SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo

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

doi:10.1016/S0896-6273(00)80157-9

SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo

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

School of Medicine

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352 Scopus citations

Abstract

Synapse-associated proteins (SAPs) are constituents of the pre- and postsynaptic submembraneous cytomatrix. Here, we present SAP102, a novel 102 kDa SAP detected in dendritic shafts and spines of asymmetric type 1 synapses. SAP102 is enriched in preparations of synaptic junctions, where it biochemically behaves as a component of the cortical cytoskeleton. Antibodies directed against NMDA receptors coimmunoprecipitate SAP102 from rat brain synaptosomes. Recombinant proteins containing the carboxy-terminal tail of NMDA receptor subunit NR2B interact with SAP102 from rat brain homogenates. All three PDZ domains in SAP102 bind the cytoplasmic tail of NR2B in vitro. These data represent direct evidence that in vivo SAP102 is involved in linking NMDA receptors to the submembraneous cytomatrix associated with postsynaptic densities at excitatory synapses.

Original language	English (US)
Pages (from-to)	255-265
Number of pages	11
Journal	Neuron
Volume	17
Issue number	2
DOIs	https://doi.org/10.1016/S0896-6273(00)80157-9
State	Published - Aug 1996

ASJC Scopus subject areas

General Neuroscience

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10.1016/S0896-6273(00)80157-9

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title = "SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo",

abstract = "Synapse-associated proteins (SAPs) are constituents of the pre- and postsynaptic submembraneous cytomatrix. Here, we present SAP102, a novel 102 kDa SAP detected in dendritic shafts and spines of asymmetric type 1 synapses. SAP102 is enriched in preparations of synaptic junctions, where it biochemically behaves as a component of the cortical cytoskeleton. Antibodies directed against NMDA receptors coimmunoprecipitate SAP102 from rat brain synaptosomes. Recombinant proteins containing the carboxy-terminal tail of NMDA receptor subunit NR2B interact with SAP102 from rat brain homogenates. All three PDZ domains in SAP102 bind the cytoplasmic tail of NR2B in vitro. These data represent direct evidence that in vivo SAP102 is involved in linking NMDA receptors to the submembraneous cytomatrix associated with postsynaptic densities at excitatory synapses.",

author = "M{\"u}ller, {Bettina M.} and Ute Kistner and Stefan Kindler and Chung, {Wook Joon} and Sven Kuhlendahl and Fenster, {Steven D.} and Lau, {Lit Fui} and Veh, {R{\"u}diger W.} and Huganir, {Richard L.} and Gundelfinger, {Eckart D.} and Garner, {Craig C.}",

note = "Funding Information: Correspondence should be addressed to C. C. G. at the University of Alabama, Birmingham (UAB). We would like to thank Elizabeth Sztul for critical reading, Olaf Mundigl (Yale University) for the hippocampal cultures, and Mary Ann Accavitti of the UAB hybridoma facility for production of SAP102 monoclonal antibodies. This work was supported by the Federal Government of Germany (BMBF), the National Institutes of Health (P50 HD32901), the Howard Hughes Medical Institute, and the Deutsche Forschungsgemeinschaft (Ri 192-19-1). ",

year = "1996",

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doi = "10.1016/S0896-6273(00)80157-9",

language = "English (US)",

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T1 - SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo

AU - Müller, Bettina M.

AU - Kistner, Ute

AU - Kindler, Stefan

AU - Chung, Wook Joon

AU - Kuhlendahl, Sven

AU - Fenster, Steven D.

AU - Lau, Lit Fui

AU - Veh, Rüdiger W.

AU - Huganir, Richard L.

AU - Gundelfinger, Eckart D.

AU - Garner, Craig C.

N1 - Funding Information: Correspondence should be addressed to C. C. G. at the University of Alabama, Birmingham (UAB). We would like to thank Elizabeth Sztul for critical reading, Olaf Mundigl (Yale University) for the hippocampal cultures, and Mary Ann Accavitti of the UAB hybridoma facility for production of SAP102 monoclonal antibodies. This work was supported by the Federal Government of Germany (BMBF), the National Institutes of Health (P50 HD32901), the Howard Hughes Medical Institute, and the Deutsche Forschungsgemeinschaft (Ri 192-19-1).

PY - 1996/8

Y1 - 1996/8

N2 - Synapse-associated proteins (SAPs) are constituents of the pre- and postsynaptic submembraneous cytomatrix. Here, we present SAP102, a novel 102 kDa SAP detected in dendritic shafts and spines of asymmetric type 1 synapses. SAP102 is enriched in preparations of synaptic junctions, where it biochemically behaves as a component of the cortical cytoskeleton. Antibodies directed against NMDA receptors coimmunoprecipitate SAP102 from rat brain synaptosomes. Recombinant proteins containing the carboxy-terminal tail of NMDA receptor subunit NR2B interact with SAP102 from rat brain homogenates. All three PDZ domains in SAP102 bind the cytoplasmic tail of NR2B in vitro. These data represent direct evidence that in vivo SAP102 is involved in linking NMDA receptors to the submembraneous cytomatrix associated with postsynaptic densities at excitatory synapses.

AB - Synapse-associated proteins (SAPs) are constituents of the pre- and postsynaptic submembraneous cytomatrix. Here, we present SAP102, a novel 102 kDa SAP detected in dendritic shafts and spines of asymmetric type 1 synapses. SAP102 is enriched in preparations of synaptic junctions, where it biochemically behaves as a component of the cortical cytoskeleton. Antibodies directed against NMDA receptors coimmunoprecipitate SAP102 from rat brain synaptosomes. Recombinant proteins containing the carboxy-terminal tail of NMDA receptor subunit NR2B interact with SAP102 from rat brain homogenates. All three PDZ domains in SAP102 bind the cytoplasmic tail of NR2B in vitro. These data represent direct evidence that in vivo SAP102 is involved in linking NMDA receptors to the submembraneous cytomatrix associated with postsynaptic densities at excitatory synapses.

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SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo

Abstract

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