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ZIP3, a new splice variant of the PKC-zeta-interacting protein family, binds to GABAC receptors, PKC-zeta, and Kv beta 2.

Authors: Croci, C  Brandstatter, JH  Enz, R 
Citation: Croci C, etal., J Biol Chem 2003 Feb 21;278(8):6128-35.
Pubmed: (View Article at PubMed) PMID:12431995
DOI: Full-text: DOI:10.1074/jbc.M205162200

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-zeta to target proteins. GABA(C) receptors are composed of three rho subunits (rho 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 rho 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 rho 3-binding region of ZIP3 contained a ZZ-zinc finger domain, which interacted with 10 amino acids conserved in rho 1-3 but not in GABA(A) receptors. Consistently, only rho 1-3 subunits bound to ZIP3. ZIP3 formed dimers with ZIP1-3 and interacted with PKC-zeta and the shaker-type potassium channel subunit Kv beta 2. Different domains of ZIP3 interacted with PKC-zeta and the rho 3 subunit, and simultaneous assembly of ZIP3, PKC-zeta and rho 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-zeta, ZIP3, and GABA(C) receptors.

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RGD Object Information
RGD ID: 634214
Created: 2003-08-29
Species: All species
Last Modified: 2003-08-29
Status: ACTIVE



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