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Last update 08 May 2025

SNAP23

Last update 08 May 2025

Basic Info

Synonyms

HsT17016, SNAP-23, SNAP23

+ [5]

Introduction

Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.

Drugs associated with SNAP23

MF-286

Target

SNAP23

Mechanism

SNAP23 inhibitors

Active Org.

Osaka University

Originator Org.

Osaka University

Active Indication

Diabetes Mellitus

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SNAP23

100 Translational Medicine associated with SNAP23

0 Patents (Medical) associated with SNAP23

492

Literatures (Medical) associated with SNAP23

01 Apr 2025·Computational Biology and Chemistry

Drug repositioning in castration-resistant prostate cancer using systems biology and computational drug design techniques

Article

Author: Jamialahmadi, Khadijeh ; Aghaee-Bakhtiari, Seyed Hamid ; Bazyari, Mohammad Javad ; Rafiee, Javad

BACKGROUND AND OBJECTIVECastration-resistant prostate cancer (CRPC) is caused by resistance to androgen deprivation treatment and leads to the death of patients and there is almost no chance of survival. Therefore, finding a cure to overcome CRPC is challenging and important, but discovering a new drug is very time-consuming and expensive. To overcome these problems, we used Drug repositioning (drug repurposing) strategy in this study.METHODSGene expression data of CRPC and primary prostate samples were extracted from the GEO database to identify DEGs. Pathway enrichment was performed to find the role of DEGs in signaling pathways. To identify hub proteins, the PPI network was reconstructed and analyzed. drug candidates were identified and to select the most effective drug, molecular docking analysis, and molecular dynamics simulation were performed. Then MTT and qRT-PCR tests were performed to check the effectiveness of the selected drug.RESULTSA total of 152 upregulated DEGs and 343 downregulated DEGs were identified, and after PPI network analysis, IKBKB, SNAP23, MYC, and NOTCH1 genes were introduced as hubs. drug candidates for IKBKB were identified and by examining the results of docking screening and molecular dynamics, sulfasalazine was selected as the most effective drug. Laboratory analyses proved the effectiveness of this drug and a decrease in the expression of all target genes was observed.CONCLUSIONIn this study, IKBKB key protein were identified in CRPC, and sulfasalazine was selected as a suitable candidate for drug repositioning and its effectiveness was confirmed through tests.

01 Mar 2025·Molecular Therapy Methods & Clinical Development

Identification of the role of SNARE proteins in rAAV vector production through interaction with the viral MAAP

Article

Author: Zhang, Xiujuan ; Hao, Siyuan ; Ning, Kang ; Qiu, Jianming ; McFarlin, Shane ; Kuz, Cagla Aksu ; Cheng, Fang

Adeno-associated virus (AAV) expresses a membrane-associated accessory protein (MAAP), a small nonstructural protein, that facilitates AAV secretion out of the plasma membrane through an association with extracellular vesicles during AAV egress. Here, we investigated the host proteins that interact with AAV2 MAAP (MAAP2) using APEX2-mediated proximity labeling. We identified two SNARE proteins, Syntaxin 7 (STX7) and synaptosome-associated protein 23 (SNAP23), a vesicle (v-)SNARE and a target (t-)SNARE, respectively, that mediate intracellular trafficking of membrane vesicles aand exhibited associations with MAAP2 in HEK293 cells. We found that MAAP2 indirectly interacted with STX7 or SNAP23, and that the knockout of STX7 or SNAP23 not only enhanced rAAV secretion into the media but also increased total vector yield during rAAV vector production in HEK293 cells. Thus, our study revealed a practical approach for producing higher yields of rAAV vectors from the media, easing downstream processes in rAAV manufacturing.

01 Feb 2025·American Journal of Physiology-Cell Physiology

Syntaxin 4-enhanced plasma membrane repair is independent of dysferlin in skeletal muscle

Article

Author: Chen, Hsin-Yu ; Michele, Daniel E

Dysferlin, a crucial Ca2+-binding protein in plasma membrane repair (PMR), shares homology with synaptotagmin, which binds Ca2+ and regulates SNARE-mediated vesicle fusion in neurons. Dysferlin was thus hypothesized to function as synaptotagmin in PMR. We demonstrate here that the activity of SNAREs is important for PMR, and overexpression of STX4 enhances PMR in both intact and dysferlin-deficient skeletal muscle. These data suggest that SNARE-mediated PMR may be independent of dysferlin in skeletal muscle.

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SNAP23

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