Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1861, Issue 3, Pages 677-684Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2018.12.019
Keywords
Exocytosis; Membrane fusion; Protein palmitoylation; Secretion
Categories
Funding
- UCSD/UCLA NIDDK (National Institute of Diabetes and Digestive and Kidney Diseases
- USA) Diabetes Research Center [P30 DK063491]
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Abundant attention has focused on synaptotagmin's C2 domains, but less is known about the structure and function of its other regions. Here, we synthesized the N-acetylated, C-end amidated and Cys-palmitated peptide (VLTCCFCICK KCLFKKKNKK K) which includes the fatty acylated cysteine residues in the membrane-affiliated domain of synaptotagmin-1. Fourier-transform infrared spectrometry indicated that this peptides conformation is influenced by environmental polarity. In artificial bilayer membranes, this peptide exhibited abundant beta-structure. Electron microscopy revealed that this peptide also promoted the stacking of liposome membranes. Together these results suggest that the fatty acylated region of synaptotagmin-1 is likely to adopt beta-structure in biological membranes. This preference for beta-structure versus alpha-helix has functional implications for the role of synaptotagmin-1 in synaptic vesicle exocytosis.
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