Cyclic AMP‐dependent protein kinase‐induced vimentin filament disassembly involves modification of the N‐terminal domain of intermediate filament subunits
- 4 July 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 234 (1) , 73-78
- https://doi.org/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.Keywords
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