Abstract
A novel study in a recent issue of Molecular Cell (Shi and Manley, 2007) provides insight into a complex signaling pathway that controls the phosphorylation status of an SR-related protein that functions as a splicing repressor following heat shock-dependent dephosphorylation.
MeSH terms
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14-3-3 Proteins / metabolism
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Adenosine Triphosphate / metabolism
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Amino Acid Motifs
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Animals
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Hot Temperature*
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Humans
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Intracellular Signaling Peptides and Proteins / metabolism
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Nuclear Proteins / chemistry
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Nuclear Proteins / metabolism*
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Phosphorylation
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Protein Binding
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Protein Phosphatase 1 / metabolism
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Protein Serine-Threonine Kinases / metabolism
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Protein Structure, Tertiary
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Protein-Tyrosine Kinases / metabolism
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RNA Precursors / metabolism*
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RNA Splicing*
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RNA, Messenger / metabolism*
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RNA-Binding Proteins / chemistry
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RNA-Binding Proteins / metabolism*
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Ribonucleoproteins, Small Nuclear / metabolism
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Serine-Arginine Splicing Factors
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Stress, Physiological / genetics
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Stress, Physiological / metabolism*
Substances
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14-3-3 Proteins
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Intracellular Signaling Peptides and Proteins
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Nuclear Proteins
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RNA Precursors
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RNA, Messenger
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RNA-Binding Proteins
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Ribonucleoproteins, Small Nuclear
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protein phosphatase inhibitor-1
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Serine-Arginine Splicing Factors
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Adenosine Triphosphate
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Clk dual-specificity kinases
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Protein-Tyrosine Kinases
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Protein Serine-Threonine Kinases
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Protein Phosphatase 1