Abstract
We show here that an active Cdk5-p35 kinase is present in Golgi membranes, where it associates with a detergent-insoluble fraction containing actin. In addition, Cdk5-p35-dependent phosphorylation of alpha-PAK immunoreactive protein species was detected in Golgi membranes, as well as an interaction with the small GTPase, Cdc42. Moreover, antisense oligonucleotide suppression of Cdk5 or p35 in young cultured neurons, as well as inhibition of Cdk5 activity with olomoucine, blocks the formation of membrane vesicles from the Golgi apparatus. Taken together, these results show a novel subcellular localization of this kinase and suggest a role for Cdk5-p35 in membrane traffic during neuronal process outgrowth.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Biological Transport
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Blotting, Western
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Brain / metabolism
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Cell Differentiation
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Cell Membrane / metabolism*
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Cells, Cultured
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Centrifugation, Density Gradient
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Cyclin-Dependent Kinase 5
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Cyclin-Dependent Kinases / antagonists & inhibitors
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Cyclin-Dependent Kinases / metabolism*
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Golgi Apparatus / enzymology*
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Golgi Apparatus / metabolism
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Intracellular Membranes / metabolism*
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Microscopy, Fluorescence
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Nerve Tissue Proteins / antagonists & inhibitors
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Nerve Tissue Proteins / metabolism*
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Neurons / cytology
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Neurons / metabolism
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Rats
Substances
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Nerve Tissue Proteins
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neuronal Cdk5 activator (p25-p35)
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Cyclin-Dependent Kinase 5
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Cdk5 protein, rat
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Cyclin-Dependent Kinases