Phosphorylation Modulates Calpain‐Mediated Proteolysis and Calmodulin Binding of the 200‐kDa and 160‐kDa Neurofilament Proteins

Jeffrey A. Greenwood, Juan C. Troncoso, Anthony C. Costello, Gail V.W. Johnson

Research output: Contribution to journalArticle

Abstract

Abstract: The effects of enzymatic dephosphorylation on neurofilament interaction with two calcium‐binding proteins, calpain and calmodulin, were examined. Dephosphorylation increased the rate and extent of 200‐kDa neurofilament protein proteolysis by calpain. In contrast, dephosphorylation of the 160‐kDa neurofilament protein did not alter the rate or extent of calpain proteolysis. However, the calpain‐induced breakdown products of native and dephosphorylated 160‐kDa neurofilament protein were different. Dephosphorylation did not change the proteolytic rate, extent, or breakdown products of the 68‐kDa neurofilament protein. Calmodulin binding to the purified individual 160‐ and 200‐kDa neurofilament proteins was increased following dephosphorylation. These results suggest that phosphorylation may regulate the metabolism and function of neurofilaments by modulating interactions with the calcium‐activated proteins calpain and calmodulin.

Original languageEnglish (US)
Pages (from-to)191-199
Number of pages9
JournalJournal of Neurochemistry
Volume61
Issue number1
DOIs
StatePublished - Jul 1993

Keywords

  • Calcium ‐ activated proteins
  • Calmodulin
  • Calpain
  • Dephosphorylation
  • Neurofilament proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'Phosphorylation Modulates Calpain‐Mediated Proteolysis and Calmodulin Binding of the 200‐kDa and 160‐kDa Neurofilament Proteins'. Together they form a unique fingerprint.

  • Cite this