TOM20-mediated transfer of Bcl2 from ER to MAM and mitochondria upon induction of apoptosis.
In this work, we have explored the subcellular localization of Bcl2, a major antiapoptotic protein. In U251 glioma cells, we found that Bcl2 is localized mainly in the ER and is translocated to MAM and mitochondria upon induction of apoptosis; this mitochondrial transfer was not restricted to the demonstrator cell ... line, even if cell-specific modulations exist. We found that the Bcl2/mitochondria interaction is controlled by TOM20, a protein that belongs to the protein import machinery of the mitochondrial outer membrane. The expression of a small domain of interaction of TOM20 with Bcl2 potentiates its anti-apoptotic properties, which suggests that the Bcl2-TOM20 interaction is proapoptotic. The role of MAM and TOM20 in Bcl2 apoptotic mitochondrial localization and function has been confirmed in a yeast model in which the ER-mitochondria encounter structure (ERMES) complex (required for MAM stability in yeast) has been disrupted. Bcl2-TOM20 interaction is thus an additional player in the control of apoptosis.
Mesh Terms:
Apoptosis, Cell Line, Tumor, Endoplasmic Reticulum, HeLa Cells, Humans, Membrane Transport Proteins, Microscopy, Confocal, Mitochondria, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Mitochondrial Precursor Protein Import Complex Proteins, Protein Transport, Proto-Oncogene Proteins c-bcl-2, Receptors, Cell Surface, Saccharomyces cerevisiae Proteins
Apoptosis, Cell Line, Tumor, Endoplasmic Reticulum, HeLa Cells, Humans, Membrane Transport Proteins, Microscopy, Confocal, Mitochondria, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Mitochondrial Precursor Protein Import Complex Proteins, Protein Transport, Proto-Oncogene Proteins c-bcl-2, Receptors, Cell Surface, Saccharomyces cerevisiae Proteins
Cell Death Dis
Date: Feb. 15, 2021
PubMed ID: 33589622
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