The C-terminal sequences of Bcl-2 family proteins mediate interactions that regulate cell death.
Biochem J
; 481(14): 903-922, 2024 Jul 17.
Article
in En
| MEDLINE
| ID: mdl-38985308
ABSTRACT
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Apoptosis
/
Proto-Oncogene Proteins c-bcl-2
Limits:
Animals
/
Humans
Language:
En
Journal:
Biochem J
Year:
2024
Document type:
Article
Affiliation country:
Canadá
Country of publication:
Reino Unido