Interaction of S-SCAM with Neural Plakophilin-RelatedArmadillo-Repeat Protein/δ-Catenin

Ide, Nobuyuki; Hata, Yoshinobu; Deguchi, Maki; Hirao, Kazuyo; Yao, Ikuko; Takai, Yoshimi

doi:10.1006/bbrc.1999.0364

Cited by 71 publications

(48 citation statements)

References 21 publications

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“…The MAGI type postsynaptic scaffolding protein S-SCAM (26,29) has been described to potentially interact with catenins via binding with its PDZ5 domain to the PDZ-binding domains of β-catenin and δ-catenin (28,40). Furthermore, S-SCAM has been suggested to bind with its WW and PDZ1 domain to neuroligin-1 (27).…”

Section: Discussionmentioning

confidence: 99%

Essential cooperation of N-cadherin and neuroligin-1 in the transsynaptic control of vesicle accumulation

Stan¹,

Pielarski²,

Brigadski

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

115

116

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Cell adhesion molecules are key players in transsynaptic communication, precisely coordinating presynaptic differentiation with postsynaptic specialization. At glutamatergic synapses, their retrograde signaling has been proposed to control presynaptic vesicle clustering at active zones. However, how the different types of cell adhesion molecules act together during this decisive step of synapse maturation is largely unexplored. Using a knockout approach, we show that two synaptic adhesion systems, N-cadherin and neuroligin-1, cooperate to control vesicle clustering at nascent synapses. Live cell imaging and fluorescence recovery after photobleaching experiments at individual synaptic boutons revealed a strong impairment of vesicle accumulation in the absence of N-cadherin, whereas the formation of active zones was largely unaffected. Strikingly, also the clustering of synaptic vesicles triggered by neuroligin-1 overexpression required the presence of N-cadherin in cultured neurons. Mechanistically, we found that N-cadherin acts by postsynaptically accumulating neuroligin-1 and activating its function via the scaffolding molecule S-SCAM, leading, in turn, to presynaptic vesicle clustering. A similar cooperation of N-cadherin and neuroligin-1 was observed in immature CA3 pyramidal neurons in an organotypic hippocampal network. Moreover, at mature synapses, N-cadherin was required for the increase in release probability and miniature EPSC frequency induced by expressed neuroligin-1. This cooperation of two cell adhesion systems provides a mechanism for coupling bidirectional synapse maturation mediated by neuroligin-1 to cell type recognition processes mediated by classical cadherins.synapse maturation | synaptic adhesion molecules | vesicle clustering

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Section: Discussionmentioning

confidence: 99%

Essential cooperation of N-cadherin and neuroligin-1 in the transsynaptic control of vesicle accumulation

Stan¹,

Pielarski²,

Brigadski

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

115

116

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“…Adenomatous polyposis coli gene product interacts with PSD-95/SAP90 and SAP97/human Discs-large tumor suppressor gene (36). NPRAP/␦-catenin interacts with synaptic scaffolding molecule (15), and NPRAP/␦-catenin and p0071 bind to PAPIN. Because both the PDZ domain-containing protein family and the armadillo repeat-containing protein family are localized at cell-cell junctions, these interactions may be important in the architecture of cell-cell junctions.…”

Section: Discussionmentioning

confidence: 99%

“…pClneo Myc ␦-catenin was described previously (15). The following constructs contain the following amino acids of PAPIN: pGex5X-3 PAPIN-2, 526 -623; pGex5X-3 PAPIN-3, 526 -794; pGex5X-3 PAPIN-9, 1-422; pClneo PAPIN, * The costs of publication of this article were defrayed in part by the payment of page charges.…”

Section: Methodsmentioning

confidence: 99%

“…When transfected in Madin-Darby canine kidney cells, NPRAP/␦-catenin is localized at adherens junctions and interacts with E-cadherin and ␤-catenin (14). We have reported that NPRAP/␦-catenin interacts with a multiple PSD-95/Dlg-A/ZO-1 (PDZ) domain-containing protein named synaptic scaffolding molecule, which interacts with various synaptic components (15). These observations suggest that NPRAP/␦-catenin and p0071 play roles in the organization of cell-cell junctions.…”

mentioning

confidence: 99%

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Papin

Deguchi

Iizuka

Hata

et al. 2000

Journal of Biological Chemistry

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A neural plakophilin-related armadillo repeat protein (NPRAP)/␦-catenin interacts with one of Alzheimer disease-related gene products, presenilin 1. We have previously reported the interaction of NPRAP/␦-catenin with synaptic scaffolding molecule, which is involved in the assembly of synaptic components. NPRAP/␦-catenin also interacts with E-cadherin and ␤-catenin and is implicated in the organization of cell-cell junctions. p0071, a ubiquitous isoform of NPRAP/␦-catenin, is localized at desmosomes in HeLa and A431 cells and at adherens junctions in Madin-Darby bovine kidney cells. We have identified here a novel protein interacting with NPRAP/ ␦-catenin and p0071 and named this protein plakophilinrelated armadillo repeat protein-interacting PSD-95/ Dlg-A/ZO-1 (PDZ) protein (PAPIN). PAPIN has six PDZ domains and binds to NPRAP/␦-catenin and p0071 via the second PDZ domain. PAPIN and p0071 are ubiquitously expressed in various tissues and are localized at cell-cell junctions in normal rat kidney cells and bronchial epithelial cells. PAPIN may be a scaffolding protein connecting components of epithelial junctions with p0071.The armadillo repeat is a repeated motif of about 40 amino acids originally identified in the Drosophila segment polarity gene, armadillo (reviewed in Ref. 1). The list of proteins containing this repeat includes ␤-catenin, plakoglobin, adenomatous polyposis coli gene product, a regulatory protein for small G protein named smg GDP dissociation stimulator, and smg GDP-dissociation stimulator-associated protein (reviewed in Refs. 1 and 2). Among them, p120 ctn and its related proteins form a family. The p120 ctn family is composed of p120 ctn , B6P/ plakophilin 1, plakophilin 2, armadillo repeat gene deleted in velo-cardiofacial syndrome, p0071, and neural plakophilin-related armadillo repeat protein (NPRAP) 1 /␦-catenin (3-10). p120 ctn has been identified as a major substrate of tyrosine kinase phosphorylation enriched at adherens junctions and contains 10 armadillo repeats (3, 11-13). p120 ctn directly interacts with E-cadherin. B6P/plakophilin 1 is a protein localized at desmosomes and interacts with keratin (4, 5). Plakophilin 2 is also localized at desmosomes (6). armadillo repeat gene deleted in velo-cardiofacial syndrome has been isolated as a gene involved in a human disorder that affects the development of tissues related to pharyngeal arches and pouches and encodes a protein containing 10 armadillo repeats (10). p0071 also has 10 armadillo repeats and is colocalized with desmoplakin in HeLa and A431 cells, but localized at adherens junctions in Madin-Darby bovine kidney cells (8). NPRAP/␦-catenin was discovered independently by two groups as a protein homologous to B6P/plakophilin 1 and as a protein interacting with presenilin 1, respectively (9, 10). NPRAP/␦-catenin has a structure similar to that of p0071 and is considered to be a neural isoform of p0071. When transfected in Madin-Darby canine kidney cells, NPRAP/␦-catenin is localized at adherens junctions and interacts with E-cadhe...

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“…Although not directly tested here, this raises the possibility that cadherin-NPRAP complexes could bind PSD-95-neuroligin complexes, linking these two adhesion structures. Members of the NPRAP/␦-catenin/p120 family bind to yet other PDZ proteins, including synaptic scaffolding molecule (S-SCAM) (Ide et al, 1999) and PAPIN (Deguchi et al, 2000) and to the LAP protein, densin180 (Izawa et al, 2002).…”

Section: Cadherin Function At Synaptic Junctionsmentioning

confidence: 99%

Synaptic Anchorage of AMPA Receptors by Cadherins through Neural Plakophilin-Related Arm Protein–AMPA Receptor-Binding Protein Complexes

Silverman¹,

Restituito²,

Lü³

et al. 2007

J. Neurosci.

113

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Cadherins function in the adhesion of presynaptic and postsynaptic membranes at excitatory synapses. Here we show that the cadherinassociated protein neural plakophilin-related arm protein (NPRAP; also called ␦-catenin) binds via a postsynaptic density-95 (PSD-95)/ discs large/zona occludens-1 (PDZ) interaction to AMPA receptor (AMPAR)-binding protein (ABP) and the related glutamate receptor (GluR)-interacting protein (GRIP), two multi-PDZ proteins that bind the GluR2 and GluR3 AMPAR subunits. The resulting cadherin-NPRAP-ABP/GRIP complexes serve as anchorages for AMPARs. Exogenous NPRAP that was bound to cadherins at adherens junctions of Madin-Darby canine kidney cells recruited ABP from the cytosol to form cadherin-NPRAP-ABP complexes, dependent on NPRAP interaction with the ABP PDZ domain 2. The cadherin-NPRAP-ABP complexes also bound GluR2. In cultured hippocampal neurons, dominant-negative mutants of NPRAP designed to disrupt tethering of ABP to NPRAP-cadherin complexes reduced surface levels of endogenous GluR2, indicating that interaction with cadherin-NPRAP-ABP complexes stabilized GluR2 at the neuronal plasma membrane. Cadherins, NPRAP, GRIP, and GluR2 copurified in the fractionation of synaptosomes and the postsynaptic density, two fractions enriched in synaptic proteins. Furthermore, synaptosomes contain NPRAP-GRIP complexes, and NPRAP localizes with the postsynaptic marker PSD-95 and with AMPARs and GRIP at spines of hippocampal neurons. Thus, tethering is likely to take place at synaptic or perisynaptic sites. NPRAP also binds PSD-95, which is a scaffold for NMDA receptors, for AMPARs in complexes with auxiliary subunits, the TARPs (transmembrane AMPA receptor regulator proteins), and for adhesion molecules. Thus, the interaction of scaffolding proteins with cadherin-NPRAP complexes may anchor diverse signaling and adhesion molecules at cadherins.

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Interaction of S-SCAM with Neural Plakophilin-RelatedArmadillo-Repeat Protein/δ-Catenin

Cited by 71 publications

References 21 publications

Essential cooperation of N-cadherin and neuroligin-1 in the transsynaptic control of vesicle accumulation

Essential cooperation of N-cadherin and neuroligin-1 in the transsynaptic control of vesicle accumulation

Papin

Synaptic Anchorage of AMPA Receptors by Cadherins through Neural Plakophilin-Related Arm Protein–AMPA Receptor-Binding Protein Complexes

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