Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Membrane fusion intermediates via directional and full assembly of the SNARE complex.

MPG-Autoren
/persons/resource/persons15219

Hernandez,  J. M.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15866

Stein,  A.
Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15710

Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14959

Cypionka,  A.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons59362

Farsi,  Z.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15985

Walla,  P. J.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15266

Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)

1479531.pdf
(Verlagsversion), 4MB

Ergänzendes Material (frei zugänglich)

1479531_SM.pdf
(Ergänzendes Material), 987KB

Zitation

Hernandez, J. M., Stein, A., Behrmann, E., Riedel, D., Cypionka, A., Farsi, Z., et al. (2012). Membrane fusion intermediates via directional and full assembly of the SNARE complex. Science, 336(6088), 1581-1584. doi:10.1126/science.1221976.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-000F-A228-9
Zusammenfassung
Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide–sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion.