High impact information on Dlgh3

• Recombinant proteins containing the carboxy-terminal tail of NMDA receptor subunit NR2B interact with SAP102 from rat brain homogenates [1].
• 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 [1].
• Antibodies directed against NMDA receptors coimmunoprecipitate SAP102 from rat brain synaptosomes [1].
• SAP102 is enriched in preparations of synaptic junctions, where it biochemically behaves as a component of the cortical cytoskeleton [1].
• Double-labeling experiments were performed for PSD-95 and for SAP 102 or PSD-93, respectively, two other members of the family of synapse-associated proteins [2].

Biological context of Dlgh3

• Synapse associated protein 102 is a novel binding partner to the cytoplasmic terminus of neurone-glial related cell adhesion molecule [3].

Anatomical context of Dlgh3

• In the OPL, however, PSD-95 and PSD-93 were found presynaptically, whereas SAP 102 was located postsynaptically at photoreceptor synapses [2].
• And, appending the N terminus of SAP-102 to PSD-95 results in localization of the chimera to both axons and dendrites [4].
• However, the labeling of the optic nerve fibre layer indicates additional functions of SAP102 in the retina [5].
• Functional expression of rat synapse-associated proteins SAP97 and SAP102 in Drosophila dlg-1 mutants: effects on tumor suppression and synaptic bouton structure [6].
• However, and most importantly, their expression > or = 14 days in vitro (DIV) was similar to that in vivo.The results of this study demonstrate that postnatal expression of all PMCAs, SAP102 and PSD95 is similar in both the in vivo hippocampus and the in vitro organotypic hippocampal slice culture [7].

Physical interactions of Dlgh3

• We identified synapse associated protein 102 (SAP102) as a new binding partner for NrCAM [3].
• All three PDZ domains in SAP102 bind the cytoplasmic tail of NR2B in vitro [1].

Regulatory relationships of Dlgh3

• Only a fraction (approximately 23%) of the SAP102 clusters expressed NR2A, suggesting SAP102 is also associated with other subunits or receptors [5].

Other interactions of Dlgh3

• No effect was detected for other members of the membrane-associated guanylate kinase protein family, such as SAP102 and PSD-95 [8].
• This is the first interaction reported for NrCAM, and its association with SAP102 suggests that it is part of a larger complex which can interact with many different signalling pathways [3].
• These events are paralleled by profound modifications of NMDA receptor NR2B subunit association with interacting elements, i.e., members of the membrane-associated guanylate kinase (MAGUK) protein family postsynaptic density-95, synapse-associated protein-97 and synapse-associated protein-102 [9].
• SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo [1].
• Double-labeling experiments were performed in order to find out whether SAP102 is involved with the clustering the N-methyl-D-aspartate (NMDA) receptor 2A subunit (NR2A) [5].

Analytical, diagnostic and therapeutic context of Dlgh3

• Immunofluorescence for SAP102 was most prominent in the inner plexiform layer (IPL) [5].
• Electron microscopy by use of pre-embedding immunocytochemistry showed that SAP102 is concentrated in the IPL in processes which are postsynaptic at bipolar cell ribbon synapses (dyads) [5].
• NMDARs are transported along microtubules on large tubulovesicular organelles, as indicated by immunoelectron microscopy, and are associated with EEA1 (early endosomal antigen 1) and SAP102 (synapse-associated protein 102), as indicated by immunocytochemistry [10].

References