The nature of the Syntaxin4 C-terminus affects Munc18c-supported SNARE assembly

Vesicular transport of cellular cargo requires targeted membrane fusion and formation of a SNARE protein complex that draws the two apposing fusing membranes together. Insulin-regulated delivery and fusion of glucose transporter-4 storage vesicles at the cell surface is dependent on two key proteins...

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Veröffentlicht in:	PloS one 2017-08, Vol.12 (8), p.e0183366-e0183366
Hauptverfasser:	Rehman, Asma, Hu, Shu-Hong, Tnimov, Zakir, Whitten, Andrew E, King, Gordon J, Jarrott, Russell J, Norwood, Suzanne J, Alexandrov, Kirill, Collins, Brett M, Christie, Michelle P, Martin, Jennifer L
Format:	Artikel
Sprache:	eng
Schlagworte:	Biology Biology and Life Sciences C-Terminus Cargo Cell surface Complex formation Crystal structure Experimental design Genetic aspects Glucose metabolism Glucose transporter In vitro methods and tests Insulin Integral membrane proteins Lysozyme Medicine Membrane fusion Membrane proteins Membranes Micelles Munc18 Proteins - metabolism Physical Sciences Physiological aspects Protein Binding Proteins Qa-SNARE Proteins - chemistry Qa-SNARE Proteins - metabolism Research and Analysis Methods SNAP receptors SNARE Proteins - metabolism
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