Abstract
We have identified a serine/threonine kinase that is rapidly activated during Fas-mediated apoptosis. Fas-activated serine/threonine kinase (FAST) is phosphorylated on serine and threonine residues in Jurkat cells. In response to Fas ligation, it is rapidly dephosphorylated and concomitantly activated to phosphorylate TIA-1, a nuclear RNA-binding protein that has been implicated as an effector of apoptosis. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation, suggesting a role in signaling downstream events in the apoptotic program. Our results introduce Fast and TIA-1 as components of a molecular cascade involved in signaling Fas-mediated apoptosis.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Antigens, Surface / physiology*
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Apoptosis / physiology*
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Consensus Sequence
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DNA, Complementary / genetics
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Humans
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Leukemia-Lymphoma, Adult T-Cell
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Membrane Proteins*
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Molecular Sequence Data
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Phosphorylation
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Poly(A)-Binding Proteins
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Protein Processing, Post-Translational*
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Protein Serine-Threonine Kinases / isolation & purification
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Protein Serine-Threonine Kinases / metabolism*
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Proteins*
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RNA-Binding Proteins / metabolism*
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Sequence Alignment
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Sequence Homology, Amino Acid
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T-Cell Intracellular Antigen-1
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Tumor Cells, Cultured
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fas Receptor
Substances
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Antigens, Surface
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DNA, Complementary
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Membrane Proteins
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Poly(A)-Binding Proteins
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Proteins
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RNA-Binding Proteins
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T-Cell Intracellular Antigen-1
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TIA1 protein, human
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fas Receptor
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FASTK protein, human
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Protein Serine-Threonine Kinases