Abstract
Protein kinases play essential biological roles by phosphorylating a diverse range of signaling molecules, but deciphering their direct physiological targets remains a challenge. A new study by Shinde et al. uses phosphoproteomics to identify glycogen synthase kinase-3 (GSK-3) substrates in mouse embryonic stem cells (mESCs), providing a broad profile of GSK-3 activity and defining a new role for this central kinase in regulating RNA splicing.
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
Publication types
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Review
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Alternative Splicing
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Animals
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Cell Cycle Proteins / metabolism
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Embryonic Stem Cells / enzymology
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Embryonic Stem Cells / metabolism
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Gene Knockdown Techniques
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Gene Ontology
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Glycogen Synthase Kinase 3 / genetics
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Glycogen Synthase Kinase 3 / metabolism*
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Humans
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Phosphorylation
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Protein Processing, Post-Translational
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RNA Splicing*
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Substrate Specificity
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Transcription Factors / metabolism*
Substances
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Cell Cycle Proteins
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Transcription Factors
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Glycogen Synthase Kinase 3