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Journal of Neuroscience, Vol 13, 3064-3074, Copyright © 1993 by Society for Neuroscience
A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures
PJ Lombroso, JR Naegele, E Sharma and M Lerner
Child Study Center, Yale University School of Medicine, New Haven, Connecticut 06536.
Immunocytochemical and biochemical studies were conducted to characterize a
brain-specific protein tyrosine phosphatase, designated STEP for striatal
enriched phosphatase. STEP immunoreactivity was most intense in select
regions of the CNS receiving a dopaminergic input, and was localized to
cell bodies, dendrites, and axonal processes. Western blot analyses of rat
brain homogenates revealed a triplet of polypeptides with relative
mobilities (M(r)) of 46 kDa, 37 kDa, and 33 kDa enriched within the
striatum. Phase separation of protein homogenates by Triton X-114
extraction indicated that this triplet was enriched in soluble but not
membrane fractions. Affinity-purified STEP fusion protein exhibited
phosphatase activity while a mutated form of the STEP fusion protein
(Cys300Ser) showed no demonstrable phosphatase activity.
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270(1):
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