A Fluorescent Reporter of the Phosphorylation Status of the Substrate Protein STAT3

Roving reporter: A reversible biosensor reports the phosphorylation status of full‐length substrate protein STAT3 by genetically incorporating 7‐hydroxycoumarin into its phosphotyrosine binding pocket (see picture). A large fluorescence increase with characteristic emission and excitation properties...

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Veröffentlicht in:	Angewandte Chemie International Edition 2011-09, Vol.50 (37), p.8692-8696
Hauptverfasser:	Lacey, Vanessa K., Parrish, Angela R., Han, Shuliang, Shen, Zhouxin, Briggs, Steven P., Ma, Yuguo, Wang, Lei
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - chemistry Amino Acids - genetics Amino Acids - metabolism Fluorescent Dyes - chemistry Fluorescent Dyes - metabolism fluorescent probes Kinases Models, Molecular Molecular Structure nonnatural amino acids Phosphorylation STAT proteins STAT3 Transcription Factor - chemistry STAT3 Transcription Factor - metabolism
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Beschreibung
Zusammenfassung:	Roving reporter: A reversible biosensor reports the phosphorylation status of full‐length substrate protein STAT3 by genetically incorporating 7‐hydroxycoumarin into its phosphotyrosine binding pocket (see picture). A large fluorescence increase with characteristic emission and excitation properties results as a response to phosphorylation of STAT3 in vitro and endogenously in nuclear extracts.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.201102923