The membrane-dipped neuronal SNARE complex: a site-directed spin labeling electron paramagnetic resonance study.
The formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex is an essential process for membrane fusion and the neurotransmitter release in neurons. As an initial step toward the determination of the membrane topology of the SNARE complex, residues at the membrane-water interface were investigated with site-specific spin labeling electron paramagnetic resonance. EPR analysis revealed that the basic amino acid-rich interfacial region, which is universal for all transmembrane SNARE proteins, inserts into the membrane, eliminating the gap between the core complex and the membrane. The result raises the possibility that core complex formation directly leads to the apposition of two membranes, which could facilitate membrane fusion.
Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
Dae-Hyuk
DH
Kweon
Chang Sup
CS
Kim
Yeon-Kyun
YK
Shin
D000595:Amino Acid Sequence; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry*; D009474:Neurons / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D050600:SNARE Proteins; D013113:Spin Labels; D033921:Vesicular Transport Proteins
D008565:Membrane Proteins; D011994:Recombinant Proteins; D050600:SNARE Proteins; D013113:Spin Labels; D033921:Vesicular Transport Proteins