Show simple item record

dc.contributor.author
Bleicken, Stephanie
dc.contributor.author
García-Sáez, Ana J.
dc.contributor.author
Conte, Elena
dc.contributor.author
Bordignon, Enrica
dc.date.accessioned
2018-09-20T09:37:39Z
dc.date.available
2017-06-10T02:00:12Z
dc.date.available
2018-09-20T09:37:39Z
dc.date.issued
2012-04-23
dc.identifier.issn
1932-6203
dc.identifier.other
10.1371/journal.pone.0035910
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/50992
dc.identifier.doi
10.3929/ethz-b-000050992
dc.description.abstract
The BH3-only protein Bid plays a key role in the induction of mitochondrial apoptosis, but its mechanism of action is still not completely understood. Here we studied the two main activation events of Bid: Caspase-8 cleavage and interaction with the membrane bilayer. We found a striking reversible behaviour of the dissociation-association events between the Bid fragments p15 and p7. Caspase-8 cleavage does not induce per se separation of the two Bid fragments, which remain in a stable complex resembling the full length Bid. Detergents trigger a complete dissociation, which can be fully reversed by detergent removal in a range of protein concentrations from 100 µM down to 500 nM. Incubation of cBid with cardiolipin-containing liposomes leads to partial dissociation of the complex. Only p15 (tBid) fragments are found at the membrane, while p7 shows no tendency to interact with the bilayer, but complete removal of p7 strongly increases the propensity of tBid to become membrane-associated. Despite the striking structural similarities of inactive Bid and Bax, Bid does not form oligomers and reacts differently in the presence of detergents and membranes, highlighting clear differences in the modes of action of the two proteins. The partial dissociation of cBid triggered by the membrane is suggested to depend on the strong and specific interaction between p15 and p7. The reversible disassembly and re-assembly of the cBid molecules at the membrane was as well proven by EPR using spin labeled cBid in the presence of isolated mitochondria. The observed dynamic dissociation of the two Bid fragments could allow the assistance to the pore-forming Bax to occur repeatedly and may explain the proposed “hit-and-run" mode of action of Bid at the bilayer.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Public Library of Science
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/3.0/
dc.title
Dynamic Interaction of cBid with Detergents, Liposomes and Mitochondria
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 3.0 Unported
ethz.journal.title
PLoS ONE
ethz.journal.volume
7
en_US
ethz.journal.issue
4
en_US
ethz.journal.abbreviated
PLoS ONE
ethz.pages.start
e35910
en_US
ethz.size
12 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.nebis
006206116
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02515 - Laboratorium für Physikalische Chemie / Laboratory of Physical Chemistry::03810 - Jeschke, Gunnar / Jeschke, Gunnar
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02515 - Laboratorium für Physikalische Chemie / Laboratory of Physical Chemistry::03810 - Jeschke, Gunnar / Jeschke, Gunnar
ethz.date.deposited
2017-06-10T02:00:33Z
ethz.source
ECIT
ethz.identifier.importid
imp59364f5f03b1423491
ethz.ecitpid
pub:83220
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-12T18:24:33Z
ethz.rosetta.lastUpdated
2021-02-15T01:49:09Z
ethz.rosetta.versionExported
true
ethz.COinS
ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.atitle=Dynamic%20Interaction%20of%20cBid%20with%20Detergents,%20Liposomes%20and%20Mitochondria&rft.jtitle=PLoS%20ONE&rft.date=2012-04-23&rft.volume=7&rft.issue=4&rft.spage=e35910&rft.issn=1932-6203&rft.au=Bleicken,%20Stephanie&Garc%C3%ADa-S%C3%A1ez,%20Ana%20J.&Conte,%20Elena&Bordignon,%20Enrica&rft.genre=article&rft_id=info:doi/10.1371/journal.pone.0035910&
 Search print copy at ETH Library

Files in this item

Thumbnail

Publication type

Show simple item record