Abdulreda Midhat H, Bhalla Akhil, Chapman Edwin R, Moy Vincent T
University of Miami Miller School of Medicine, Physiology and Biophysics Department, Miami, Florida 33136, USA.
Biophys J. 2008 Jan 15;94(2):648-55. doi: 10.1529/biophysj.107.114298. Epub 2007 Sep 14.
This study investigated the effect of soluble N-ethylmaleimide-sensitive factor-attachment protein (SNAP) receptors (SNAREs) on the fusion of egg L-alpha-phosphatidylcholine bilayers using atomic force microscope (AFM) spectroscopy. AFM measurements of the fusion force under compression were acquired to reveal the energy landscape of the fusion process. A single main energy barrier governing the fusion process was identified in the absence and presence of SNAREs in the bilayers. Under compression, a significant downward shift in the fusion dynamic force spectrum was observed when cognate v- and t-SNAREs were present in the opposite bilayers. The presence of vesicle-associated membrane protein (VAMP) and binary syntaxin and SNAP 25 in the apposed bilayers resulted in a reduction in the height of the activation potential by approximately 1.3 k(B)T and a >2-fold increase in the width of the energy barrier. The widening of the energy barrier in the presence SNAREs is interpreted as an increase in the compressibility of the membranes, which translates to a greater ease in the bilayer deformation and subsequently the fusion of the membranes under compression. Facilitation of membrane fusion was observed only when SNAREs were present in both bilayers. Moreover, addition of the soluble cytoplasmic domain of VAMP, which interferes with the interaction between opposing v- and t-SNAREs, prevented such facilitation. These observations implicated the interaction between the cytoplasmic domains of opposing SNAREs in the observed fusion facilitation, possibly by destabilizing the bilayers through pulling on their transmembrane segments. Our AFM compression measurements revealed that SNARE-mediated membrane fusion proceeded through a sequence of two approximately 5 nm collapses of the membrane, an observation that is consistent with the existence of a hemifused state during the fusion process.
本研究利用原子力显微镜(AFM)光谱研究了可溶性N-乙基马来酰亚胺敏感因子附着蛋白(SNAP)受体(SNAREs)对卵L-α-磷脂酰胆碱双层膜融合的影响。通过AFM测量压缩下的融合力,以揭示融合过程的能量态势。在双层膜中不存在和存在SNAREs的情况下,均确定了一个控制融合过程的单一主要能量屏障。在压缩过程中,当同源的v-SNARE和t-SNARE存在于相对的双层膜中时,观察到融合动力谱有显著的向下移动。相对双层膜中存在囊泡相关膜蛋白(VAMP)、二元突触融合蛋白和SNAP 25,导致激活电位的高度降低约1.3k(B)T,能量屏障的宽度增加超过2倍。存在SNAREs时能量屏障变宽被解释为膜的可压缩性增加,这意味着在压缩下双层膜更容易变形,进而更容易融合。仅当两个双层膜中都存在SNAREs时才观察到膜融合的促进作用。此外,添加干扰相对的v-SNARE和t-SNARE之间相互作用的VAMP可溶性胞质结构域可阻止这种促进作用。这些观察结果表明,相对SNAREs的胞质结构域之间的相互作用参与了所观察到的融合促进过程,可能是通过拉动跨膜片段使双层膜不稳定来实现的。我们的AFM压缩测量结果表明,SNARE介导的膜融合通过膜的两个约5nm的塌陷序列进行,这一观察结果与融合过程中半融合状态的存在一致。