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Science 3 September 1999:
Vol. 285. no. 5433, pp. 1565 - 1569
DOI: 10.1126/science.285.5433.1565
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Reports

Differential Stimulation of PKC Phosphorylation of Potassium Channels by ZIP1 and ZIP2

Jianping Gong, Jia Xu, * Magdalena Bezanilla, dagger Rika van Huizen, Rachel Derin, Min Li ddagger

Targeting of protein modification enzymes is a key biochemical step to achieve specific and effective posttranslational modifications. Two alternatively spliced ZIP1 and ZIP2 proteins are described, which bind to both Kvbeta 2 subunits of potassium channel and protein kinase C (PKC) zeta , thereby acting as a physical link in the assembly of PKCzeta -ZIP-potassium channel complexes. ZIP1 and ZIP2 differentially stimulate phosphorylation of Kvbeta 2 by PKCzeta . They also interact to form heteromultimers, which allows for a hybrid stimulatory activity to PKCzeta . Finally, ZIP1 and ZIP2 coexist in the same cell type and are elevated differentially by neurotrophic factors. These results provide a mechanism for specificity and regulation of PKCzeta -targeted phosphorylation.

Department of Physiology and Department of Neuroscience, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
*   Present address: Aurora Biosciences Corporation, San Diego, CA 92121, USA.

dagger    Present address: The Salk Institute for Biological Studies, San Diego, CA 92186, USA.

ddagger    To whom correspondence should be addressed. E-mail: minli{at}jhmi.edu

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