Ask about this productRelated genes to: SNAP25 antibody
- Gene:
- SNAP25 NIH gene
- Name:
- synaptosome associated protein 25
- Previous symbol:
- SNAP
- Synonyms:
- SNAP-25, RIC-4, RIC4, SEC9, bA416N4.2, dJ1068F16.2
- Chromosome:
- 20p12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-01-24
- Date modifiied:
- 2016-10-05
Related products to: SNAP25 antibody
Related articles to: SNAP25 antibody
- Current proteomic analyses of presynaptic compartments largely rely on synaptosome fractions prepared from whole brain or dissected brain regions. However, the accurate identification of proteins that are truly enriched at presynaptic sites is limited by the purification efficiency and the intrinsic heterogeneity of synaptosome preparations. Alternative approaches that achieve higher spatial specificity are therefore required. Here, we established an in situ proximity biotinylation platform based on APEX2 to profile the proteomes of presynaptic boutons and their neighboring axons in living neurons. In cultured hippocampal neurons, presynaptic boutons were selectively labeled using APEX2-Synapsin 1, whereas axonal regions including presynaptic boutons were labeled using APEX2-SNAP-25, enabling compartment-resolved proteomic comparison. Through quantitative mass spectrometry and systematic analysis, we selected approximately 500 proteins that are preferentially enriched in boutons relative to axons. This bouton-enriched proteome includes canonical synaptic vesicle proteins and well-characterized active zone components, validating the spatial specificity of the approach. In addition, it reveals protein clusters suggestive of specialized signaling pathways related to ATP production and protein degradation, indicating previously underappreciated metabolic and proteostatic specialization enriched in presynaptic terminals. Together, our dataset provides a resource for the study of synaptic function under physiological and pathological conditions and establishes a generalizable strategy for spatially resolved proteomic analysis of neuronal subcompartmentation. - Source: PubMed
Publication date: 2026/05/13
Nakazawa KeitaTaoufiq ZacharieKakuda NobutoGoda YukikoTakamori Shigeo - Tumor-secreted exosomes are essential in driving tumor progression by releasing multivesicular bodies (MVBs), which are endosome organelles containing intraluminal vesicles (ILVs), as exosomes. However, the mechanisms controlling MVB biosynthesis, trafficking, and exosome exocytosis are not fully understood. - Source: PubMed
Publication date: 2026/05/12
Bai SuwenSun HexingLiu RongZhang WenjunWei YuanLuo YumeiWang MinghuaWu JingChan David WDu Juan - In this study, we thoroughly investigated the potential mechanisms underlying the therapeutic effects of Botulinum Toxin Type A (BoNT-A) on ameliorating pruritic behavior and allodynia in a murine model of atopic dermatitis (AD). Recognizing the pivotal role of mast cells in AD pathogenesis, we hypothesized that BoNT-A inhibits mast cell degranulation via the cleavage of SNAP-25. Using P815 cells and primary mast cells, we confirmed the expression of SNAP-25 and SV2, and through siRNA-mediated knockdown, we validated that SNAP-25 is a pivotal mediator of mast cell degranulation and the specific target required for BoNT-A' s inhibitory action. In our in vivo experiments utilizing MC903-induced AD mice, we observed that BoNT-A administration significantly reduced scratching bouts and alleviated pruritus allodynia while decreasing mast cell recruitment in both epidermal and dermal layers. Furthermore, to elucidate the involvement of the central nervous system, we constructed a BoNT-A/FITC complex and demonstrated that the toxin undergoes retrograde transport from peripheral nerves to the spinal cord dorsal horn. Therefore, it appears to exert an antipruritic effect by downregulating the expression of pruritus-related ion channels and neuropeptides, specifically TRPV1 and CGRP. Consequently, our findings establish that BoNT-A exerts its therapeutic effects through a dual mechanism: peripherally by inhibiting mast cell degranulation via the SNAP-25/SV2 pathway, and centrally by modulating neurogenic inflammation within the spinal cord, thus providing a novel perspective for the treatment of allergic diseases. - Source: PubMed
Publication date: 2026/05/07
Lan Ya-AnGuo Jia-XiYao Min-HuaZhang Xiao-YuLiao Zi-RuiZhang Ruo-HuiJing Yu-Hong - Protein-protein interactions (PPIs) underpin most cellular processes, and disruptions to these interactions can lead to cellular dysfunction and disease. Understanding PPIs is essential for studying disease mechanisms, yet traditional experimental approaches are time- and labor-intensive. Recent advances in AI-based structural prediction tools, including AlphaFold2 and RoseTTAFold2, now enable efficient exploration of potential PPIs. To develop an integrated and practical multi-tool system for PPI investigation, we present a dual-arm computational pipeline centered on the ZWINT (SIP30) kinetochore protein, which we identified as a key gene in neuropathic signaling. The first arm of the workflow generates PPI models using AlphaFold2 and RoseTTAFold2 and evaluates model consistency using TM-Align. The second arm assesses binding affinity by identifying interface residues with PyMOL and calculating docking scores with HADDOCK. Together, these methods provide both quantitative and qualitative evaluations of candidate PPIs. Using this framework, we examined three established interactors (SNAP25, CAMK2A, UBC) and four exploratory proteins (STX1A, VCP, BLOC1S2, ARC) in combination with ZWINT. This study demonstrates that AI-supported analysis can streamline PPI discovery by prioritizing biologically plausible interactors and guiding downstream experimental validation. - Source: PubMed
Publication date: 2026/04/30
Abdelfattah NoraBroncales BridgetAlbert IvanaKohan JaimeeYu Lei - Aging is the primary risk factor for sporadic Alzheimer's disease (AD). While amyloid-beta oligomers (AβOs) accumulation is a key neuropathological process in AD, their specific effects in aged brains and how aging modulates brain response to AβOs remains poorly understood. We investigated how aging contributes to AβO-induced neurotoxicity and cognitive deficits in mice. - Source: PubMed
Publication date: 2026/05/02
Allouche AhmadColin JulieBirck CatherineSchroeder HenriTallandier ValentinBaldoni MarionMuller ChristopheAfrassi MohamedViolle Nicolas