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Vol. 10, Issue 12, 4033-4041, December 1999

Phosphorylation of SNAP-23 by the Novel Kinase SNAK Regulates t-SNARE Complex Assembly

J.-P. Cabaniols,^* V. Ravichandran, and P.A. Roche

Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892

The docking and fusion of cargo-containing vesicles with target membranes of eukaryotic cells is mediated by the interaction of SNARE proteins present on both vesicle and target membranes. In many cases, the target membrane SNARE, or t-SNARE, exists as a complex of syntaxin with a member of the SNAP-25 family of palmitoylated proteins. We have identified a novel human kinase SNAK (SNARE kinase) that specifically phosphorylates the nonneuronal t-SNARE SNAP-23 in vivo. Interestingly, only SNAP-23 that is not assembled into t-SNARE complexes is phosphorylated by SNAK, and phosphorylated SNAP-23 resides exclusively in the cytosol. Coexpression with SNAK significantly enhances the stability of unassembled SNAP-23, and as a consequence, the assembly of newly synthesized SNAP-23 with syntaxin is augmented. These data demonstrate that phosphorylation of SNAP-23 by SNAK enhances the kinetics of t-SNARE assembly in vivo.

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^* Present address: Institut Pasteur, U277, Biologie Moleculaire du Gen, 25 rue du Dr. Roux, 75724 Paris Cedex 15, France.

Corresponding author. E-mail address: paul.roche{at}nih.gov.

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Molecular Biology of the Cell
Vol. 10, 4033-4041, December 1999
Copyright © 1999 by The American Society for Cell Biology

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