Title: Fluorescence studies on the interaction of inhibitor-2 and okadaic acid with the catalytic subunit of type-1 phosphoprotein phosphatases
Authors: Picking, Wd ×
Kudlicki, W
Kramer, G
Hardesty, B
Vandenheede, Jackie
Merlevede, Wilfried
Park, Ik
Depaoliroach, A #
Issue Date: Oct-1991
Publisher: Amer chemical soc
Series Title: Biochemistry vol:30 issue:42 pages:10280-10287
Abstract: Phosphatase inhibitor 2 was mutagenized and expressed in Escherichia coli to produce a protein with a single cysteinyl residue at position 129. The newly introduced sulfhydryl group was labeled with a maleimide derivative of coumarin (CPM). The resulting fluorescent inhibitor 2 molecule (CPM-I2) retains biological activity and binds to the catalytic subunit of type 1 phosphatase (PP1-C) with a K(d) similar to the K(i) of native I2 (2-3 nM). Fluorescence anisotropy data indicate that kinase F(A) (glycogen synthase kinase 3) does not dissociate the CPM-I2.PP1-C complex but rather causes a conformational change in the I2 molecule that is retained even after the CPM-I2 is displaced by an excess of native I2. The fluorescence data presented here also indicate that okadaic acid and I2 are competitive for binding to PP1-C, even after kinase F(A) treatment of the CPM-I2.PP1-C complex.
ISSN: 0006-2960
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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