Abstract
Among all Bcl2 homology domain 3 (BH3)-only proteins known to date, APR/PMAIP1/Noxa, albeit showing weak proapoptotic potential on its own, appears to be crucial in fine-tuning cell death decisions by targeting the prosurvival molecule Mcl1 for proteasomal degradation. This event appears critical for cell death induction along the mitochondrial Bcl2-regulated apoptosis pathway in response to factor deprivation or DNA damage, presumably by sensitizing the cell toward the action of additional BH3-only protein family members. This review aims to summarize the function of Noxa in normal physiology, stress-induced cell death and tumorigenesis.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptosis / physiology*
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Child
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DNA Damage*
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Gene Expression Regulation
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Humans
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Invertebrates / metabolism
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Mice
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Mice, Knockout
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Molecular Sequence Data
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Myeloid Cell Leukemia Sequence 1 Protein
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Neoplasm Proteins / physiology
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Neoplasms / etiology
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Neoplasms / genetics
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Neoplasms / metabolism
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Neoplasms / therapy
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Protein Structure, Tertiary
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Proto-Oncogene Proteins c-bcl-2 / chemistry
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Proto-Oncogene Proteins c-bcl-2 / metabolism
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Proto-Oncogene Proteins c-bcl-2 / physiology*
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Sequence Alignment
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Sequence Homology, Amino Acid
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Tetradecanoylphorbol Acetate / pharmacology
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Tumor Suppressor Protein p53 / physiology
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Vertebrates / metabolism
Substances
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Mcl1 protein, mouse
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Myeloid Cell Leukemia Sequence 1 Protein
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Neoplasm Proteins
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PMAIP1 protein, human
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Pmaip1 protein, mouse
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Proto-Oncogene Proteins c-bcl-2
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Tumor Suppressor Protein p53
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Tetradecanoylphorbol Acetate