RGS22) results in severe congenital hydrocephalus in both mice and rats. Interestingly, RGS22 is specifically expressed in ependymal cells within the brain. Using conditional knock-out mice, we further demonstrate that the deletion of Rgs22 exclusively in nervous system is sufficient to induce hydrocephalus. Mechanistically, we show that Rgs22 deficiency leads to the ependymal denudation and impaired ciliogenesis. This phenomenon can be attributed to the excessive activation of lysophosphatidic acid receptor (LPAR) signaling under Rgs22 condition, as the LPAR blockade effectively alleviates hydrocephalus in Rgs22 rats. Therefore, our findings unveil a previously unrecognized role of RGS22 in the central nervous system, and present RGS22 as a potential diagnostic and therapeutic target for hydrocephalus. - Source: PubMed
Publication date: 2024/10/10
Pang XueGu LinHan Qiu-YingXing Jia-QingZhao MingHuang Shao-YiYi Jun-XiPan JieHong HaoXue WenZhou Xue-QingSu Zhi-HuiZhang Xin-RanSun Li-MingJiang Shao-ZhenLuo DanChen LingWang Zheng-JieYu YuXia TianZhang Xue-MinLi Ai-LingZhou TaoCai HongLi Tao - Phaeochromocytomas and paragangliomas (PPGLs) are rare neuroendocrine tumours. Pathogenic variants have been identified in more than 15 susceptibility genes; associated tumours are grouped into three Clusters, reinforced by their transcriptional profiles. Cluster 1A PPGLs have pathogenic variants affecting enzymes of the tricarboxylic acid cycle, including succinate dehydrogenase. Within inherited PPGLs, these are the most common. PPGL tumours are known to undergo epigenetic reprograming, and here, we report on global histone post-translational modifications and DNA methylation levels, alongside clinical phenotypes. - Source: PubMed
Publication date: 2023/12/20
Chatzikyriakou ProdromosBrempou DimitriaQuinn MarkFishbein LaurenNoberini RobertaAnastopoulos Ioannis NTufton NicolaLim Eugenie SObholzer RupertHubbard Johnathan GMoonim MufaddalBonaldi TizianaNathanson Katherine LIzatt LouiseOakey Rebecca J - Regulator of G-protein signaling 22 (RGS22) is specifically expressed in the testis and in tumors of epithelial origin, but the expression and role of RGS22 in pancreatic cancer are unclear. In this study, 52 pairs of pancreatic ductal adenocarcinoma (PDAC) and adjacent non-neoplastic tissue samples with the corresponding clinical data were used to examine the expression of RGS22 and its relationship with PDAC prognosis. The findings showed that the expression of RGS22 was higher in the PDAC tissues than in the adjacent non-tumorous tissues and its expression was associated with the degree of blood vessel invasion. The experiments with PDAC cell lines and a normal control cell line showed that the proliferation, invasion, and metastasis of PDAC cells were suppressed by RGS22 overexpression and enhanced by RGS22 knockdown. The effect of RGS22 on PDAC xenografts was studied using subcutaneous implantation of tumor cells in BALB/cA-nu mice, and the results corroborated the findings. Analysis of the regulators of RGS22 showed that it was positively regulated by the transcription factor Yin Yang-1 (YY1). Thus, YY1-mediated RGS22 regulation suppressed the proliferation, migration, and invasion of PDAC. - Source: PubMed
Publication date: 2022/11/02
Cao Shou-JiGe Wan-LiMeng Ling-DongChen QunMiao YiJiang Kui-RongZhang Jing-Jing - In the context of artificial insemination, male fertility is defined as the ability to produce functional spermatozoa able to withstand cryopreservation. We hypothesized that interindividual variations in fertility depend on the proportion of the fully functional sperm population contained in the insemination dose. The objective of this study was to identify protein markers of the fully functional sperm subpopulation. Insemination doses from four high-fertility (HF) and four low-fertility (LF) bulls with comparable post-thaw quality parameters were selected for proteomic analysis using iTRAQ technology. Thawed semen was centrifuged through a Percoll gradient to segregate the motile (high density [HD]) from the immotile (low density [LD]) sperm populations. Sperm proteins were extracted with sodium deoxycholate and four groups were compared: LD and HD spermatozoa from LF and HF bulls. A total of 498 unique proteins were identified and quantified. Comparison of HD spermatozoa from HF and LF bulls revealed that five proteins were significantly more abundant in the HF group (AK8, TPI1, TSPAN8, OAT, and DBIL5) whereas five proteins were more abundant in the LF group (RGS22, ATP5J, CLU, LOC616319, and CCT5). Comparison of LD spermatozoa from HF and LF bulls revealed that four proteins were significantly more abundant in the HF group (IL4I1, CYLC2, OAT, and ARMC3) whereas 15 proteins were significantly more abundant in the LF group (HADHA, HSP90AA1, DNASE1L3, SLC25A20, GPX5, TCP1, HIP1, CLU, G5E622, LOC616319, HSPA2, NUP155, DPY19L2, SPERT, and SERPINE2). DBIL5, TSPAN8, and TPI1 showed potential as putative markers of the fully functional sperm subpopulation. - Source: PubMed
Publication date: 2019/05/27
D'Amours OlivierCalvo ÉzéquielBourassa SylvieVincent PatrickBlondin PatrickSullivan Robert