Ask about this productRelated genes to: Snap29 Blocking Peptide
- Gene:
- SNAP29 NIH gene
- Name:
- synaptosome associated protein 29
- Previous symbol:
- -
- Synonyms:
- SNAP-29, CEDNIK
- Chromosome:
- 22q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-17
- Date modifiied:
- 2016-06-01
Related products to: Snap29 Blocking Peptide
Related articles to: Snap29 Blocking Peptide
- To investigate the effects of Mucin 1 (MUC1) in human triple-negative breast cancer MDA-MB-231cells, the MDA-MB-231 cell line with MUC1 knockout (231-MUC1-KO) was constructed by CRISPR/Cas9 gene editing. Cell proliferation was evaluated using EDU and colony formation assays, and cell migration and invasion were detected by transwell assay. Autophagy flow was assessed by western blot and Ad-mCherry-GFP-LC3B dual-fluorescence system and validated by lysosome inhibitor barfimycin A1 and autophagy inducer rapamycin. Key proteins of autophagosomes and lysosomal fusion (STXl7, SNAP29) and lysosomal tagged protein (LAMP1) were detected by western blot, and lysosomal pH was evaluated by Lysotracker Red fluorescence. MUC1 expression was low in human normal breast epithelial cells MCF-10A, but was highly expressed in human MDA-MB-231 cells and tissues. Successful MUC1 knockout was confirmed by gene sequencing, RT-qPCR, and western blot. Loss of MUC1 gene expression in 231-MUC1-KO significantly reduced proliferation, migration, and invasion. Compared with the control group, MUC1 knockout led to a significant increase of autophagy-related proteins LC3-II and p62, which is consistent with the effect of lysosome inhibitor bleomycin A1. After adding the autophagy inducer rapamycin, compared with the control group, the accumulation of LC3-II and p62 proteins also further increased. The expression level of LAMP1 was downregulated and the lysosome pH increased, but the expression levels of STXl7 and SNAP29 were not affected. These findings suggest that MUC1 promotes malignant behaviors in MDA-MB-231 cells by regulating autophagic flow, likely through lysosomal dysfunction-mediated autophagy blockade. - Source: PubMed
Publication date: 2026/04/27
Huang ZhimeiZhao JiayaoZhang QinqinLuo YuChen WenqingLiu ZhengchunLiu Xiuli - Emerging evidence implicates premature placental senescence as a central driver of pregnancy complications, though its underlying mechanisms remain elusive. Here, we report marked downregulation of IL33 (interleukin 33) in villi from unexplained recurrent pregnancy loss (URPL) patients, concomitant with elevated trophoblast senescence. More importantly, knockout mice exhibited placental senescence and impaired trophoblast invasion. Mechanistically, senescent trophoblasts displayed metabolic dysregulation - including enhanced glycolysis and lactate accumulation - which disrupted macroautophagic/autophagic flux and mitochondrial function. Lactate-induced lysine lactylation at residue K169 of SNAP29 (synaptosome associated protein 29) promoted its degradation, impairing macroautophagy/autophagy and trophoblast function, ultimately driving pregnancy loss. In interventional studies, senotherapies with metformin or dasatinib plus quercetin restored placental development and improved pregnancy outcomes in both IL33-deficient and inflammation-induced miscarriage models. Our findings establish the IL33-senescence-lactate axis as a critical pathway in URPL pathogenesis and support senomodulation as a therapeutic strategy.: 2-DG: 2-deoxy-D-glucose; BafA1: bafilomycin A1; CHX: cycloheximide; CTB: cytotrophoblasts; D-gal: D-galactose; EVT: extravillous trophoblasts; HDAC: histone deacetylase; H2O2: hydrogen peroxide; IL33: Interleukin 33; LPS: lipopolysaccharide; SA-GLB1/β-gal: senescence-associated galactosidase beta 1; SASP: senescence-associated secretory phenotype; SNAP29: synaptosome associated protein 29; STB: syncytiotrophoblasts; UMAP: uniform manifold approximation and projection; URPL: unexplained recurrent pregnancy loss; VP: etoposide. - Source: PubMed
Publication date: 2026/04/22
Lu Jia-JingSheng Yan-RanHu Wen-TingLiu Yu-KaiXie FengLi Ming-QingZhu Xiao-Yong - Many poxviruses are significant zoonotic pathogens threatening public health. Autophagy, a regulated process vital for cellular homeostasis, can participate in defense against virus invasion. However, the relationship between poxviruses and host cell autophagy is not fully understood. This study shows that vaccinia virus (VACV) induces autophagy but blocks autophagosome-lysosome fusion. Modified vaccinia virus Ankara (MVA), an attenuated VACV strain that cannot replicate in most mammalian cells, fails to do so. Both pharmacological inhibition of early autophagy via 3-MA treatment and genetic ablation of ATG3 and ATG7 led to a significant enhancement of MVA replication. The VACV protein A52 inhibits autolysosome formation by disrupting interactions between SNAP29, STX17, and VAMP8, which is crucial for autophagic flux. Importantly, A52 also promotes the degradation of SNAP29, thereby aiding viral replication. Furthermore, SNAP29 is a newly identified host restriction factor for MVA, as its suppression enables MVA replication in human cells. These findings elucidate how poxviruses modulate autophagy for their own replication and further explain MVA's restriction in human cells. - Source: PubMed
Publication date: 2026/04/13
Niu KangFang YongxiangDeng YiningWang ZiyueXie ShijieZhu JundaSong BaifenWu WenxueJing ZhizhongPeng Chen - The chronic accumulation of ΔFosB in striatal medium spiny neurons has been implicated as a pivotal contributor to the pathogenesis of levodopa-induced dyskinesia (LID). While recent studies have implicated autophagy in the degradation of ΔFosB and the amelioration of LID, the precise mechanisms remain elusive. We induced LID in a unilateral 6-hydroxydopamine-lesioned parkinsonism rat model via chronic levodopa treatment. To modulate the autophagy pathway, we overexpressed ATG14 in the striatum of LID rats and administered chloroquine, an autophagy inhibitor, peripherally. We assessed LID severity using abnormal involuntary movements (AIMs) scores. Western blotting, real-time quantitative polymerase chain reaction, immunofluorescence, immunohistochemistry, transmission electron microscopy, and Golgi staining were employed to measure autophagy flux, synaptic alterations, and ΔFosB levels. Chronic levodopa treatment reduced ATG14 and SNARE complex (STX17, SNAP29, and VAMP8) levels, disrupted their interaction, impaired autophagy flux, affected synaptic function, and led to ΔFosB accumulation in the striatum of PD rats. Upregulating ATG14 in the striatum of LID rats improved AIMs scores, facilitated SNARE-mediated autophagosome-lysosome fusion, restored synaptic deficits, and promoted ΔFosB degradation. However, these beneficial effects of ATG14 upregulation were negated by chloroquine administration. Our findings suggest that upregulating ATG14 enhances SNARE formation, promoting autophagy flux and thereby reducing LID occurrence by facilitating ΔFosB degradation. - Source: PubMed
Wu YiLiu KeZhang ZhaoyuanMa ZhuoranTang ZhichengChang AnOuyang HaoxuanZhai HengCao XuebingXu Yan - T-2 toxin is a persistent, bioaccumulative environmental contaminant that poses major health threats to humans and animals. Endoplasmic reticulum (ER) stress and autophagy are two interconnected stress responses critical for maintaining cellular homeostasis. Berbamine (BBM) is an important member of bis-benzy lisoquinoline alkaloid with diverse biological activities. This study aimed to identify the molecular target of BBM against T-2 toxin-induced hepatotoxicity, focusing on autophagy-ER stress crosstalk. We systematically evaluated autophagy and ER stress in human HepaRG cells using immunoblotting, transmission electron microscopy and an autophagy reporter assay. T-2 toxin was found to concurrently activate PINK1/Parkin-mediated mitophagy and suppress Keap1-mediated FAM134B ubiquitination-dependent ER-phagy, thereby triggering ER stress. Integrated evidence from molecular dynamics and western blot demonstrated that BBM upregulated and stabilized BNIP3, blocking the VAMP8-SNAP29 interaction to inhibit T-2 toxin-induced autophagy and subsequent ER stress. Moreover, in vivo mouse experiments demonstrated that 30 mg/kg BBM significantly alleviated T-2 toxin-induced liver injury by suppressing both autophagic flux and ER stress; BBM significantly reduced serum levels of liver enzymes, ALT, and AST. Collectively, our findings elucidate a novel mechanism wherein T-2 toxin-induced mitophagy inhibits ER-phagy to drive ER stress-mediated liver injury and highlight the therapeutic potential of BBM in alleviating T-2 toxin-induced liver injury. - Source: PubMed
Publication date: 2026/03/06
Xu QiangDeng LuyuXu JintaoWu ZhikaiLin RuqinDeng YiqunWen Jikai