期刊
CHEMISTRY & BIOLOGY
卷 17, 期 9, 页码 1018-1029出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2010.06.018
关键词
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资金
- National Institutes of Health [P50 CA94056]
- Medical Scientist Training Program
- Alvin J. Siteman Cancer Center at Barnes-Jewish Hospital
- Washington University School of Medicine
- National Science Foundation
- American Cancer Society
Understanding the functional complexity of protein interactions requires mapping biomolecular complexes within the cellular environment over biologically relevant time scales. Herein, we describe a set of reversible multicolored heteroprotein complementation fragments based on various firefly and click beetle luciferases that utilize the same substrate, D-luciferin. Luciferase heteroprotein fragment complementation systems enabled dual-color quantification of two discrete pairs of interacting proteins simultaneously or two distinct proteins interacting with a third shared protein in live cells. Using real-time analysis of click beetle green and click beetle red luciferase heteroprotein fragment complementation applied to beta-TrCP, an E3-ligase common to the regulation of both beta-catenin and I kappa B alpha, GSK3 beta was identified as a candidate kinase regulating I kappa B alpha processing. These dual-color protein interaction switches may enable directed dynamic analysis of a variety of protein interactions in living cells.
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