STX7

Last update 08 May 2025

Basic Info

Synonyms

STX7, syntaxin 7, Syntaxin-7

Introduction

May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes.

100 Clinical Results associated with STX7

100 Translational Medicine associated with STX7

0 Patents (Medical) associated with STX7

104

Literatures (Medical) associated with STX7

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.

02 Jan 2025·Autophagy

GORASP2 promotes phagophore closure and autophagosome maturation into autolysosomes

Article

Author: Zhang, Xing ; Zhao, Xiaodan ; Wang, Yijie ; Zhang, Zhenqian ; Zhang, Yue ; Huang, Lei ; Fu, Tingting ; Zhang, Xiaoyan ; Jian, Yannan ; Xing, Yusheng

As the central hub of the secretory pathway, the Golgi apparatus plays a crucial role in maintaining cellular homeostasis in response to stresses. Recent studies have revealed the involvement of the Golgi tether, GORASP2, in facilitating autophagosome-lysosome fusion by connecting LC3-II and LAMP2 during nutrient starvation. However, the precise mechanism remains elusive. In this study, utilizing super-resolution microscopy, we observed GORASP2 localization on the surface of autophagosomes during glucose starvation. Depletion of GORASP2 hindered phagophore closure by regulating the association between VPS4A and the ESCRT-III component, CHMP2A. Furthermore, we found that GORASP2 controls RAB7A activity by modulating its GEF complex, MON1A-CCZ1, thereby impacting RAB7A's interaction with the HOPS complex. The assembly of both STX17-SNAP29-VAMP8 and YKT6-SNAP29-STX7 SNARE complexes was also attenuated without GORASP2. These findings suggest that GORASP2 helps seal autophagosomes and activate the RAB7A-HOPS-SNAREs membrane fusion machinery for autophagosome maturation, highlighting its membrane tethering function in response to stresses.Abbreviations: BafA1: bafilomycin A₁; ESCRT: endosomal sorting complex required for transport; FPP: fluorescence protease protection; GEF: guanine nucleotide exchange factor; GFP: green fluorescent protein; GORASP2: golgi reassembly stacking protein 2; GSB: glucose starvation along with bafilomycin A₁; HOPS: homotypic fusion and protein sorting; LAMP2: lysosomal associated membrane protein 2; MAP1LC3B: microtubule associated protein 1 light chain 3 beta; PBS: phosphate-buffered saline; PtdIns3K: phosphatidylinositol 3-kinase; PtdIns3P: phosphatidylinositol-3-phosphate; PK: proteinase K; SNARE: soluble N-ethylmaleimide-sensitive factor attachment protein receptor; SIM: structured illumination microscopy; UVRAG: UV radiation resistance associated.

01 Dec 2024·Diabetes

Optimized Proteomic Analysis of Insulin Granules From MIN6 Cells Identifies Scamp3, a Novel Regulator of Insulin Secretion and Content

Article

Author: Webster, Hayley ; Norris, Nicholas ; Kebede, Melkam A. ; Thomas, Helen E. ; Larance, Mark ; Loudovaris, Thomas ; Yau, Belinda ; Senior, Alistair M. ; Famularo, Carlo

Pancreatic β-cells in the islets of Langerhans are key to maintaining glucose homeostasis by secreting the peptide hormone insulin. Insulin is packaged within vesicles named insulin secretory granules (ISGs), which recently have been considered to have intrinsic structures and proteins that regulate insulin granule maturation, trafficking, and secretion. Previously, studies have identified a handful of novel ISG-associated proteins, using different separation techniques. The present study combines an optimized ISG isolation technique and mass spectrometry–based proteomics, with an unbiased protein correlation profiling and targeted machine-learning approach to uncover 211 ISG-associated proteins with confidence. Four of these proteins, syntaxin-7, synaptophysin, synaptotagmin-13, and Scamp3 have not been previously associated with ISG. Through colocalization analysis of confocal imaging, we validate the association of these proteins to the ISG in MIN6 and human β-cells. We further validate the role for one (Scamp3) in regulating insulin content and secretion from β-cells for the first time. Scamp3 knockdown INS-1 cells have reduced insulin content and dysfunctional insulin secretion. These data provide the basis for future investigation of Scamp3 in β-cell biology and the regulation of insulin secretion.Article Highlights

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STX7

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