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.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:45 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 10:27 p.m.) |
Indexed | 1 day, 14 hours ago (Sept. 4, 2025, 10:14 a.m.) |
Issued | 37 years, 2 months ago (July 4, 1988) |
Published | 37 years, 2 months ago (July 4, 1988) |
Published Online | 23 years, 10 months ago (Oct. 19, 2001) |
Published Print | 37 years, 2 months ago (July 4, 1988) |
@article{Evans_1988, title={Cyclic AMP‐dependent protein kinase‐induced vimentin filament disassembly involves modification of the N‐terminal domain of intermediate filament subunits}, volume={234}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(88)81306-1}, DOI={10.1016/0014-5793(88)81306-1}, number={1}, journal={FEBS Letters}, publisher={Wiley}, author={Evans, Robert M.}, year={1988}, month=jul, pages={73–78} }