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Título

Direct Interactions Between Tbid And Bcl-xlΔXl Are Enhanced In Lipid Membranes

AutorGarcía-Sáez, Ana J.; Ries, Jonas; Orzáez, Mar; Pérez-Payá, Enrique ; Schwille, Petra
Fecha de publicación10-feb-2009
EditorElsevier
CitaciónBiophysical Journal 96(3 S1): 425a-425a (2009)
ResumenThe proteins of the Bcl-2 family are key regulators of apoptosis, but their molecular mechanisms remains controversial. Two important aspects that center the debate involve the interaction network between the pro- and antiapoptotic family members and the role of their translocation to the mitochondrial outer membrane (MOM) during apoptosis. We have used FCCS to examine quantitatively the dynamic interactions of Bid and tBid with Bcl-xLΔCt in solution and in lipid membranes. We found that only the active form tBid binds to Bcl-xLΔCt and that the membrane strongly promotes binding between them. Importantly for drug design, a BH3 peptide from Bid disrupts the tBid/Bcl-xL complex in solution but not in lipid bilayers. Our findings convincingly suggest that the most relevant interaction between tBid and Bcl-xL happens in the membrane and reveal its significance as an additional regulatory stage for MOM permeabilization.
Descripción2190-Pos B160
Versión del editorhttp://dx.doi.org/10.1016/j.bpj.2008.12.2174
URIhttp://hdl.handle.net/10261/17719
DOI10.1016/j.bpj.2008.12.2174
ISSN0006-3495
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