Enzymology of intracellular membrane fusion

1991 ◽  
Vol 69 (3) ◽  
pp. 98-104 ◽  
Author(s):  
J. E. Rothman
Keyword(s):  
Membrane Fusion ◽  
Intracellular Membrane ◽  
Intracellular Membrane Fusion

scholarly journals A Dynamin Homolog Promotes the Transition from Hemifusion to Content Mixing in Intracellular Membrane Fusion

Traffic ◽  
2014 ◽  
Vol 15 (5) ◽  
pp. 558-571 ◽  
Author(s):  
Aditya Kulkarni ◽  
Kannan Alpadi ◽  
Tirupataiah Sirupangi ◽  
Christopher Peters
Keyword(s):  
Membrane Fusion ◽  
Intracellular Membrane ◽  
Intracellular Membrane Fusion

scholarly journals Dynamin−SNARE interactions control trans-SNARE formation in intracellular membrane fusion

2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Kannan Alpadi ◽  
Aditya Kulkarni ◽  
Sarita Namjoshi ◽  
Sankaranarayanan Srinivasan ◽  
Katherine H. Sippel ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Intracellular Membrane ◽  
Intracellular Membrane Fusion

Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion

Nature ◽  
2005 ◽  
Vol 436 (7049) ◽  
pp. 410-414 ◽  
Author(s):  
Christoph Reese ◽  
Felix Heise ◽  
Andreas Mayer
Keyword(s):  
Membrane Fusion ◽  
Intracellular Membrane ◽  
Intracellular Membrane Fusion

scholarly journals Topological arrangement of the intracellular membrane fusion machinery

2011 ◽  
Vol 22 (14) ◽  
pp. 2612-2619 ◽  
Author(s):  
Shailendra S. Rathore ◽  
Nilanjan Ghosh ◽  
Yan Ouyang ◽  
Jingshi Shen
Keyword(s):  
Membrane Fusion ◽  
Fusion Reaction ◽  
Coiled Coil ◽  
Intracellular Membrane ◽  
Sm Proteins ◽  
Protein Receptors ◽  
Reconstituted System ◽  
Sm Protein ◽  
First Time ◽  
Intracellular Membrane Fusion

Soluble N-ethylmaleimide–sensitive factor attachment protein receptors (SNAREs) form a four-helix coiled-coil bundle that juxtaposes two bilayers and drives a basal level of membrane fusion. The Sec1/Munc18 (SM) protein binds to its cognate SNARE bundle and accelerates the basal fusion reaction. The question of how the topological arrangement of the SNARE helices affects the reactivity of the fusion proteins remains unanswered. Here we address the problem for the first time in a reconstituted system containing both SNAREs and SM proteins. We find that to be fusogenic a SNARE topology must support both basal fusion and SM stimulation. Certain topological combinations of exocytic SNAREs result in basal fusion but cannot support SM stimulation, whereas other topologies support SM stimulation without inducing basal fusion. It is striking that of all the possible topological combinations of exocytic SNARE helices, only one induces efficient fusion. Our results suggest that the intracellular membrane fusion complex is designed to fuse bilayers according to one genetically programmed topology.

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