A reduced SNARE model for membrane fusion.
نویسندگان
چکیده
Let's get together: A minimal model system was developed to mimic the SNARE-protein-mediated fusion of biological membranes (see picture). Fusion between two populations of liposomes is controlled by a pair of complementary lipidated oligopeptides that form noncovalent coiled-coil complexes and thereby force the membranes into close proximity to promote fusion. The model system displays the key characteristics of in vivo fusion events.
منابع مشابه
SNARE derived peptide mimic inducing membrane fusionw
Membrane fusion is a central cellular process in eukaryotic cells. In the secretory pathway connecting organelles between the endoplasmic reticulum and the plasma membrane, fusion is mediated by sets of SNARE proteins ( soluble N-ethylmaleimide-sensitive factor attachment r eceptor). 1 Complementary sets of SNARE proteins are associated with the respective membranes. Upon contact, the SNAREs fo...
متن کاملModel of SNARE-Mediated Membrane Adhesion Kinetics
SNARE proteins are conserved components of the core fusion machinery driving diverse membrane adhesion and fusion processes in the cell. In many cases micron-sized membranes adhere over large areas before fusion. Reconstituted in vitro assays have helped isolate SNARE mechanisms in small membrane adhesion-fusion and are emerging as powerful tools to study large membrane systems by use of giant ...
متن کاملSec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.
Intracellular membrane fusion requires SNARE proteins in a trans-complex, anchored to apposed membranes. Proteoliposome studies have suggested that SNAREs drive fusion by stressing the lipid bilayer via their transmembrane domains (TMDs), and that SNARE complexes require a TMD in each docked membrane to promote fusion. Yeast vacuole fusion is believed to require three Q-SNAREs from one vacuole ...
متن کاملSynaptotagmin-1 utilizes membrane bending and SNARE binding to drive fusion pore expansion.
In regulated vesicle exocytosis, SNARE protein complexes drive membrane fusion to connect the vesicle lumen with the extracellular space. The triggering of fusion pore formation by Ca(2+) is mediated by specific isoforms of synaptotagmin (Syt), which employ both SNARE complex and membrane binding. Ca(2+) also promotes fusion pore expansion and Syts have been implicated in this process but the m...
متن کاملDeterminants of Synaptobrevin Regulation in Membranes□D
Neuronal exocytosis is driven by the formation of SNARE complexes between synaptobrevin 2 on synaptic vesicles and SNAP-25/syntaxin 1 on the plasma membrane. It has remained controversial, however, whether SNAREs are constitutively active or whether they are down-regulated until fusion is triggered. We now show that synaptobrevin in proteoliposomes as well as in purified synaptic vesicles is co...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Angewandte Chemie
دوره 48 13 شماره
صفحات -
تاریخ انتشار 2009