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Vol. 11, Issue 8, 2591-2604, August 2000
-Like Isoform
Department of Biochemistry and Biophysics, Hormone Research
Institute, University of California, San Francisco, CA 94143-0534
The formation of small vesicles is mediated by cytoplasmic coats
the assembly of which is regulated by the activity of GTPases, kinases,
and phosphatases. A heterotetrameric AP-3 adaptor complex has been
implicated in the formation of synaptic vesicles from PC12 endosomes
(Faundez et al., 1998). When the small GTPase ARF1 is
prevented from hydrolyzing GTP, we can reconstitute AP-3 recruitment to
synaptic vesicle membranes in an assembly reaction that requires temperatures above 15°C and the presence of ATP suggesting that an
enzymatic step is involved in the coat assembly. We have now found an
enzymatic reaction, the phosphorylation of the AP-3 adaptor complex,
that is linked with synaptic vesicle coating. Phosphorylation occurs in
the 
3 subunit of the complex by a kinase similar to casein kinase
1
. The kinase copurifies with neuronal-specific AP-3. In vitro,
purified casein kinase I selectively phosphorylates the 3A and 3B
subunit at its hinge domain. Inhibiting the kinase hinders the
recruitment of AP-3 to synaptic vesicles. The same inhibitors that
prevent coat assembly in vitro also inhibit the formation of synaptic
vesicles in PC12 cells. The data suggest, therefore, that the mechanism
of AP-3-mediated vesiculation from neuroendocrine endosomes requires
the phosphorylation of the adaptor complex at a step during or after
AP-3 recruitment to membranes.
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