Ask about this productRelated genes to: SDCBP antibody
- Gene:
- SDCBP NIH gene
- Name:
- syndecan binding protein
- Previous symbol:
- -
- Synonyms:
- SYCL, MDA-9
- Chromosome:
- 8q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-02-11
- Date modifiied:
- 2015-12-16
Related products to: SDCBP antibody
Related articles to: SDCBP antibody
- The immune checkpoint receptor T cell immunoreceptor with Ig and ITIM domains (TIGIT) can signal via cytoplasmic motifs to regulate T cell function. The signaling molecules that mediate inhibitory TIGIT signaling and its regulation in T cells remain poorly defined. Here, proximity proteomics is employed to define TIGIT-proximal proteins upon CD155 engagement, identifying several that are ligation-specific, including those involved in signaling (Grb2 and SOS1), cytoskeletal regulation (CD2AP and SdcBP), and endocytosis (IST1 and SNX3). Through crosslinking followed by immunoprecipitation, we show that TIGIT and CD2AP directly interact, representing a novel association. A TIGIT mutant (Y225A/Y231A) incapable of inhibitory signaling prevents recruitment of these proteins. Strikingly, T cell receptor (TCR) stimulation is essential for TIGIT to engage with these pathways. Mechanistically, phosphorylation of TIGIT requires both CD155 ligation and TCR activation, resulting in its signaling and internalization. TCR activation-dependent TIGIT signaling establishes a regulatory mechanism that limits checkpoint control to when functionally required. - Source: PubMed
Publication date: 2026/08/05
Zammit William HLe Maistre Lucy JElliot Thomas A ECain Stuart AHumphries Martin JDavis Daniel MWorboys Jonathan D - Syndecan binding protein (SDCBP) has been shown to be upregulated in esophageal squamous cell carcinoma (ESCC) and predicts poor prognosis in our previous research. SDCBP stimulated the proliferation and tumor formation and may be a target for ESCC. However, the participation of SDCBP in epithelial-mesenchymal transition (EMT) and ESCC metastasis is unclear. In this study, we found that SDCBP promoted the EMT process of ESCC cells and facilitated ESCC metastasis both in vitro and in vivo. Mechanically, SDCBP was found to influence the activation of the Wnt-β-catenin pathway. β-catenin expression and nuclear localization were regulated by SDCBP, accompanied by altered expression of Wnt-β-catenin pathway target genes. Additionally, SDCBP interacted with Y-box binding protein 1 (YBX1) and abnormally upregulated YBX1 in ESCC was responsible for SDCBP-mediated regulation of ESCC migration and invasion. Finally, SDCBP was identified to be transcriptionally regulated by the Wnt-β-catenin pathway. Thus, our study provides a better understanding of the SDCBP-YBX1-Wnt-β-catenin axis in ESCC metastasis and explores a positive feedback loop between SDCBP and the Wnt-β-catenin pathway, offering more compelling evidence for employing SDCBP as a target for ESCC treatment. - Source: PubMed
Du RuijuanBian BoLuo ManyuYuan ChenGuo KeleiLi KaiZhang HuiZhang GuangjiHan Li - Melanoma differentiation associated gene-9 (MDA-9), also known as Syntenin-1 or SDCBP, exhibits elevated expression in multiple cancers, promoting invasion, migration, and tumor cell survival. The TCGA database reveals high MDA-9 expression in late-stage HPV (-) HNSCC tissues, which associates with poor patient survival. Moreover, bioinformatics analyses support a potential role of MDA-9 in promoting cancer stemness in HNSCC tissues. We characterized the functional role of MDA-9 in HNSCC tumorigenesis, particularly in relation to cancer stem cell maintenance. Knockdown of MDA-9 suppresses BMI1, a functional cancer stem cell marker in HNSCC, and the self-renewal of cultured HNSCC cells. Mechanistically, MDA-9 controls expression of BMI1 through NF-κB p65. Targeting MDA-9 with a specific small molecule pharmacological inhibitor, IVMT-Rx-4, inhibits HNSCC growth and metastasis in a HNSCC xenograft mouse model. In vivo lineage tracing reveals that IVMT-Rx-4 potently inhibits self-renewal and tumorigenicity of Bmi1 cancer stem cells in a spontaneous model of HNSCC. Additionally, IVMT-Rx-4 significantly improves treatment with cisplatin by eliminating cisplatin-enriched Bmi1 cancer stem cells, thereby overcoming cisplatin resistance. Taken together, our results demonstrate that targeting MDA-9 with IVMT-Rx-4 is an effective strategy for treating HNSCC by eliminating cancer stem cells, and IVMT-Rx-4 is a promising chemical entity that may be amenable for developing an effective therapy for HNSCC. - Source: PubMed
Publication date: 2026/06/24
Rilee Grace JZaman Shadid UManupati KanakarajuMa ZhikunHoyle Rosalie GBacolod Manny DLopresti Marion QBrown Anne MDas Swadesh KFisher Paul BLi Jiong - The intrinsic dynamic asymmetry between homologous PDZ domains in multidomain scaffold proteins offers insight into how they achieve multivalent partner recognition. Through a systematic x-ray crystallographic analysis of tandem PDZ1-PDZ2 domains in human syntenin-1 (SDCBP/MDA-9), we solved nine high-resolution structures and uncovered fundamental differences in conformational plasticity between these sequentially similar domains. Pairwise root mean square deviation (RMSD) analysis of 20 PDZ1 structures across multiple crystal forms revealed substantial structural variability concentrated in the Lys119-Ile125 and Ala181-Glu184 loops-key regions governing ligand specificity within PDZ1's binding cleft-whereas PDZ2 maintained remarkable structural conservation, indicating divergent evolutionary constraints on these tandem domains. Comparative analysis of isotropic B-factors and multistructure RMSD highlighted the limitations of B-factors alone and emphasized the value of multistructure comparisons for mapping dynamic landscapes. Molecular dynamics (MD) simulations implemented through GROMACS corroborate the crystallographic observations, showing elevated residue-specific fluctuation values in PDZ1's ligand-binding interface compared to analogous PDZ2 regions, and steady-state heteronuclear NOE measurements support enhanced loop flexibility in PDZ1 relative to PDZ2. Together, these findings indicate that PDZ1's conformational diversity represents an inherent biophysical property rather than a crystallographic artifact, suggest a functional division of labor in which PDZ1's structural plasticity enables broad ligand recognition via conformational selection while PDZ2's rigid architecture stabilizes the tandem domain arrangement, and provide an atomic-level framework for developing domain-selective therapeutics targeting syntenin-1 in cancer, viral infection, and neurodevelopmental disorders. - Source: PubMed
Ando NatsunoHanazono YuyaSakuma KoyaNumoto NobutakaHamajima RyuseiTenno TakeshiOshima AtsunoriIto NobutoshiHiroaki Hidekazu - Cytogenetics analysis of adipocytic tumours revealed varieties of chromosomal translocations beyond MDM2 amplification, so, this report aimed to identify these translocations and recognise the altered genes with their fusion partners. - Source: PubMed
Atta I SShafek S IAbdel-Hamid M