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Vol. 53, Issue 5, 827-836, May 1998
Neuroscience Laboratory, A role for phosphoinositides in the endocytosis of muscarinic
cholinergic receptors (mAChRs) has been investigated via inhibition of
the activity of phosphatidylinositol-4-kinase (PI4K). Pretreatment of
SH-SY5Y neuroblastoma cells with micromolar concentrations of
wortmannin (WT), LY-294002, or phenylarsine oxide (PAO), three chemically distinct agents known to inhibit PI4K, resulted in both an
inhibition of agonist-induced endocytosis of mAChRs and a selective
reduction in the 32P-labeling of
phosphatidylinositol-4-phosphate. PAO-mediated inhibition of both
receptor endocytosis and phosphoinositide synthesis could be fully
reversed by inclusion of the bifunctional thiol 2,3-dimercaptopropanol. The requirement for phosphoinositide synthesis in mAChR endocytosis was
independent of a role for these lipids in the maintenance of the
cytoskeleton because disruption of the latter with cytochalasin D,
ML-7, or colchicine failed to inhibit receptor internalization. Determination of PI4K activity in subcellular fractions of SH-SY5Y cells indicated that enzyme activity in fractions enriched in endocytic
vesicles and cytosol was preferentially inhibited by WT, LY-294002, and
PAO, a profile consistent with the subcellular distribution of the
110-kDa 
isoform of PI4K, as determined by Western blot analysis.
Activity of PI4K present in immunoprecipitated cell lysates was
inhibited >75% by inclusion of each of the three inhibitors. These
results indicate that ongoing synthesis of phosphoinositides is
necessary for mAChR endocytosis and that the activity of a WT-sensitive
form of PI4K, such as PI4K, is required.
Copyright © 1998 by The American Society for Pharmacology and Experimental Therapeutics
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