STX4

Protein-coding gene in the species Homo sapiens
title: "STX4" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/STX4" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0
::summary Protein-coding gene in the species Homo sapiens ::
Syntaxin-4 is a protein that in humans is encoded by the STX4 gene.
Interactions
STX4 has been shown to interact with:
- Gelsolin,
- NAPA,
- RAB4A,
- SNAP-25,
- SNAP23,
- STXBP1,
- STXBP5,
- Syntaxin binding protein 3,
- TXLNB,
- VAMP2,
- VAMP3, and
- Vesicle-associated membrane protein 8.
References
References
- (Jun 1994). "Isolation and sequence analysis of the human syntaxin-encoding gene". Gene.
- (Feb 2006). "Syntaxins 3 and 4 are concentrated in separate clusters on the plasma membrane before the establishment of cell polarity". Molecular Biology of the Cell.
- "Entrez Gene: STX4 Syntaxin 4".
- (January 2012). "Gelsolin associates with the N terminus of syntaxin 4 to regulate insulin granule exocytosis". Molecular Endocrinology.
- (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature.
- (Feb 2001). "Direct interaction of Rab4 with syntaxin 4". The Journal of Biological Chemistry.
- (Jun 1995). "A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic". The Journal of Biological Chemistry.
- (Jun 1996). "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues". The Journal of Biological Chemistry.
- (Apr 1999). "Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion". Blood.
- (Dec 1998). "Three novel proteins of the syntaxin/SNAP-25 family". The Journal of Biological Chemistry.
- (Aug 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Archives of Oral Biology.
- (May 2003). "Syntaxin isoform specificity in the regulation of renal H+-ATPase exocytosis". The Journal of Biological Chemistry.
- (May 1997). "Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c". Biochemical and Biophysical Research Communications.
- (Jun 2000). "Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment". Journal of Immunology.
- (Mar 2000). "Role of SNAP23 in insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2". The Journal of Biological Chemistry.
- (Apr 2003). "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain". The Journal of Biological Chemistry.
- (Aug 2003). "A role for Sec1/Munc18 proteins in platelet exocytosis". The Biochemical Journal.
- (Sep 2003). "Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation". The Journal of Biological Chemistry.
- (Jul 2004). "Identification and characterization of taxilin isoforms". Biochemical and Biophysical Research Communications.
- (Jan 2003). "Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils". Journal of Immunology.
- (Aug 1996). "Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2". The Biochemical Journal.
- (Aug 2002). "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion". Blood.
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