Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

DAP-1, a novel protein that interacts with the guanylate kinase-like domains of hDLG and PSD-95.

http://www.ncbi.nlm.nih.gov/pubmed/9286858

BACKGROUND: The human homologue of the Drosophila discs large tumour suppressor protein (hDLG) and closely related proteins such as postsynaptic density protein 95 kDa (PSD-95) are associated with N-methyl-D-aspartate receptors (NMDA-R) and Shaker-type K+ channels, and are thought to be involved in their clustering. RESULTS: We have identified a protein named DAP-1 that binds to the guanylate kinase-like domains of hDLG and PSD-95. DAP-1 was found to associate with hDLG, PSD-95, NMDA-R and adenomatous polyposis coli protein (APC). Furthermore, we found that DAP-1 is specifically expressed in the brain and colocalizes with PSD-95 and APC in mouse cerebellum. We also found that DAP-1 is colocalized with PSD-95 and NMDA-R at the synapses in cultured rat hippocampal neurons. CONCLUSION: Our findings suggest that DAP-1 may play several roles in the molecular organization of synapses and neuronal cell signalling by interacting with hDLG and PSD-95, which in turn are associated with receptors, ion channels and APC.

Pubmed ID: 9286858 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Adenomatous Polyposis Coli Protein | Amino Acid Sequence | Animals | Apoptosis Regulatory Proteins | Binding Sites | Brain | Cerebellum | Cloning, Molecular | Cytoskeletal Proteins | Guanylate Kinase | Hippocampus | Humans | Intracellular Signaling Peptides and Proteins | Male | Membrane Proteins | Mice | Microscopy, Immunoelectron | Molecular Sequence Data | Nerve Tissue Proteins | Neurons | Nucleoside-Phosphate Kinase | Precipitin Tests | Proteins | Rabbits | Rats | Receptors, N-Methyl-D-Aspartate | Repetitive Sequences, Nucleic Acid | Sequence Homology, Amino Acid

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

None

BioGRID (Data, Interactions)

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.