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PML Regulates Apoptosis at Endoplasmic Reticulum by Modulating Calcium Release
- Publication Year :
- 2010
-
Abstract
- Promoting Apoptosis During acute disease, the promyelocytic leukemia (PML) protein becomes fused to another protein as a result of a chromosomal translocation. This protein appears to have multiple and varied functions, including the ability to form distinctive complexes in the nucleus that suppress tumorigenesis and promote apoptotic cell death. Giorgi et al. (p. 1247 , published online 28 October; see the Perspective by Culjkovic-Kraljacic and Borden ) have proposed a mechanism by which PML influences the cellular signals that promote apoptosis. The protein was localized at sites of contact between the endoplasmic reticulum and mitochondria, where it associated with a calcium channel, a protein kinase, and a protein phosphatase, to regulate calcium mobilization into the mitochondrion, which then triggers the cell death program.
- Subjects :
- Recombinant Fusion Proteins
Apoptosis
Inositol 1,4,5-Trisphosphate
Biology
Promyelocytic Leukemia Protein
Endoplasmic Reticulum
Cell Line
Promyelocytic leukemia protein
Mice
Adenosine Triphosphate
Cytosol
Stress, Physiological
Animals
Homeostasis
Humans
Inositol 1,4,5-Trisphosphate Receptors
Calcium Signaling
Protein Phosphatase 2
mitochondria
cell death
calcium
Phosphorylation
Protein kinase A
Protein kinase B
Cells, Cultured
Calcium signaling
Cell Nucleus
Multidisciplinary
Endoplasmic reticulum
Tumor Suppressor Proteins
Nuclear Proteins
Protein phosphatase 2
Intracellular Membranes
Cell biology
Mitochondria
biology.protein
Calcium
Signal transduction
Proto-Oncogene Proteins c-akt
Transcription Factors
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....d99da13185e6688ffe90df57d868eb1e