Literature DB >> 26153704

Synaptobrevin transmembrane domain influences exocytosis by perturbing vesicle membrane curvature.

Che-Wei Chang1, Meyer B Jackson2.   

Abstract

Membrane fusion requires that nearly flat lipid bilayers deform into shapes with very high curvature. This makes membrane bending a critical force in determining fusion mechanisms. A lipid bilayer will bend spontaneously when material is distributed asymmetrically between its two monolayers, and its spontaneous curvature (C0) will influence the stability of curved fusion intermediates. Prior work on Ca(2+)-triggered exocytosis revealed that fusion pore lifetime (τ) varies with vesicle content (Q), and showed that this relation reflects membrane bending energetics. Lipids that alter C0 change the dependence of τ on Q. These results suggested that the greater stability of an initial exocytotic fusion pore associated with larger vesicles reflects the need to bend more membrane during fusion pore dilation. In this study, we explored the possibility of manipulating C0 by mutating the transmembrane domain (TMD) of the vesicle membrane protein synaptobrevin 2 (syb2). Amperometric measurements of exocytosis in mouse chromaffin cells revealed that syb2 TMD mutations altered the relation between τ and Q. The effects of these mutations showed a striking periodicity, changing sign as the structural perturbation moved through the inner and outer leaflets. Some glycine and charge mutations also influenced the dependence of τ on Q in a manner consistent with expected changes in C0. These results suggest that side chains in the syb2 TMD influence the kinetics of exocytosis by perturbing the packing of the surrounding lipids. The present results support the view that membrane bending occurs during fusion pore expansion rather than during fusion pore formation. This supports the view of an initial fusion pore through two relatively flat membranes formed by protein.
Copyright © 2015 Biophysical Society. Published by Elsevier Inc. All rights reserved.

Entities:  

Mesh:

Substances:

Year:  2015        PMID: 26153704      PMCID: PMC4571039          DOI: 10.1016/j.bpj.2015.05.021

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  42 in total

1.  Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity.

Authors:  D Langosch; J M Crane; B Brosig; A Hellwig; L K Tamm; J Reed
Journal:  J Mol Biol       Date:  2001-08-24       Impact factor: 5.469

2.  Field theoretic study of bilayer membrane fusion. I. Hemifusion mechanism.

Authors:  K Katsov; M Müller; M Schick
Journal:  Biophys J       Date:  2004-08-23       Impact factor: 4.033

3.  Tension in secretory granule membranes causes extensive membrane transfer through the exocytotic fusion pore.

Authors:  J R Monck; G Alvarez de Toledo; J M Fernandez
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

4.  Membrane bending energy and fusion pore kinetics in Ca(2+)-triggered exocytosis.

Authors:  Zhen Zhang; Meyer B Jackson
Journal:  Biophys J       Date:  2010-06-02       Impact factor: 4.033

Review 5.  Inferring structures of kinetic intermediates in Ca(2+)-triggered exocytosis.

Authors:  Meyer B Jackson
Journal:  Curr Top Membr       Date:  2011       Impact factor: 3.049

6.  A structural role for the synaptobrevin 2 transmembrane domain in dense-core vesicle fusion pores.

Authors:  Che-Wei Chang; Enfu Hui; Jihong Bai; Dieter Bruns; Edwin R Chapman; Meyer B Jackson
Journal:  J Neurosci       Date:  2015-04-08       Impact factor: 6.167

7.  SNARE complex zipping as a driving force in the dilation of proteinaceous fusion pores.

Authors:  Meyer B Jackson
Journal:  J Membr Biol       Date:  2010-05-30       Impact factor: 1.843

Review 8.  Molecular machines governing exocytosis of synaptic vesicles.

Authors:  Reinhard Jahn; Dirk Fasshauer
Journal:  Nature       Date:  2012-10-11       Impact factor: 49.962

9.  Minimum membrane bending energies of fusion pores.

Authors:  Meyer B Jackson
Journal:  J Membr Biol       Date:  2009-10-29       Impact factor: 1.843

10.  Temporally resolved catecholamine spikes correspond to single vesicle release from individual chromaffin cells.

Authors:  R M Wightman; J A Jankowski; R T Kennedy; K T Kawagoe; T J Schroeder; D J Leszczyszyn; J A Near; E J Diliberto; O H Viveros
Journal:  Proc Natl Acad Sci U S A       Date:  1991-12-01       Impact factor: 11.205

View more
  6 in total

1.  The Transmembrane Domain of Synaptobrevin Influences Neurotransmitter Flux through Synaptic Fusion Pores.

Authors:  Chung-Wei Chiang; Che-Wei Chang; Meyer B Jackson
Journal:  J Neurosci       Date:  2018-07-16       Impact factor: 6.167

2.  The SNAP-25 linker supports fusion intermediates by local lipid interactions.

Authors:  Ahmed Shaaban; Madhurima Dhara; Walentina Frisch; Ali Harb; Ali H Shaib; Ute Becherer; Dieter Bruns; Ralf Mohrmann
Journal:  Elife       Date:  2019-03-18       Impact factor: 8.140

Review 3.  Membrane tension and membrane fusion.

Authors:  Michael M Kozlov; Leonid V Chernomordik
Journal:  Curr Opin Struct Biol       Date:  2015-08-15       Impact factor: 6.809

4.  Lipid-anchored Synaptobrevin Provides Little or No Support for Exocytosis or Liposome Fusion.

Authors:  Che-Wei Chang; Chung-Wei Chiang; Jon D Gaffaney; Edwin R Chapman; Meyer B Jackson
Journal:  J Biol Chem       Date:  2015-12-08       Impact factor: 5.157

Review 5.  Fusion pores and their control of neurotransmitter and hormone release.

Authors:  Che-Wei Chang; Chung-Wei Chiang; Meyer B Jackson
Journal:  J Gen Physiol       Date:  2017-02-06       Impact factor: 4.086

Review 6.  v-SNARE function in chromaffin cells.

Authors:  Madhurima Dhara; Ralf Mohrmann; Dieter Bruns
Journal:  Pflugers Arch       Date:  2017-09-08       Impact factor: 3.657

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.