PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse

Disruption of the presynaptically enriched polyphosphoinositide phosphatase synaptojanin 1 leads to an increase of clathrin-coated intermediates and of polymerized actin at endocytic zones of nerve terminals. These changes correlate with elevated levels of PI(4,5)P(2) in neurons. We report that phos...

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Bibliographic Details
Published in:Neuron (Cambridge, Mass.) Mass.), 2001-10, Vol.32 (1), p.79-88
Main Authors: Wenk, M R, Pellegrini, L, Klenchin, V A, Di Paolo, G, Chang, S, Daniell, L, Arioka, M, Martin, T F, De Camilli, P
Format: Article
Language:English
Subjects:
Actins - metabolism
Animals
Antibodies
Brain - enzymology
Clathrin - metabolism
Microscopy, Electron
Nerve Tissue Proteins - metabolism
Phosphatidylinositol 4,5-Diphosphate - biosynthesis
Phosphoric Monoester Hydrolases - metabolism
Phosphorylation
Phosphotransferases (Alcohol Group Acceptor) - analysis
Phosphotransferases (Alcohol Group Acceptor) - immunology
Phosphotransferases (Alcohol Group Acceptor) - metabolism
Rabbits
Rats
Synaptic Membranes - enzymology
Synaptic Membranes - ultrastructure
Synaptic Vesicles - enzymology
Synaptic Vesicles - ultrastructure
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Summary:Disruption of the presynaptically enriched polyphosphoinositide phosphatase synaptojanin 1 leads to an increase of clathrin-coated intermediates and of polymerized actin at endocytic zones of nerve terminals. These changes correlate with elevated levels of PI(4,5)P(2) in neurons. We report that phosphatidylinositol phosphate kinase type Igamma (PIPKIgamma), a major brain PI(4)P 5-kinase, is concentrated at synapses. Synaptojanin 1 and PIPKIgamma antagonize each other in the recruitment of clathrin coats to lipid membranes. Like synaptojanin 1 and other proteins involved in endocytosis, PIPKIgamma undergoes stimulation-dependent dephosphorylation. These results implicate PIPKIgamma in the synthesis of a PI(4,5)P(2) pool that acts as a positive regulator of clathrin coat recruitment and actin function at the synapse.
ISSN:0896-6273