
pmid: 17964256
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.
Hot Temperature, Serine-Arginine Splicing Factors, RNA Splicing, Amino Acid Motifs, Intracellular Signaling Peptides and Proteins, Nuclear Proteins, RNA-Binding Proteins, Cell Biology, Protein Serine-Threonine Kinases, Protein-Tyrosine Kinases, Ribonucleoproteins, Small Nuclear, Protein Structure, Tertiary, Adenosine Triphosphate, 14-3-3 Proteins, Protein Phosphatase 1, RNA Precursors, Animals, Humans, RNA, Messenger, Phosphorylation, Molecular Biology, Protein Binding
Hot Temperature, Serine-Arginine Splicing Factors, RNA Splicing, Amino Acid Motifs, Intracellular Signaling Peptides and Proteins, Nuclear Proteins, RNA-Binding Proteins, Cell Biology, Protein Serine-Threonine Kinases, Protein-Tyrosine Kinases, Ribonucleoproteins, Small Nuclear, Protein Structure, Tertiary, Adenosine Triphosphate, 14-3-3 Proteins, Protein Phosphatase 1, RNA Precursors, Animals, Humans, RNA, Messenger, Phosphorylation, Molecular Biology, Protein Binding
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