5.14 The Biophysics of Membrane Fusion
作者： R.N. Collins , R.W. Holz , J. Zimmerberg
DOI: 10.1016/B978-0-12-374920-8.00523-3
关键词:
摘要: A crucial interplay between protein conformations and lipid membrane energetics emerges as the guiding principle for regulation mechanism of fusion in biological systems. As some basics become clear, a myriad compelling questions come to fore. Is interior pore or lipid? Why is synaptic release so fast? PIP 2 needed exocytosis? How does peptide insertion lead viruses cell membranes? What role TMD play? can studies on fission contribute our understanding fusion? exactly are SNARE proteins doing?
sci-hub.se 参考文章(140)
Qiang Huang, Rachakonda P Sivaramakrishna, Kai Ludwig, Thomas Korte, Christoph Böttcher, Andreas Herrmann, None, Early steps of the conformational change of influenza virus hemagglutinin to a fusion active state. Stability and energetics of the hemagglutinin Biochimica et Biophysica Acta. ,vol. 1614, pp. 3- 13 ,(2003) , 10.1016/S0005-2736(03)00158-5
L. Edelmann, P.I. Hanson, E.R. Chapman, R. Jahn, Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. The EMBO Journal. ,vol. 14, pp. 224- 231 ,(1995) , 10.1002/J.1460-2075.1995.TB06995.X
N Calakos, R H Scheller, Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle. Journal of Biological Chemistry. ,vol. 269, pp. 24534- 24537 ,(1994) , 10.1016/S0021-9258(17)31422-9
I.C. Griff, R Schekman, J.E. Rothman, C.A. Kaiser, The yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein. Journal of Biological Chemistry. ,vol. 267, pp. 12106- 12115 ,(1992) , 10.1016/S0021-9258(19)49812-8
Xing Han, John H. Bushweller, David S. Cafiso, Lukas K. Tamm, Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nature Structural & Molecular Biology. ,vol. 8, pp. 715- 720 ,(2001) , 10.1038/90434
Markin Vs, Borovjagin Vl, Kozlov Mm, On the Theory of Membrane Fusion. The Stalk Mechanism General Physiology and Biophysics. ,vol. 3, pp. 361- 377 ,(1984)
Ajaybabu V. Pobbati, Adelia Razeto, Matthias Böddener, Stefan Becker, Dirk Fasshauer, Structural Basis for the Inhibitory Role of Tomosyn in Exocytosis Journal of Biological Chemistry. ,vol. 279, pp. 47192- 47200 ,(2004) , 10.1074/JBC.M408767200
Levon G. Abrahamyan, Samvel R. Mkrtchyan, James Binley, Min Lu, Grigory B. Melikyan, Fredric S. Cohen, The cytoplasmic tail slows the folding of human immunodeficiency virus type 1 Env from a late prebundle configuration into the six-helix bundle Journal of Virology. ,vol. 79, pp. 106- 115 ,(2005) , 10.1128/JVI.79.1.106-115.2005
Yasuyuki Fujita, Hiromichi Shirataki, Toshiaki Sakisaka, Takeshi Asakura, Takeshi Ohya, Hirokazu Kotani, Shigekazu Yokoyama, Hideo Nishioka, Yoshiharu Matsuura, Akira Mizoguchi, Richard H Scheller, Yoshimi Takai, Tomosyn: a Syntaxin-1-Binding Protein that Forms a Novel Complex in the Neurotransmitter Release Process Neuron. ,vol. 20, pp. 905- 915 ,(1998) , 10.1016/S0896-6273(00)80472-9
D A Eberhard, C L Cooper, M G Low, R W Holz, Evidence that the inositol phospholipids are necessary for exocytosis. Loss of inositol phospholipids and inhibition of secretion in permeabilized cells caused by a bacterial phospholipase C and removal of ATP Biochemical Journal. ,vol. 268, pp. 15- 25 ,(1990) , 10.1042/BJ2680015