Cyclic AMP-dependent protein kinase-induced vimentin filament disassembly involves modification of the N-terminal domain of intermediate filament subunits

FEBS Lett. 1988 Jul 4;234(1):73-8. doi: 10.1016/0014-5793(88)81306-1.

Abstract

The intermediate filament protein vimentin was phosphorylated with cAMP-dependent protein kinase under conditions that induce filament disassembly. Digestion of phosphorylated vimentin with lysine-specific endoprotease and subsequent tryptic peptide mapping indicated that a 12 kDa N-terminal fragment contained all the phosphorylation sites found in the intact molecule. Analysis of cyanogen bromide digests indicated that two phosphorylated peptides were produced, with the major 32P-labeled species representing amino acid position 14-72, and a minor 32P-labeled peptide representing amino acid positions 1-13. These results demonstrate that phosphorylation of sites within the N-terminal head domain of vimentin are associated with phosphorylation induced filament disassembly.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Cricetinae
  • Cyanogen Bromide
  • Cyclic AMP / pharmacology*
  • Cytoskeleton / metabolism*
  • Intermediate Filaments / metabolism*
  • Kinetics
  • Peptide Fragments / metabolism
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Trypsin / metabolism
  • Vimentin / metabolism*

Substances

  • Peptide Fragments
  • Vimentin
  • Adenosine Triphosphate
  • Cyclic AMP
  • Protein Kinases
  • Trypsin
  • Cyanogen Bromide