The C-terminal sequences of Bcl-2 family proteins mediate interactions that regulate cell death.

Autor:	Nguyen D; Department of Medical Biophysics, Faculty of Medicine, University of Toronto, Toronto, Canada.; Biological Sciences Platform, Odette Cancer Program, Sunnybrook Research Institute, Toronto, Canada., Osterlund E; Department of Biochemistry and Biomedical Sciences, Faculty of Health Science, McMaster University, Hamilton, Canada., Kale J; Biological Sciences Platform, Odette Cancer Program, Sunnybrook Research Institute, Toronto, Canada., Andrews DW; Department of Medical Biophysics, Faculty of Medicine, University of Toronto, Toronto, Canada.; Biological Sciences Platform, Odette Cancer Program, Sunnybrook Research Institute, Toronto, Canada.; Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, Canada.
Jazyk:	angličtina
Zdroj:	The Biochemical journal [Biochem J] 2024 Jul 17; Vol. 481 (14), pp. 903-922.
DOI:	10.1042/BCJ20210352
Abstrakt:	Programmed cell death via the both intrinsic and extrinsic pathways is regulated by interactions of the Bcl-2 family protein members that determine whether the cell commits to apoptosis via mitochondrial outer membrane permeabilization (MOMP). Recently the conserved C-terminal sequences (CTSs) that mediate localization of Bcl-2 family proteins to intracellular membranes, have been shown to have additional protein-protein binding functions that contribute to the functions of these proteins in regulating MOMP. Here we review the pivotal role of CTSs in Bcl-2 family interactions including: (1) homotypic interactions between the pro-apoptotic executioner proteins that cause MOMP, (2) heterotypic interactions between pro-apoptotic and anti-apoptotic proteins that prevent MOMP, and (3) heterotypic interactions between the pro-apoptotic executioner proteins and the pro-apoptotic direct activator proteins that promote MOMP. (© 2024 The Author(s).)
Databáze:	MEDLINE
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