TY - JOUR
T1 - α-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery
AU - Park, Yongsoo
AU - Vennekate, Wensi
AU - Yavuz, Halenur
AU - Preobraschenski, Julia
AU - Hernandez, Javier M.
AU - Riedel, Dietmar
AU - Walla, Peter Jomo
AU - Jahn, Reinhard
PY - 2014/6/6
Y1 - 2014/6/6
N2 - Neuronal exocytosis is mediated by soluble N-ethylmaleimidesensitive factor attachment protein receptor (SNARE) proteins. Before fusion, SNARE proteins form complexes bridging the membrane followed by assembly toward the C-terminal membrane anchors, thus initiating membrane fusion. After fusion, the SNARE complex is disassembled by the AAAATPase N-ethylmaleimide-sensitive factor that requires the cofactor α-SNAP to first bind to the assembled SNARE complex. Using chromaffin granules and liposomes we now show that α-SNAP on its own interferes with the zippering of membraneanchored SNARE complexes midway through the zippering reaction, arresting SNAREs in a partially assembled transcomplex and preventing fusion. Intriguingly, the interference does not result in an inhibitory effect on synaptic vesicles, suggesting that membrane properties also influence the final outcome of α-SNAP interference with SNARE zippering. We suggest that binding of α-SNAP to the SNARE complex affects the ability of the SNARE complex to harness energy or transmit force to the membrane.
AB - Neuronal exocytosis is mediated by soluble N-ethylmaleimidesensitive factor attachment protein receptor (SNARE) proteins. Before fusion, SNARE proteins form complexes bridging the membrane followed by assembly toward the C-terminal membrane anchors, thus initiating membrane fusion. After fusion, the SNARE complex is disassembled by the AAAATPase N-ethylmaleimide-sensitive factor that requires the cofactor α-SNAP to first bind to the assembled SNARE complex. Using chromaffin granules and liposomes we now show that α-SNAP on its own interferes with the zippering of membraneanchored SNARE complexes midway through the zippering reaction, arresting SNAREs in a partially assembled transcomplex and preventing fusion. Intriguingly, the interference does not result in an inhibitory effect on synaptic vesicles, suggesting that membrane properties also influence the final outcome of α-SNAP interference with SNARE zippering. We suggest that binding of α-SNAP to the SNARE complex affects the ability of the SNARE complex to harness energy or transmit force to the membrane.
UR - http://www.scopus.com/inward/record.url?scp=84902136636&partnerID=8YFLogxK
U2 - 10.1074/jbc.M114.556803
DO - 10.1074/jbc.M114.556803
M3 - Article
C2 - 24778182
AN - SCOPUS:84902136636
SN - 0021-9258
VL - 289
SP - 16326
EP - 16335
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 23
ER -