Ask about this productRelated genes to: SNX27 antibody
- Gene:
- SNX27 NIH gene
- Name:
- sorting nexin 27
- Previous symbol:
- -
- Synonyms:
- MY014, KIAA0488, MGC20471
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-05
- Date modifiied:
- 2019-04-15
Related products to: SNX27 antibody
Related articles to: SNX27 antibody
- Retinal ischemia/reperfusion (I/R) injury is a major cause of vision loss, characterized by retinal edema and progressive retinal ganglion cell (RGC) death. Aquaporin-4 (AQP4), a water channel abundantly expressed in glial cells, plays a pivotal role in edema formation by regulating water homeostasis. Geranylgeranylacetone (GGA), a clinically approved anti-ulcer drug, functions as a potent and non-toxic inducer of heat shock protein 70 (HSP70) and has recently been implicated in the regulation of aquaporin trafficking. In parallel, the sorting nexin 27 (SNX27)-retromer complex is a key mediator of endosomal sorting and recycling of membrane proteins back to the plasma membrane, thereby maintaining their functional activity. In this study, we demonstrate that retinal I/R injury triggers altered subcellular localization of AQP4, with enhanced internalization compared with sham retinas. Concomitantly, SNX27-retromer expression was significantly upregulated at both mRNA and protein levels, and biochemical as well as imaging assays confirmed its interaction with AQP4. In a pre-ischemia dosing paradigm (prophylactic), GGA markedly attenuated retinal edema and RGC loss, and promoted the interaction between HSP70 and the SNX27-retromer complex. Importantly, GGA treatment reduced SNX27-retromer expression, thereby limiting AQP4 recycling to the plasma membrane and favoring its lysosome-associated trafficking. These effects were largely reversed by quercetin, a pharmacological inhibitor of HSP70, highlighting an HSP70-dependent mechanism. Together, our findings identify a previously unrecognized role of HSP70 in regulating SNX27-retromer-mediated AQP4 trafficking. By disrupting AQP4 recycling, GGA alleviates early retinal edema following I/R injury, providing mechanistic rationale for future therapeutic development. - Source: PubMed
Qian WeijianZhang LirongCheng XuefengXue KaigeTian RanFan PingXu JinZhu ShujuanQiu GuopingRan JianhuaGan Shengwei - - Source: PubMed
Publication date: 2026/05/13
Wang ShengnanZhang DanZhang Leiliang - A growing body of evidence suggests that exposure to environmental noise is linked to the development of cardiovascular disease (CVD). Here, we used two-sample Mendelian randomization (MR) to investigate whether noise-related DNA methylation (DNAm) alterations are causally associated with CVDs and their risk factors. - Source: PubMed
Publication date: 2026/04/30
Xiao HuaSun LeiQin XiuZhang HaoFengHe FuDongNan YuFanChen HaiYanHao Guang - Many proteins can reach the cell surface through a Golgi-independent unconventional protein secretion (UPS) pathway, particularly under cellular stress conditions. However, the molecular mechanisms that mediate UPS remain largely elusive. In this study, VPS26A-containing retromer complex, along with the sorting nexin SNX27, is identified as a regulator of UPS of transmembrane proteins, including the trafficking-deficient ∆F508 mutant CFTR, which causes cystic fibrosis, and the SARS-CoV-2 spike protein, associated with COVID-19. A targeted CRISPR knockout screen identified VPS26A as a key contributor in the UPS of ∆F508-CFTR. Subsequent molecular analyses revealed that SNX27 recruits ∆F508-CFTR to the VPS26A-VPS35-VPS29 retromer complex, facilitating its transport to the cell surface under UPS-inducing conditions. Additionally, VPS26A and SNX27 are necessary for UPS of the spike protein, enabling the formation of intact SARS-CoV-2 virions. These findings suggest that the retromer complex and SNX27, known for their roles in recycling endosomes, mediate previously unrecognized functions in the UPS of transmembrane proteins. - Source: PubMed
Publication date: 2026/04/06
Kim Ye JinLee ChaeyoungSeo Soo KyungRoh Jae WonLee Hye RyungHwang Su JinChang NienpingChoi Hee SeongShin Dong HoonKim Hui KwonKim Han SangCho Hyun-SooLee Jae MyunGee Heon YungLee Min GooNoh Shin Hye - The evolutionarily conserved Retromer complex, composed of Vps29, Vps26 and Vps35, is an essential regulator of endosomal retrieval of transmembrane cargo proteins. For cargo sorting and trafficking to take place, Retromer assembles into coated tubulovesicular carriers together with various sorting nexin (SNX) adaptor proteins including SNX3 and SNX27 in metazoans, and Snx3 or the dimeric Vps5-Vps17 SNX-BAR proteins in yeast. Although Retromer-coated tubulovesicular carriers are vital for its function, the in vitro reconstitution of these membrane assemblies for structural and functional studies can be technically challenging. Approaches include the use of giant unilamellar vesicles and supported membrane tubules for fluorescence imaging, or smaller multilamellar vesicles (MLVs) to generate uniform tubules for imaging by cryoelectron tomography (CryoET). This chapter describes protocols for producing MLVs for membrane binding studies of Retromer and assembling the yeast Retromer-Vps5-Vps17 heteropentameric complex for reconstituting membrane tubulation for CryoET studies. We also discuss our observations of both poorly ordered and well-ordered Retromer coats observed in this experimental setup. - Source: PubMed
Publication date: 2026/01/23
Chen Kai-EnTillu Vikas AAriotti NicholasCollins Brett M