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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)255-265
Number of pages11
JournalNeuron
Volume17
Issue number2
DOIs
StatePublished - Aug 1996

ASJC Scopus subject areas

  • Neuroscience(all)

Fingerprint Dive into the research topics of 'SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo'. Together they form a unique fingerprint.

Cite this