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Cell death regulation by the Bcl‐2 protein family in the mitochondria
Author(s) -
Tsujimoto Yoshihide
Publication year - 2003
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.10254
Subject(s) - microbiology and biotechnology , mitochondrion , mitochondrial apoptosis induced channel , apoptosis , bcl 2 family , cytochrome c , programmed cell death , mitochondrial membrane transport protein , translocase of the inner membrane , cytoplasm , biology , mitochondrial permeability transition pore , inner mitochondrial membrane , dnaja3 , inner membrane , mitochondrial fusion , mitochondrial dna , biochemistry , gene
An increase in the permeability of the outer mitochondrial membrane is central to apoptotic cell death, since it leads to the release of several apoptogenic factors, such as cytochrome c and Smac/Diablo, into the cytoplasm that activate downstream death programs. During apoptosis, the mitochondria also release AIF and endonuclease G, both of which are translocated to the nucleus and are implicated in apoptotic nuclear changes that occur in a caspase‐independent manner. Mitochondrial membrane permeability is directly controlled by the major apoptosis regulator, i.e., the Bcl‐2 family of proteins, mainly through regulation of the formation of apoptotic protein‐conducting pores in the outer mitochondrial membrane, although the precise molecular mechanisms are still not completely understood. Here, I focus on the mechanisms by which Bcl‐2 family members control the permeability of mitochondrial membrane during apoptosis. © 2003 Wiley‐Liss, Inc.