Abstract
Post-translational modifications, such as acetylation and ubiquitination, can greatly expand the functionality of a particular protein. The promyelocytic leukemia (PML) protein is a functionally promiscuous protein with proposed roles in many cellular processes. Its cellular headquarters are the macromolecular structures termed PML nuclear bodies. Post-translational modification of PML is emerging as a defining feature of this protein that regulates its physiological consequences. This review will highlight the expansion of our knowledge about the post-translational modifications of PML.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Humans
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Nuclear Proteins / metabolism
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Nuclear Proteins / physiology*
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Phosphorylation
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Promyelocytic Leukemia Protein
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Protein Processing, Post-Translational*
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Receptors, Retinoic Acid / metabolism
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Retinoic Acid Receptor alpha
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Small Ubiquitin-Related Modifier Proteins / metabolism
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Transcription Factors / metabolism
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Transcription Factors / physiology*
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Tumor Suppressor Proteins / metabolism
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Tumor Suppressor Proteins / physiology*
Substances
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Nuclear Proteins
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Promyelocytic Leukemia Protein
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RARA protein, human
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Receptors, Retinoic Acid
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Retinoic Acid Receptor alpha
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Small Ubiquitin-Related Modifier Proteins
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Transcription Factors
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Tumor Suppressor Proteins
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PML protein, human