Literature DB >> 12842832

What is the role of SNARE proteins in membrane fusion?

Joseph G Duman1, John G Forte.   

Abstract

Soluble N-ethylmaleimide-sensitive factor activating protein receptor (SNARE) proteins have been at the fore-front of research on biological membrane fusion for some time. The subcellular localization of SNAREs and their ability to form the so-called SNARE complex may be integral to determining the specificity of intracellular fusion (the SNARE hypothesis) and/or serving as the minimal fusion machinery. Both the SNARE hypothesis and the idea of the minimal fusion machinery have been challenged by a number of experimental observations in various model systems, suggesting that SNAREs may have other functions. Considering recent advances in the SNARE literature, it appears that SNAREs may actually function as part of a complex fusion "machine." Their role in the machinery could be any one or a combination of roles, including establishing tight membrane contact, formation of a scaffolding on which to build the machine, binding of lipid surfaces, and many others. It is also possible that complexations other than the classic SNARE complex participate in membrane fusion.

Entities:  

Mesh:

Substances:

Year:  2003        PMID: 12842832     DOI: 10.1152/ajpcell.00091.2003

Source DB:  PubMed          Journal:  Am J Physiol Cell Physiol        ISSN: 0363-6143            Impact factor:   4.249


  43 in total

1.  Single molecule observation of liposome-bilayer fusion thermally induced by soluble N-ethyl maleimide sensitive-factor attachment protein receptors (SNAREs).

Authors:  Mark E Bowen; Keith Weninger; Axel T Brunger; Steven Chu
Journal:  Biophys J       Date:  2004-09-03       Impact factor: 4.033

2.  The specificity of SNARE-dependent fusion is encoded in the SNARE motif.

Authors:  Fabienne Paumet; Vahid Rahimian; James E Rothman
Journal:  Proc Natl Acad Sci U S A       Date:  2004-02-23       Impact factor: 11.205

Review 3.  Regulation of the epithelial sodium channel (ENaC) by membrane trafficking.

Authors:  Michael B Butterworth
Journal:  Biochim Biophys Acta       Date:  2010-03-27

4.  Identification of novel ATP13A2 interactors and their role in α-synuclein misfolding and toxicity.

Authors:  Marija Usenovic; Adam L Knight; Arpita Ray; Victoria Wong; Kevin R Brown; Guy A Caldwell; Kim A Caldwell; Igor Stagljar; Dimitri Krainc
Journal:  Hum Mol Genet       Date:  2012-05-29       Impact factor: 6.150

5.  Molecular identification and reconstitution of depolarization-induced exocytosis monitored by membrane capacitance.

Authors:  Roy Cohen; Bernhard M Schmitt; Daphne Atlas
Journal:  Biophys J       Date:  2005-09-08       Impact factor: 4.033

6.  Correlation between vesicle quantal size and fusion pore release in chromaffin cell exocytosis.

Authors:  Christian Amatore; Stéphane Arbault; Imelda Bonifas; Yann Bouret; Marie Erard; Andy G Ewing; Leslie A Sombers
Journal:  Biophys J       Date:  2005-03-25       Impact factor: 4.033

7.  Evidence that the SpoIIIE DNA translocase participates in membrane fusion during cytokinesis and engulfment.

Authors:  Nai-Jia Linda Liu; Rachel J Dutton; Kit Pogliano
Journal:  Mol Microbiol       Date:  2006-02       Impact factor: 3.501

8.  Differential localization of aquaporin-2 and glucose transporter 4 in polarized MDCK cells.

Authors:  Takahiro Hasegawa; Toshiyuki Matsuzaki; Yuki Tajika; Abduxukur Ablimit; Takeshi Suzuki; Takeo Aoki; Haruo Hagiwara; Kuniaki Takata
Journal:  Histochem Cell Biol       Date:  2007-01-06       Impact factor: 4.304

Review 9.  Regulation of the epithelial sodium channel by membrane trafficking.

Authors:  Michael B Butterworth; Robert S Edinger; Raymond A Frizzell; John P Johnson
Journal:  Am J Physiol Renal Physiol       Date:  2008-05-28

10.  Annexin A7 trafficking to alveolar type II cell surface: possible roles for protein insertion into membranes and lamellar body secretion.

Authors:  Avinash Chander; Tudevdagva Gerelsaikhan; Pavan K Vasa; Kelly Holbrook
Journal:  Biochim Biophys Acta       Date:  2013-02-19
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.