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

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
StatePublished - 1993

Fingerprint

Proteolysis
Neurofilament Proteins
Phosphorylation
Calpain
Calmodulin
Intermediate Filaments
Calcium-Binding Proteins
Metabolism
Calcium
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Phosphorylation modulates calpain-mediated proteolysis and calmodulin binding of the 200-kDa and 160-kDa neurofilament proteins. / Greenwood, Jeffrey A.; Troncoso, Juan C; Costello, Anthony C.; Johnson, Gail V W.

In: Journal of Neurochemistry, Vol. 61, No. 1, 1993, p. 191-199.

Research output: Contribution to journalArticle

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