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Updated: Aug 8, 2026

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay
Published on: January 20, 2015
The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase
K Haraguchi1, K Satoh, H Yanai
1Laboratory of Molecular and Genetic Information, Institute for Molecular and Cellular Biosciences, The University of Tokyo, Japan.
Background:
Postsynaptic density (PSD)-95 interacts with and mediates clustering of the N-methyl-D-aspartate-receptors (NMDA-R). PSD-95 also interacts with the hDLG-associated protein DAP, which is also called Synapse-associated protein 90-associated protein (SAPAP), and Guanylate kinase-associated protein (GKAP).
Results:
DAP interacted directly with the dynein light chain (DLC) family of proteins. DLC was contained in the NMDA-R-PSD-95-DAP-neuronal nitric oxide synthase (nNOS) complex. Furthermore, DAP interacted with nNOS and recruited it into the Triton X-100-insoluble fraction of transfected cells.
Conclusion:
DAP interacts directly with DLC and nNOS, and links these proteins to the NMDA-R-PSD-95 complex.
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