FLJ30934 Blocking Peptide
- Known as:
- FLJ30934 Blocking Peptide
- Catalog number:
- 33r-1323
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- FLJ30934 Blocking Peptide
Related genes to: FLJ30934 Blocking Peptide
- Gene:
- SNX32 NIH gene
- Name:
- sorting nexin 32
- Previous symbol:
- SNX6B
- Synonyms:
- FLJ30934
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2008-02-25
- Date modifiied:
- 2015-09-02
Related products to: FLJ30934 Blocking Peptide
Related articles to: FLJ30934 Blocking Peptide
- Most Alzheimer disease (AD) susceptibility genes have poorly understood roles in the central nervous system (CNS). To address this gap, we systematically characterized 100 conserved candidate AD risk genes using a cross-species strategy in the fruit fly, Drosophila melanogaster. Genes were prioritized based primarily on human functional genomic evidence. We generated custom loss-of-function alleles for each of the conserved fly orthologs. Most of the genes are expressed in the adult brain, including 24 neuron- and 13 glia-specific expression patterns. Overall, we identify 50 candidate AD risk gene homologs with requirements for CNS structure or function, including 18 whose loss of function causes neurodegeneration (e.g., Snx6/SNX32 and ClC-a/CLCN1), 35 required for neurophysiology (e.g., Arr1/ARRB2 and stai/STMN4), and eight with diminished CNS resilience following a thermal or mechanical stress (e.g., cindr/CD2AP and Amph/BIN1). In a parallel screen, we found 28 AD risk gene homologs (e.g., Ets98B/SPI1 and Yod1/YOD1) that modify the neurotoxicity of either amyloid-β peptide or tau protein, which aggregate to form AD pathology. To translate our findings back to human AD, we used oligogenic risk scores based on gene clusters with shared nervous system phenotypes in flies, pinpointing functional pathways that differentially drive AD risk. Our results-available online via the Alzheimer's Locus Integrative Cross-species Explorer portal-reveal nervous system requirements for dozens of AD risk genes and may enable dissection of causal heterogeneity in AD. - Source: PubMed
Publication date: 2025/10/29
Deger Jennifer MHannan Shabab BGu MingxueStrohlein Colleen EGoodman Lindsey DPasupuleti SasidharShaik ZahidMa LiwenLi YarongLi JiayangStephens Morgan CTyrlík MichalLiu ZhandongAl-Ramahi IsmaelBotas JuanShaw Chad AKanca OguzBellen Hugo JShulman Joshua M - Most Alzheimer's disease (AD) susceptibility genes have poorly understood roles in the central nervous system (CNS). To address this gap, we systematically characterized 100 conserved candidate AD risk genes using a cross-species strategy in the fruit fly, . Genes were prioritized based primarily on human functional genomic evidence. We generated custom, loss-of-function alleles for each of the conserved fly orthologs. Most of the genes (80%) are expressed in the adult brain, including 24 neuron- and 13 glia-specific expression patterns. Overall, we identify 50 candidate AD risk gene homologs with requirements for CNS structure or function, including 18 whose loss of function causes neurodegeneration (e.g., and ), 35 required for neurophysiology (e.g., /), and 8 with diminished CNS resilience following a thermal or mechanical stress (e.g., , ). In a parallel screen, we found 28 AD risk gene homologs (e.g, , ) that modify the neurotoxicity of either amyloid-β peptide or tau protein, which aggregate to form AD pathology. To translate our findings back to human AD, we developed and deployed oligogenic risk scores based on gene clusters with shared nervous system phenotypes in flies, pinpointing functional pathways that differentially drive AD risk. Our results-available online via the Alzheimer's Locus Integrative Cross-species Explorer (alice.nrihub.org)-reveal novel nervous system requirements for dozens of AD risk genes and may enable dissection of causal heterogeneity in AD. - Source: PubMed
Publication date: 2025/07/30
Deger Jennifer MHannan Shabab BGu MingxueStrohlein Colleen EGoodman Lindsey DPasupuleti SasidharShaik ZahidMa LiwenLi YarongLi JiayangStephens Morgan CTyrlík MichalLiu ZhandongAl-Ramahi IsmaelBotas JuanShaw Chad AKanca OguzBellen Hugo JShulman Joshua M - SNX32 is a member of the evolutionarily conserved Phox (PX) homology domain- and Bin/Amphiphysin/Rvs (BAR) domain- containing sorting nexin (SNX-BAR) family of proteins, which play important roles in sorting and membrane trafficking of endosomal cargoes. Although SNX32 shares the highest amino acid sequence homology with SNX6, and has been believed to function redundantly with SNX5 and SNX6 in retrieval of the cation-independent mannose-6-phosphate receptor (CI-MPR) from endosomes to the trans-Golgi network (TGN), its role(s) in intracellular protein trafficking remains largely unexplored. Here, we report that it functions in parallel with SNX1 in mediating epidermal growth factor (EGF)-stimulated postendocytic trafficking of the epidermal growth factor receptor (EGFR). Moreover, SNX32 interacts directly with EGFR, and recruits SNX5 to promote sorting of EGF-EGFR into multivesicular bodies (MVBs) for lysosomal degradation. Thus, SNX32 functions distinctively from other SNX-BAR proteins to mediate signaling-coupled endolysosomal trafficking of EGFR. - Source: PubMed
Wang DouZhao XiaWang PanpanLiu Jia-Jia - African swine fever virus (ASFV) causes a highly contagious and deadly disease in domestic pigs and European wild boars, posing a severe threat to the global pig industry. ASFV CP204L, a highly immunogenic protein, is produced during the early stages of ASFV infection. However, the impact of CP204L protein-interacting partners on the outcome of ASFV infection is poorly understood. To accomplish this, coimmunoprecipitation and mass spectrometry analysis were conducted in ASFV-infected porcine alveolar macrophages (PAMs). We have demonstrated that sorting nexin 32 (SNX32) is a CP204L-binding protein and that CP204L interacted and colocalized with SNX32 in ASFV-infected PAMs. ASFV growth and replication were promoted by silencing SNX32 and suppressed by overexpressing SNX32. SNX32 degraded CP204L by recruiting the autophagy-related protein Ras-related protein Rab-1b (RAB1B). RAB1B overexpression inhibited ASFV replication, while knockdown of RAB1B had the opposite effect. Additionally, RAB1B, SNX32, and CP204L formed a complex upon ASFV infection. Taken together, this study demonstrates that SNX32 antagonizes ASFV growth and replication by recruiting the autophagy-related protein RAB1B. This finding extends our understanding of the interaction between ASFV CP204L and its host and provides new insights into exploring the relationship between ASFV infection and autophagy.IMPORTANCEAfrican swine fever (ASF) is a highly contagious and acute hemorrhagic viral disease with a high mortality near 100% in domestic pigs. ASF virus (ASFV), which is the only member of the family , is a dsDNA virus of great complexity and size, encoding more than 150 proteins. Currently, there are no available vaccines against ASFV. ASFV CP204L represents the most abundantly expressed viral protein early in infection and plays an important role in regulating ASFV replication. However, the mechanism by which the interaction between ASFV CP204L and host proteins affects ASFV replication remains unclear. In this study, we demonstrated that the cellular protein SNX32 interacted with CP204L and degraded CP204L by upregulating the autophagy-related protein RAB1B. In summary, this study will help us understand the interaction mechanism between CP204L and its host upon infection and provide new insights for the development of vaccines and antiviral drugs. - Source: PubMed
Publication date: 2024/01/03
Yang WenpingLi LingxiaZhang JingWu JunhuangKang WeifangWang YueDing HaiyanLi DanZheng Haixue - Sorting nexins (SNX) are a family of proteins containing the Phox homology domain, which shows a preferential endo-membrane association and regulates cargo sorting processes. Here, we established that SNX32, an SNX-BAR (Bin/Amphiphysin/Rvs) sub-family member associates with SNX4 via its BAR domain and the residues A226, Q259, E256, R366 of SNX32, and Y258, S448 of SNX4 that lie at the interface of these two SNX proteins mediate this association. SNX32, via its PX domain, interacts with the transferrin receptor (TfR) and Cation-Independent Mannose-6-Phosphate Receptor (CIMPR), and the conserved F131 in its PX domain is important in stabilizing these interactions. Silencing of SNX32 leads to a defect in intracellular trafficking of TfR and CIMPR. Further, using SILAC-based differential proteomics of the wild-type and the mutant SNX32, impaired in cargo binding, we identified Basigin (BSG), an immunoglobulin superfamily member, as a potential interactor of SNX32 in SHSY5Y cells. We then demonstrated that SNX32 binds to BSG through its PX domain and facilitates its trafficking to the cell surface. In neuroglial cell lines, silencing of SNX32 leads to defects in neuronal differentiation. Moreover, abrogation in lactate transport in the SNX32-depleted cells led us to propose that SNX32 may contribute to maintaining the neuroglial coordination via its role in BSG trafficking and the associated monocarboxylate transporter activity. Taken together, our study showed that SNX32 mediates the trafficking of specific cargo molecules along distinct pathways. - Source: PubMed
Publication date: 2023/05/09
Sugatha JiniPriya AmulyaRaj PrateekJaimon EbsySwaminathan UmaJose AnjuPucadyil Thomas JohnDatta Sunando