SAP102, a Novel Postsynaptic Protein That Interacts with NMDA Receptor Complexes In Vivo

Müller, Bettina; Kistner, Ute; Kindler, Stefan; Chung, Wook Joon; Kuhlendahl, Sven; Fenster, Steven D.; Lau, Lester F.; Veh, Rüdiger W.; Huganir, Richard L.; Gundelfinger, Eckart D.; Garner, Craig C.

doi:10.1016/s0896-6273(00)80157-9

Cited by 398 publications

(314 citation statements)

References 32 publications

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“…There are other examples showing, that more than one PDZ domain containing protein is binding to the same C-terminal target. For example the proteins PSD-95, SAP97, SAP102 are all binding to the C-terminus of the N-methyl-D-aspartatreceptor subtype 2 (NR2) (Kornau et al, 1995;Niethammer et al, 1996;MuÈ ller et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

Erdmann

Kuhlmann²,

Leßmann

et al. 2000

Oncogene

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Mutations of the tumor suppressor protein APC (Adenomatous Polyposis Coli) are linked to familiar and sporadic human colon cancer. Here we describe a novel interaction between the APC protein and the protein tyrosine phosphatase PTP-BL carrying ®ve PDZ protein ± protein interaction domains. Exclusively, the second PDZ domain (PDZ2) of PTP-BL is binding to the extreme C-terminus of the APC protein, as determined by yeast two-hybrid studies. Using surface plasmon resonance analysis we established a dissociation constant (K D ) of 8.1610 79 M. We ®nd that a naturally occurring splice insertion of ®ve amino acids (PDZ2b) abolishes its binding a nity to the APC protein. The in vivo interaction between PTP-BL and the APC protein was shown by coprecipitation experiments in transfected COS cells. Furthermore, in cultured epithelial Madine Carnine Kidney cells the subcellular colocalization was demonstrated for the nucleus and also for the tips of cellular extensions. The interaction of the APC protein with a protein tyrosine phosphatase may indirectly modulate the steady state levels of tyrosine phosphorylations of associated proteins, such as b-catenin playing a major role in the regulation of cell division, migration and cell adhesion. Oncogene (2000) 19, 3894 ± 3901.

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Section: Discussionmentioning

confidence: 99%

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

Erdmann

Kuhlmann²,

Leßmann

et al. 2000

Oncogene

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“…This interaction is likely to play an important role in the clustering of receptors at the membrane (Gomperts, 1996). The exact function of the SH3 and guanylate kinase of PSD-95 are poorly understood (Kistner et al, 1995;MuÈ ller et al, 1996). The ®rst two PDZ motifs of PSD-95 form a domain and mediate the binding to the receptors .…”

Section: Identi®cation Of New Human Cellular Proteins With Pdz Domainsmentioning

confidence: 99%

“…An important function is the clustering of receptors and their association with the cytoskeleton. These proteins are also important factors in signal transduction pathways, as it is now wellestablished for the wint/wingless pathway which involves the PDZ protein Dsh (Miller and Moon, 1996). Another interesting example is the phosphotyrosine phosphatase FAP1/PTP-BAS which regulates negatively the activity of Fas by its association with this receptor (Sato et al, 1995).…”

Section: Interaction Of the Viral Protein Tax With Pdz Proteinsmentioning

confidence: 99%

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

et al. 1998

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Infection by HTLV-1 has been correlated with the appearance of various proliferative or degenerative diseases. Some of these disorders have been observed in transgenic mice expressing the Tax protein, which is known to transactivate various viral and cellular promoters through interactions with several transcription factors. In this study we show that the C-terminus of this viral oncoprotein represents a motif permitting binding of Tax to the PDZ domains of several cellular proteins. A two-hybrid screen with Tax as bait indeed yielded complementary DNAs coding for six proteins including PDZ domains. Two of them correspond to truncated forms of the PSD-95 and b1-syntrophin proteins, another clone codes for a protein homologous to the product of the C. elegans gene lin-7. The other three clones code for new human members of the PDZ family of cellular proteins. The interaction of Tax with the products of these clones was con®rmed by immunoprecipitation assays in mammalian cells, and analysis of various mutants of Tax established the importance of the Cterminal amino acids for several of these interactions. These data suggest that Tax could perturb the normal function of targeted cellular proteins by strongly interacting with their PDZ domains.

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“…Other postsynaptic proteins sharing structural similarity with PSD-95 were subsequently identified: SAP102 (Muller et al 1996), PSD-93/chapsyn-110 (Brenman et al 1996;Kim et al 1996) and SAP97 (Muller et al 1995). Similarly, a group of PDZ molecules interacting with a-amino-3-hydroxy-5-methyl-4-isoxzolepropionic acid (AMPA)-type glutamate receptors has been identified.…”

mentioning

confidence: 99%

Selective reduction of a PDZ protein, SAP‐97, in the prefrontal cortex of patients with chronic schizophrenia

Toyooka

Iritani

Makifuchi

et al. 2002

Journal of Neurochemistry

111

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Many postsynaptic density proteins carrying postsynaptic density-95/discs large/zone occludens-1 (PDZ) domain(s) interact with glutamate receptors to control receptor dynamics and synaptic plasticity. Here we examined the expression of PDZ proteins, synapse-associated protein (SAP) 97, postsynaptic density (PSD)-95, chapsyn-110, GRIP1 and SAP102, in post-mortem brains of schizophrenic patients and control subjects, and evaluated their contribution to schizophrenic pathology. Among these PDZ proteins, SAP97 exhibited the most marked change: SAP97 protein levels were decreased to less than half that of the control levels specifically in the prefrontal cortex of schizophrenic patients. In parallel, its binding partner, GluR1, similarly decreased in the same brain region. The correlation between SAP97 and GluR1 levels in control subjects was, however, altered in schizophrenic patients. SAP102 levels were also significantly reduced in the hippocampus of schizophrenic patients, but this reduction was correlated with sample storage time and post-mortem interval. There were no changes in the levels of the other PDZ proteins in any of the regions examined. In addition, neuroleptic treatment failed to mimic the SAP97 change. These findings suggest that a phenotypic loss of SAP97 is associated with the postsynaptic impairment in prefrontal excitatory circuits of schizophrenic patients. Keywords: chapsyn-110, GRIP1, PSD-95, psychosis, SAP102, SAP97. Address correspondence and reprint requests to Hiroyuki Nawa, Department of Molecular Biology, Brain Research Institute, Niigata University, Asahimachi-dori 1-757, Niigata 951-8585, Japan. E-mail: hnawa@bri.niigata-u.ac.jpAbbreviations used: ABP, AMPA receptor-binding protein; AMPA, a-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid; BDNF, brainderived neurotrophic factor; DTT, dithiothreitol; LPT, long-term potentiation; NSE, neuron-specific enolase; PAGE, polyacrylamide gel electrophoresis; PDZ, PSD-95/discs large/zone occludens-1; PVDF, polyvinylidene difluoride; PSD, postsynaptic density; SAP, synapseassociated protein; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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SAP102, a Novel Postsynaptic Protein That Interacts with NMDA Receptor Complexes In Vivo

Cited by 398 publications

References 32 publications

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain

The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins

Selective reduction of a PDZ protein, SAP‐97, in the prefrontal cortex of patients with chronic schizophrenia

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