Ask about this productRelated genes to: Snx10 antibody
- Gene:
- SNX10 NIH gene
- Name:
- sorting nexin 10
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 7p15.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-10
- Date modifiied:
- 2014-11-18
Related products to: Snx10 antibody
Related articles to: Snx10 antibody
- - Source: PubMed
Publication date: 2026/02/16
Hao Haiping - Acute lung injury (ALI) is a common complication of sepsis in connection with excessive inflammation and accumulation of oxidative stress. Sorting nexin 10 (SNX10) is a sorting nexin family member involved in inflammatory processes. This study aimed to explore the function of SNX10 in ALI. The cecal ligation and puncture (CLP) model was established to induce ALI in C57BL/6J mice. CLP mice exhibited elevated levels of SNX10 expression in the lung tissues. Mice were intratracheally injected with 50 μL adenovirus (108 PFU) containing short hairpin RNA plasmid targeting SNX10. SNX10 knockdown mice showed remission of CLP-induced pulmonary edema, hemorrhage, inflammatory infiltration, and thickened alveolar septum. SNX10 downregulation reduced reactive oxygen species (ROS) levels, increased superoxide dismutase activity and glutathione content, and decreased malondialdehyde content in the lung tissues. SNX10 knockdown decreased the phosphorylation of NF-κB p65 and its nuclear translocation, thus inhibiting the levels of tumor necrosis factor (TNF)-α and interleukin (IL)-6. Furthermore, SNX10 downregulation inhibited the NLRP3, p20 caspase 1, and ASC protein levels and the levels of IL-18 and IL-1β. A549 cells were treated with lipopolysaccharide (LPS) (10 μg/mL) for 24 h to simulate the inflammatory condition and SNX10 was knocked down using small interfering RNA. SNX10 knockdown cells showed increased viability and less ROS accumulation. Consistent with the in vivo results, the NF-κB/NLRP3 pathway and the secretion of inflammatory cytokines were inhibited after SNX10 knockdown in A549 cells. In summary, SNX10 downregulation mitigated sepsis-induced oxidative stress and pulmonary inflammation by inhibiting the NF-κB/NLRP3 pathway. - Source: PubMed
Publication date: 2026/02/16
Wei MinYang JianYu ZejiaLi ShanXie HuiYuan ShiyangHuang QiujieZhang HuiFeng Jun - In this exploratory pilot study, we profiled human periodontal ligament (PDL) transcriptomes during early orthodontic tooth movement (OTM). Early-stage (0-10 days) transcriptional dynamics under tension and compression remain insufficiently understood, and no dedicated user-friendly resource has been available for exploring large-scale human data. - Source: PubMed
Publication date: 2026/02/18
Zhang XiaoqiXing LuAi-Gumaei WaseemZhang XiaoqianWang QingxuanLi MinqiLong HuLai Wenli - Colorectal cancer (CRC) originates from biological events caused by gene mutations in normal intestinal epithelial cells (IECs). Sorting nexin 10 (SNX10) is a tumor suppressor in CRC that is involved in regulating chaperone-mediated autophagy (CMA) activity, which is implicated in the pathogenesis of CRC and glycolysis process. DEP domain containing 5 (DEPDC5) is a negative upstream regulator of mammalian target of rapamycin complex 1 (mTORC1). α-hederin has anti-CRC effects. We previously found that SNX10 knockdown in normal human IECs promoted glycolysis and decreased DEPDC5 expression, which was reversed by α-hederin. However, the specific mechanism has not yet been elucidated. Here, we aimed to investigate the specific regulatory mechanism of SNX10 on DEPDC5 expression, and the action of α-hederin on this process. We demonstrated that the degradation of DEPDC5 protein was accelerated after SNX10 knockdown, causing the activation of the mTORC1 pathway, which relied on CMA activation and lysosomal function enhancement. SNX10 interacted with DEPDC5 and recruited it to lysosomes for degradation, and the glycolysis level mediated by mTORC1 was elevated. Additionally, these phenotypes in shSNX10 IECs were compromised by SNX10 rescue. Moreover, α-hederin bound to the SNX10-DEPDC5 complex and impaired the interaction between SNX10 and DEPDC5, thereby inhibiting CMA-mediated DEPDC5 degradation, impairing the aberrant activation of mTORC1 signaling, and eventually reversing the elevation of glycolysis caused by SNX10 knockdown. Overall, we are the first to demonstrate that SNX10-mediated DEPDC5 degradation is a novel strategy for malignant transformation of normal human IECs, with α-hederin regulated during this process. - Source: PubMed
Publication date: 2025/04/12
Feng HuiWang JinTao LihuipingLi LiuFan MinminYu ChengtaoSun DongdongCheng HaiboShen Weixing - Bone-resorbing osteoclasts (OCLs) are large, multi-nucleated cells that are formed through well-regulated differentiation and cell fusion of monocyte-macrophage precursors. Abnormally increased or decreased OCL-mediated bone resorption perturbs bone structure and homeostasis and may lead to severe illnesses, such as osteoporosis and autosomal recessive osteopetrosis (ARO), respectively. Mutations in the intracellular trafficking-associated protein sorting nexin 10 (SNX10) lead to "OCL-rich" ARO, in which OCLs are inactive. Mature, SNX10-deficient murine OCLs fuse continuously to generate gigantic cells, in vitro and in vivo, unlike wild-type OCLs that stop fusing with each other upon maturation, indicating that SNX10 is required for both the resorptive activity of OCLs and the arrest of cell fusion upon maturation. Mutations in CLC-7 and OSTM1, which comprise the lysosomal voltage-gated Cl-/H+ exchanger, also induce OCL-rich ARO in humans and in mouse models, and are associated with the presence of large OCLs. In this study we explored the molecular interplay between SNX10, CLC-7 and OSTM1 by comparing the phenotypes of cultured mouse OCLs lacking one of these proteins. We show that loss of each protein leads to the formation of similarly-gigantic OCLs in culture, due to deregulated fusion between mature OCLs that proceeds with similar kinetics. All three proteins co-localize in LAMP1-positive lysosomes, located at both perinuclear and peripheral regions of mature wild-type OCLs. SNX10-KO OCLs exhibit few peripheral lysosomes containing CLC-7 and OSTM1, indicating that SNX10 is required for regulating their trafficking to the cell periphery. CLC-7 and SNX10 physically interact with each other and loss of CLC-7 depletes peripheral OSTM1-containing lysosomes, indicating that CLC-7 is also required for this transport. Taken together, these findings indicate that SNX10 and CLC-7 regulate the subcellular distribution of lysosomes containing CLC-7 and OSTM1, thereby establishing a functional link between these three proteins that controls both the fusion and functionality of mature OCLs. - Source: PubMed
Publication date: 2025/12/18
Reuven NinaWinograd-Katz SabinaBarnea-Zohar MaayanPri-Or AmirLevin YishaiVacher JeanGeiger BenjaminElson Ari