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J. Biol. Chem., Vol. 278, Issue 8, 6128-6135, February 21, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/8/6128    most recent M205162200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Croci, C. Articles by Enz, R. Search for Related Content PubMed PubMed Citation Articles by Croci, C. Articles by Enz, R. Social Bookmarking                      What's this?

ZIP3, a New Splice Variant of the PKC--interacting Protein Family, Binds to GABA_C Receptors, PKC-, and Kv2^*

Cristina Croci, Johann Helmut Brandstätter^§, and Ralf Enz^¶

From the  Emil-Fischer-Zentrum, Institut für Biochemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Fahrstrasse 17, 91054 Erlangen, Germany and ^§ Max-Planck-Institut für Hirnforschung, Abteilung Neuroanatomie, Deutschordenstrasse 46, 60528 Frankfurt, Germany

The correct targeting of modifying enzymes to ion channels and neurotransmitter receptors represents an important biological mechanism to control neuronal excitability. The recent cloning of protein kinase C-zeta interacting proteins (ZIP1, ZIP2) identified new scaffolds linking the atypical protein kinase PKC- to target proteins. GABA_C receptors are composed of three  subunits (1-3) that are highly expressed in the retina, where they are clustered at synaptic terminals of bipolar cells. A yeast two-hybrid screen for the GABA_C receptor 3 subunit identified ZIP3, a new C-terminal splice variant of the ZIP protein family. ZIP3 was ubiquitously expressed in non-neuronal and neuronal tissues, including the retina. The 3-binding region of ZIP3 contained a ZZ-zinc finger domain, which interacted with 10 amino acids conserved in 1-3 but not in GABA_A receptors. Consistently, only 1-3 subunits bound to ZIP3. ZIP3 formed dimers with ZIP1-3 and interacted with PKC- and the shaker-type potassium channel subunit Kv2. Different domains of ZIP3 interacted with PKC- and the 3 subunit, and simultaneous assembly of ZIP3, PKC- and 3 was demonstrated in vitro. Subcellular co-expression of ZIP3 binding partners in the retina supported the proposed protein interactions. Our results indicate the formation of a ternary postsynaptic complex containing PKC-, ZIP3, and GABA_C receptors.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF439403.

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