Phosphorylation of Specific Serine Residues in the PKR Activation Domain of PACT Is Essential for Its Ability to Mediate Apoptosis

Activation of the latent protein kinase, PKR, by extracellular stresses and triggering of resultant cellular apoptosis are mediated by the protein, PACT, which itself gets phosphorylated in stressed cells. We have analyzed the underlying biochemical mechanism by carrying out alanine-scanning mutagen...

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Veröffentlicht in:	The Journal of biological chemistry 2006-11, Vol.281 (46), p.35129-35136
Hauptverfasser:	Peters, Gregory A., Li, Shoudong, Sen, Ganes C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Apoptosis - physiology Binding Sites Cell Line, Tumor eIF-2 Kinase - genetics eIF-2 Kinase - metabolism Enzyme Activation Gene Expression Regulation Humans Mutation Phosphorylation Protein Structure, Tertiary RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Serine
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