Involvement of fodrin-binding proteins in the structure of the neuronal postsynaptic density and regulation by phosphorylation

Harry LeVine, Naji E. Sahyoun

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)59-65
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume138
Issue number1
DOIs
StatePublished - Jul 16 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Involvement of fodrin-binding proteins in the structure of the neuronal postsynaptic density and regulation by phosphorylation'. Together they form a unique fingerprint.

Cite this