Involvement of fodrin-binding proteins in the structure of the neuronal postsynaptic density and regulation by phosphorylation.
Novel polypeptides with Mr values about 140,000 bind fodrin and spectrin and are enriched in the postsynaptic density (PSD) compared to other tissues or subcellular fractions. 125I-fodrin binding to these polypeptides is competed for by unlabeled spectrin. These polypeptides are distinct from ankyrin and its proteolytic fragments and from band 4.1 which also bind fodrin. Phosphorylation of PSDs by the endogenous calmodulin-dependent protein kinase markedly reduces 125I-fodrin binding to the transblotted preparation. Such an event may play a regulatory role in governing protein-protein interactions among elements of the PSD.
D000818:Animals; D017487:Ankyrins; D001667:Binding, Competitive; D001798:Blood Proteins / Q000378:metabolism; D001923:Brain Chemistry; D002352:Carrier Proteins / Q000378:metabolism; D002450:Cell Communication; D002452:Cell Count; D003598:Cytoskeletal Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000378:metabolism; D008840:Microfilament Proteins / Q000378:metabolism; D008970:Molecular Weight; D009474:Neurons / Q000166:cytology*; D009479:Neuropeptides; D010766:Phosphorylation; D051381:Rats; D013049:Spectrin / Q000378:metabolism; D013569:Synapses / Q000378:metabolism*
D017487:Ankyrins; D001798:Blood Proteins; D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D009479:Neuropeptides; D013049:Spectrin; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1