ZIP3, a New Splice Variant of the PKC-ζ-interacting Protein Family, Binds to GABAC Receptors, PKC-ζ, and Kvβ2

Croci, Cristina; Brandstätter, Johann Helmut; Enz, Ralf

doi:10.1074/jbc.m205162200

Cited by 54 publications

(100 citation statements)

References 58 publications

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“…For binding assays with native proteins, rat brains were homogenized in 0.32 M Saccharose, 20 mM Tris-HCl, pH 7.4, containing DNaseI and protease inhibitors (Roche Diagnostics) and centrifuged at 700 ϫ g for 5 min as described (32). The supernatant was collected and centrifuged at 30,000 ϫ g for 30 min, and 5 mg of the resulting supernatant were incubated with glutathione-Sepharose beads, coated with GST or GST fusion proteins, for 5 h under slow agitation.…”

Section: Methodsmentioning

confidence: 99%

“…Fusion proteins were purified under native conditions, immobilized to glutathione-Sepharose beads, and incubated with the cytosolic fractions of E. coli expressing PP1␥1 as described (31,32). C-terminal domains of mGluR1a, -5a, and -5b were also synthesized in vitro using the T7 promoter of pET41 according to the RiboMAX RNA Production Kit and the Flexi Rabbit Reticulocyte Lysate System (Promega) in the presence of [ 35 S]methionine (Amersham Biosciences).…”

Section: Methodsmentioning

confidence: 99%

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Group I Metabotropic Glutamate Receptors Bind to Protein Phosphatase 1C

Croci

Sticht

Brandstätter

et al. 2003

Journal of Biological Chemistry

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The modulation of neurotransmitter receptors by kinases and phosphatases represents a key mechanism in controlling synaptic signal transduction. However, molecular determinants involved in the specific targeting and interactions of these enzymes are largely unknown. Here, we identified both catalytic ␥-isoforms of protein phosphatase 1C (PP1␥1 and PP1␥2) as binding partners of the group I metabotropic glutamate receptors type 1a, 5a, and 5b in yeast cells and pull-down assays, using recombinant and native protein preparations. The tissue distribution of interacting proteins was compared, and protein phosphatase 1C was detected in dendrites of retinal bipolar cells expressing the respective interacting glutamate receptors. We mapped interacting domains within binding partners and identified five amino acids in the intracellular C termini of the metabotropic glutamate receptors type 1a, 5a, 5b, and 7b being both necessary and sufficient to bind protein phosphatase 1C. Furthermore, we show a dose-dependent competition of these C termini in binding the enzyme. Based on our data, we investigated the structure of the identified amino acids bound to protein phosphatase 1C by homology-based molecular modeling. In summary, these results provide a molecular description of the interaction between protein phosphatase 1C and metabotropic glutamate receptors and thereby increase our understanding of glutamatergic signal transduction.The correct targeting and localization of proteins to synaptic specializations represents an important biological mechanism to regulate neuronal excitability. Increasing evidence underlines the importance of macromolecular signaling complexes, where functionally related proteins such as ion channels, neurotransmitters receptors, kinases, and phosphatases are arranged in close vicinity and are physically anchored to the synaptic cytoskeleton. Therefore, identification and characterization of interactions between synaptically localized proteins adds substantially to our understanding of molecular mechanisms of neurotransmission.Receptors for glutamate are divided in ion channel-associated (ionotropic) receptors of the AMPA-, Kainate-, and NMDAtype and in G-protein coupled (metabotropic) receptors. Although ionotropic glutamate receptors mediate fast synaptic transmission, metabotropic glutamate receptors (mGluRs) 1 modulate neuronal excitability and development, synaptic plasticity, transmitter release, and memory function using a variety of intracellular second messenger systems (1). The eight known members of this protein family are sub-divided into three groups, based on sequence homology, associated second messenger systems, and pharmacological properties (2). mGluR1 and mGluR5 (group I) stimulate phospholipase C, are selectively activated by quisqualate, and are generally expressed perisynaptically at postsynaptic sites (3-7). mGluR2 and mGluR3 (group II) are negatively coupled to adenylyl cyclase and do not show a specific preference for pre-or postsynaptic neurons (8 -10). mGluR4, mGluR7, and...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Group I Metabotropic Glutamate Receptors Bind to Protein Phosphatase 1C

Croci

Sticht

Brandstätter

et al. 2003

Journal of Biological Chemistry

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“…In addition to binding Tax1BP1, TRAF-6 interacts with members of the PKC-ζ interacting protein family that are termed p62 or ZIP1-3 [31]. Interestingly, as Tax1BP1, also ZIP proteins bind to the TM3-4 loops of GABA C receptor ρ subunits and it was proposed that ZIP proteins function as a linker between GABA C receptors and PKC-ζ [11]. Similar to Tax1BP1, ZIP proteins use different domains to bind GABA C receptors, TRAF-6 and PKC-ζ and thus could serve as a scaffold between these proteins [11,31].…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, as Tax1BP1, also ZIP proteins bind to the TM3-4 loops of GABA C receptor ρ subunits and it was proposed that ZIP proteins function as a linker between GABA C receptors and PKC-ζ [11]. Similar to Tax1BP1, ZIP proteins use different domains to bind GABA C receptors, TRAF-6 and PKC-ζ and thus could serve as a scaffold between these proteins [11,31]. This hypothesis is supported by our finding that Tax1BP1 and the ZIP-binding PKC-ζ are co-localized with GABA C receptors in the retina.…”

Section: Discussionmentioning

confidence: 99%

“…The intracellular loop between TM3 and TM4 contains consensus sequences for enzymes and phosphorylation of this region was demonstrated in [8]. In recent years, several proteins binding to the TM3-4 loop of different ρ subunits were identified, including proteins of the ZIP family that interact with PKC (protein kinase C), GLYT-1 (glycine transporter-1), CRABP-I (cellular retinoic acid-binding protein-I) and MAP-1B (microtubule-associated protein 1B) [9][10][11][12]. However, MAP-1B knockout mice had a normal retina [13] and the physiological consequences of the other protein interactions have not been elucidated either.…”

Section: Introductionmentioning

confidence: 99%

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Tax1-binding protein 1 is expressed in the retina and interacts with the GABAC receptor ρ1 subunit

Ulrich

Seeber

Becker

et al. 2006

Biochemical Journal

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Macromolecular signalling complexes that link neurotransmitter receptors to functionally and structurally associated proteins play an important role in the regulation of neurotransmission. Thus the identification of proteins binding to neurotransmitter receptors describes molecular mechanisms of synaptic signal transduction. To identify interacting proteins of GABA C (where GABA is γ -aminobutyric acid) receptors in the retina, we used antibodies specific for GABA C receptor ρ1-3 subunits. Analysis of immunoprecipitated proteins by MALDI-TOF MS (matrixassisted laser-desorption ionization-time-of-flight MS) identified the liver regeneration-related protein 2 that is identical with amino acids 253-813 of the Tax1BP1 (Tax1-binding protein 1). A Cterminal region of Tax1BP1 bound to an intracellular domain of the ρ1 subunit, but not to other subunits of GABA C , GABA A or glycine receptors. Confocal laser-scanning microscopy demonstrated co-localization of Tax1BP1 and ρ1 in clusters at the cell membrane of transfected cells. Furthermore, Tax1BP1 and GABA C receptors were co-expressed in both synaptic layers of the retina, indicating that Tax1BP1 is a component of GABA C receptor-containing signal complexes.

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Expression and Purification of ZNF191(243–368) in Three Expression Systems

Zhao¹,

Teng²,

Ding³

et al. 2007

Chin. J. Chem.

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ZNF191(243-368), a new human zinc finger protein, probably relates to some hereditary diseases and cancers. To obtain adequate amount of ZNF191(243-368) for the study of its property, structure and function, three different expression systems of inclusion-body, glutathione S-transferase (GST), and hexahistidine (6×His) were used and compared. Among these systems, the expression level of ZNF191(243-368) was increased in inclusion body system under a higher isopropylthio-β-D-galactoside (IPTG) concentration, but the non-target proteins were also increased more, which made its purification more difficult and the yield lower. The expression of His-tag fusion protein was almost not affected by IPTG concentration, temperature and inducing time. At a high IPTG concentration the highest expression yield for GST fusion protein was obtained. And the fusion proteins can be partially purified by a single affinity chromatography step. The fusion protein systems show advantages for expression of these proteins.

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ZIP3, a New Splice Variant of the PKC-ζ-interacting Protein Family, Binds to GABAC Receptors, PKC-ζ, and Kvβ2

Cited by 54 publications

References 58 publications

Group I Metabotropic Glutamate Receptors Bind to Protein Phosphatase 1C

Group I Metabotropic Glutamate Receptors Bind to Protein Phosphatase 1C

Tax1-binding protein 1 is expressed in the retina and interacts with the GABAC receptor ρ1 subunit

Expression and Purification of ZNF191(243–368) in Three Expression Systems

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