help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Originally published as Biophys J. BioFAST on April 6, 2007.
doi:10.1529/biophysj.106.100370
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
biophysj.106.100370v1
93/1/103    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by García-Sáez, A. J.
Right arrow Articles by Schwille, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by García-Sáez, A. J.
Right arrow Articles by Schwille, P.
Biophysical Journal 93:103-112 (2007)
© 2007 The Biophysical Society

Pore Formation by a Bax-Derived Peptide: Effect on the Line Tension of the Membrane Probed by AFM

Ana J. García-Sáez *, Salvatore Chiantia *, Jesús Salgado {dagger} and Petra Schwille *

* Biotechnologisches Zentrum der TU Dresden, Dresden, Germany; and {dagger} Instituto de Ciencia Molecular, Universitat de València, Burjassot, Spain

Correspondence: Address reprint requests to Petra Schwille, Tatzberg 47-51, 1307 Dresden, Germany. Tel.: 49-351-4634-0328; E-mail: petra.schwille{at}biotec.tu-dresden.de.

Bax is a critical regulator of physiological cell death that increases the permeability of the outer mitochondrial membrane and facilitates the release of the so-called apoptotic factors during apoptosis. The molecular mechanism of action is unknown, but it probably involves the formation of partially lipidic pores induced by Bax. To investigate the interaction of Bax with lipid membranes and the physical changes underlying the formation of Bax pores, we used an active peptide derived from helix 5 of this protein (Bax-{alpha}5) that is able to induce Bax-like pores in lipid bilayers. We report the decrease of line tension due to peptide binding both at the domain interface in phase-separated lipid bilayers and at the pore edge in atomic force microscopy film-rupture experiments. Such a decrease in line tension may be a general strategy of pore-forming peptides and proteins, as it affects the energetics of the pore and stabilizes the open state.




This article has been cited by other articles:


Home page
 Biophys. JHome page
P. Schon, A. J. Garcia-Saez, P. Malovrh, K. Bacia, G. Anderluh, and P. Schwille
Equinatoxin II Permeabilizing Activity Depends on the Presence of Sphingomyelin and Lipid Phase Coexistence
Biophys. J., July 15, 2008; 95(2): 691 - 698.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
L. Zhou and D. C. Chang
Dynamics and structure of the Bax-Bak complex responsible for releasing mitochondrial proteins during apoptosis
J. Cell Sci., July 1, 2008; 121(13): 2186 - 2196.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
S. Qian, W. Wang, L. Yang, and H. W. Huang
Structure of the Alamethicin Pore Reconstructed by X-Ray Diffraction Analysis
Biophys. J., May 1, 2008; 94(9): 3512 - 3522.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
PNAS, April 1, 2008; 105(13): 5087 - 5092.


Home page
 J. Biol. Chem.Home page
O. Terrones, A. Etxebarria, A. Landajuela, O. Landeta, B. Antonsson, and G. Basanez
BIM and tBID Are Not Mechanistically Equivalent When Assisting BAX to Permeabilize Bilayer Membranes
J. Biol. Chem., March 21, 2008; 283(12): 7790 - 7803.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2007 by the Biophysical Society.