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J. Biol. Chem., Vol. 264, Issue 6, 3206-3210, Feb, 1989
CD Smith and KJ Chang
Incorporation of 32P from [gamma-32P]ATP into phosphatidylinositol 4,5-
bisphosphate (PIP2) in membranes isolated from rat brain was enhanced in a
concentration-dependent manner by the GTP analogue guanosine 5'-O-
(thio)triphosphate (GTP gamma S). In contrast, neither the labeling of
phosphatidylinositol 4-phosphate in the same membranes nor PIP kinase
activity in the soluble fraction were stimulated by GTP gamma S. Synthesis
of [32P]PIP2 was not stimulated by GTP, GDP, GMP, or ATP; however, the
stimulatory effects of GTP gamma S were antagonized by GTP, GDP, and
guanosine 5'-O-thiodiphosphate (GDP beta S). The nucleotide-stimulated
labeling of PIP2 was not due to protection of [gamma-32P] ATP from
hydrolysis, activation of PIP2 hydrolysis by phospholipase C, or inhibition
of PIP2 hydrolysis by its phosphomonoesterase. Therefore,
phosphatidylinositol 4-phosphate kinase activity in brain membranes may be
regulated by a guanine nucleotide regulatory protein. This system may
enhance the resynthesis of PIP2 following receptor-mediated activation of
phospholipase C.
Regulation of brain phosphatidylinositol-4-phosphate kinase by GTP analogues. A potential role for guanine nucleotide regulatory proteins
Division of Cell Biology, Burroughs Wellcome Co., Research Triangle Park, North Carolina 27709.
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