Moonlighting glyceraldehyde-3-phosphate dehydrogenase: posttranslational modification,protein and nucleic acid interactions in normal cells and in human pathology |
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Authors: | Michael A. Sirover |
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Affiliation: | 1. Department of Pharmacology, Lewis Katz School of Medicine, Temple University, Philadelphia, PA, USA michael.sirover@temple.edu |
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Abstract: | Abstract Moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) exhibits multiple functions separate and distinct from its historic role in energy production. Further, it exhibits dynamic changes in its subcellular localization which is an a priori requirement for its multiple activities. Separately, moonlighting GAPDH may function in the pathology of human disease, involved in tumorigenesis, diabetes, and age-related neurodegenerative disorders. It is suggested that moonlighting GAPDH function may be related to specific modifications of its protein structure as well as the formation of GAPDH protein: protein or GAPDH protein: nucleic acid complexes. |
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Keywords: | Glyceraldehyde-3-phosphate dehydrogenase moonlighting protein posttranslational modification mRNA stability DNA structure |
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