Ask about this productRelated genes to: SNX9 antibody
- Gene:
- SNX9 NIH gene
- Name:
- sorting nexin 9
- Previous symbol:
- -
- Synonyms:
- SH3PX1, SDP1, SH3PXD3A
- Chromosome:
- 6q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-10
- Date modifiied:
- 2015-02-02
Related products to: SNX9 antibody
Related articles to: SNX9 antibody
- Hepatocellular carcinoma (HCC) is a highly aggressive primary liver malignancy characterized by limited therapeutic options and poor prognosis. Within the tumor microenvironment (TME), tumor-associated macrophages (TAMs) predominantly exhibit an M2-like phenotype, contributing to immune escape and tumor progression. Zymogen granule protein 16 (ZG16) has been reported to be downregulated in HCC, but its precise biological function and molecular mechanisms remain poorly understood. Therefore, we aimed to investigate the impact of ZG16 on HCC cell metastasis and TAM infiltration, as well as to elucidate its molecular mechanism. - Source: PubMed
Publication date: 2026/03/04
Meng HuiWang ZeyuanWang LiyeFang XiaokunLi HaonanMa WeiqianDing YiNan ManmanMeng YuLi LingLi YizhenChen KuishengZhang Mingzhi - NUMB is an endocytic protein with tumor suppressor activity, largely mediated by its ability to inhibit p53 degradation. This function depends on the inclusion of a short alternatively spliced exon (Ex3) in NUMB, although the mechanistic link between endocytosis and p53 regulation remains unclear. Here, we show that the Ex3-encoded sequence directs NUMB to the plasma membrane, where it forms a complex with the endocytic adaptor SNX9. This complex recruits p53 in an SNX9-dependent manner and is internalized and trafficked to multivesicular bodies, culminating in exosomal secretion, in a process requiring both SNX9 and NUMB. Exosomal p53 is taken up by recipient cells and translocated to the nucleus, where it activates p53-dependent transcriptional and phenotypic programs. These findings suggest that exosome-mediated p53 transfer may contribute to the establishment of a tumor-suppressive microenvironment. - Source: PubMed
Publication date: 2026/01/30
Cacciatore RobertaBasile AndreaFreddi StefanoSchiano Lomoriello IreneZucca Carlo RibelleCiossani GiuseppeScietti LuigiCuomo AlessandroRonzoni SimonaPelicci SimoneFaretta MarioZaccheroni ElenaPelicci GiulianaMatafora VittoriaBachi AngelaGunby Rosalind HelenPece SalvatoreSigismund SaraLanzetti LetiziaColaluca Ivan NicolaDi Fiore Pier Paolo - AIM2, an inflammasome sensor, has been extensively investigated for its ability to induce pyroptosis in macrophages. However, its role in the adaptive immune system remains poorly studied, particularly in B cells. AIM2 knockout mice had decreased follicular (FO) and marginal zone (MZ) B cell subsets and impaired IgG3 switching. The activation of B cells enhanced the co-localization of AIM2 and BCR. Interestingly, AIM2 exerts dual regulatory effects on BCR signaling transduction by positively regulating the PI3K-AKT signaling axis and negatively regulating the BTK-NFκB signaling axis. Through immunoprecipitation-mass spectrometry (IP-MS) analysis, SNX9 was identified as a critical molecule that promotes downstream signaling by facilitating the association of PI3K with CD19 in an AIM2-dependent manner. Furthermore, AIM2 is involved in the endocytosis of BCR and CD19 and the subsequent antigen uptake and presentation processes via SNX9-WASP interaction. In AIM2 knockout mice, this dual regulation leads to reduced overall BCR signaling characterized by decreased calcium signaling and reduced antibody production following RBD immunization. Conversely, AIM2 is overexpressed in B cells of Kawasaki disease patients, contributing to the development of this autoimmune disease. In summary, our study has unveiled a novel positive regulatory role of AIM2 in B cell receptor activation, endocytosis, and humoral response, focusing on AIM2-associated signaling pathways in B cells. - Source: PubMed
Publication date: 2025/12/23
Huang YanmeiGao PengyueLuo LiBai YuxinWang WeijiayiJiang PanpanZhang XinLai JuanLiu JuChang JiangDai XinLuo XiGuan FeiMiller HeatherDu XingrongLei JiahuiYang LuLiu Chaohong - Sorting nexin 9 () is involved in intracellular vesicle transport and signal transduction, and its abnormal expression is related to the occurrence and development of a variety of cancers. In lung adenocarcinoma (LUAD), the role and molecular mechanism of remain unclear. This study combined bioinformatics analysis and validation to explore its expression characteristics in LUAD, its specific effects on tumor development, and its potential molecular mechanism and prognostic value. - Source: PubMed
Publication date: 2025/11/26
Liu WeidiYin YichenWang BaozhenLi TaoChen Jing - EspF is an enteropathogenic Escherichia coli (EPEC) effector protein that interferes with intestinal epithelial cell signaling by binding to the Src homology 3 (SH3) domain of sorting nexin 9 (SNX9) and the GTPase-binding domain (GBD) of neural Wiskott-Aldrich syndrome protein (N-WASP) with its C-terminal proline-rich repeats. To understand the molecular basis of these interactions, we characterized the structure, dynamics, and binding thermodynamics of EspF and its target protein domain complexes. We also elaborated on our previous study on EspF, a homologous effector in enterohemorrhagic E. coli (EHEC), and compared the two effectors. We show that EspF is intrinsically disordered but that NMR chemical shifts expose the pre-structured polyproline II (PPII) helical SH3- and helical GBD-binding motifs. These motifs mimic their cellular counterparts but are fine-tuned to prevail in competitive binding. Factors behind EspF's higher affinity for GBD relative to the cellular ligand are key residue mutations and a C-terminally elongated polar interaction interface. The latter compensates for the lack of an "extended arm", the critical substitution promoting high affinity for GBD in EspF. With this advantage, EspF outcompetes the autoinhibitory N-WASP C-helix and stimulates actin polymerization. EspF binds SNX9 SH3 with an extended binding interface, residues N-terminal to the RxAPxxP core motif being essential to strong binding. We define the SNX9 SH3-binding epitope as ϕxPxRxAPxxP and propose to re-delineate the EPEC EspF repeat boundaries accordingly. Furthermore, a characteristic C secondary chemical shift pattern is recognized as a fingerprint of polyproline II (PPII) helical conformation in the SH3 binding epitope. - Source: PubMed
Publication date: 2025/10/10
Tossavainen HelenaKarjalainen MikaelAntenucci LinaHellman MaaritPermi Perttu