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J. Biol. Chem., Vol. 265, Issue 4, 1924-1927, 02, 1990
Y Hashimoto, BA Perrino and TR Soderling
The hypothesis that calcineurin, the Ca2+/calmodulin-dependent protein
phosphatase, contains an autoinhibitory domain was tested using synthetic
peptides corresponding to regions of the carboxyl-terminus of calcineurin.
Of the several peptides analyzed, one, containing residues
I-T-S-F-E-E-A-K-G-L-D-R-I-N-E-R-M-P-P-R-R-D-A-M-P, gave complete inhibition
of its protein phosphatase activity. Using [32P]myosin light chain as
substrate an IC50 of about 10 microM was obtained with either native
calcineurin, assayed in the presence of Ca2+/calmodulin, or with
calcineurin subjected to partial proteolysis which converts it to a fully
active phosphatase when assayed in the presence of [ethylenebis
(oxyethylenenitrilo)]tetraacetic acid. With 50 mM p- nitrophenylphosphate
as substrate an IC50 of about 40 microM was observed. Studies with
overlapping peptides suggested that the sequence P-P-R-R-D-A-M-P was
essential but not sufficient for the observed inhibition. Kinetic analysis
indicated that the inhibition of phosphatase activity was not competitive
with respect to [32P]myosin light chain. This peptide did not show
significant inhibition of the catalytic subunits of protein phosphatases
type I or type IIA or of Ca2+/calmodulin-dependent protein kinase II. These
results indicate that amino acids within this sequence of calcineurin
constitute a unique autoinhibitory domain which interacts with the active
site and is responsible for the low basal phosphatase activity in the
absence of Ca2+/calmodulin.
Identification of an autoinhibitory domain in calcineurin
Howard Hughes Medical Institute, Vanderbilt University Medical School, Nashville, Tennessee 37232-0615.
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