Home > Publications database > Pro-apoptotic cBid and Bax exhibit distinct membrane remodeling activities: An AFM study. > print

001     119256
005     20240228145430.0
024 7 _ |2 doi
|a 10.1016/j.bbamem.2016.10.007
024 7 _ |2 pmid
|a pmid:27755971
024 7 _ |2 ISSN
|a 0005-2736
024 7 _ |2 ISSN
|a 1879-2642
024 7 _ |a altmetric:12648412
|2 altmetric
037 _ _ |a DKFZ-2017-00042
041 _ _ |a eng
082 _ _ |a 570
100 1 _ |0 P:(DE-HGF)0
|a Unsay, Joseph D
|b 0
|e First author
245 _ _ |a Pro-apoptotic cBid and Bax exhibit distinct membrane remodeling activities: An AFM study.
260 _ _ |a Amsterdam
|b Elsevier
|c 2017
336 7 _ |2 DRIVER
|a article
336 7 _ |2 DataCite
|a Output Types/Journal article
336 7 _ |0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
|a Journal Article
|b journal
|m journal
|s 1511336702_29010
336 7 _ |2 BibTeX
|a ARTICLE
336 7 _ |2 ORCID
|a JOURNAL_ARTICLE
336 7 _ |0 0
|2 EndNote
|a Journal Article
520 _ _ |a Bcl-2 proteins are key regulators of the mitochondrial outer membrane (MOM) permeabilization that mediates apoptosis. During apoptosis, Bid is cleaved (cBid) and translocates to the MOM, where it activates Bax. Bax then oligomerizes and induces MOM permeabilization. However, little is known about how these proteins affect membrane organization aside from pore formation. In previous studies, we have shown that both cBid and Bax are able to remodel membranes and stabilize curvature. Here, we dissected the independent effects of Bax and cBid on supported lipid structures mimicking the mitochondrial composition by means of atomic force spectroscopy. We show that cBid did not permeabilize the membrane but lowered the membrane breakthrough force. On the other hand, Bax effects were dependent on its oligomeric state. Monomeric Bax did not affect the membrane properties. In contrast, oligomeric Bax lowered the breakthrough force of the membrane, which in the context of pore formation, implies a lowering of the line tension at the edge of the pore.
536 _ _ |0 G:(DE-HGF)POF3-312
|a 312 - Functional and structural genomics (POF3-312)
|c POF3-312
|f POF III
|x 0
588 _ _ |a Dataset connected to CrossRef, PubMed,
700 1 _ |a Cosentino, Katia
|b 1
700 1 _ |a Sporbeck, Katharina
|b 2
700 1 _ |a García-Sáez, Ana J
|b 3
773 _ _ |0 PERI:(DE-600)2209384-9
|a 10.1016/j.bbamem.2016.10.007
|g Vol. 1859, no. 1, p. 17 - 27
|n 1
|p 17 - 27
|t Biochimica et biophysica acta / Biomembranes
|v 1859
|x 0005-2736
|y 2017
909 C O |o oai:inrepo02.dkfz.de:119256
|p VDB
910 1 _ |0 I:(DE-588b)2036810-0
|6 P:(DE-HGF)0
|a Deutsches Krebsforschungszentrum
|b 0
|k DKFZ
913 1 _ |0 G:(DE-HGF)POF3-312
|1 G:(DE-HGF)POF3-310
|2 G:(DE-HGF)POF3-300
|a DE-HGF
|l Krebsforschung
|v Functional and structural genomics
|x 0
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF3
|b Gesundheit
914 1 _ |y 2017
915 _ _ |0 StatID:(DE-HGF)0420
|2 StatID
|a Nationallizenz
915 _ _ |0 StatID:(DE-HGF)0100
|2 StatID
|a JCR
|b BBA-BIOMEMBRANES : 2015
915 _ _ |0 StatID:(DE-HGF)0200
|2 StatID
|a DBCoverage
|b SCOPUS
915 _ _ |0 StatID:(DE-HGF)0600
|2 StatID
|a DBCoverage
|b Ebsco Academic Search
915 _ _ |0 StatID:(DE-HGF)0030
|2 StatID
|a Peer Review
|b ASC
915 _ _ |0 StatID:(DE-HGF)0199
|2 StatID
|a DBCoverage
|b Thomson Reuters Master Journal List
915 _ _ |0 StatID:(DE-HGF)0110
|2 StatID
|a WoS
|b Science Citation Index
915 _ _ |0 StatID:(DE-HGF)0150
|2 StatID
|a DBCoverage
|b Web of Science Core Collection
915 _ _ |0 StatID:(DE-HGF)0111
|2 StatID
|a WoS
|b Science Citation Index Expanded
915 _ _ |0 StatID:(DE-HGF)1030
|2 StatID
|a DBCoverage
|b Current Contents - Life Sciences
915 _ _ |0 StatID:(DE-HGF)1050
|2 StatID
|a DBCoverage
|b BIOSIS Previews
915 _ _ |0 StatID:(DE-HGF)9900
|2 StatID
|a IF < 5
920 1 _ |0 I:(DE-He78)B160-20160331
|k B160
|l Membranbiophysik
|x 0
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-He78)B160-20160331
980 _ _ |a UNRESTRICTED

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21