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Cyclic AMP‐dependent protein kinase‐induced vimentin filament disassembly involves modification of the N‐terminal domain of intermediate filament subunits
Author(s) -
Evans Robert M.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81306-1
Subject(s) - cyanogen bromide , vimentin , phosphorylation , protein filament , intermediate filament protein , intermediate filament , peptide , biochemistry , protein kinase a , chemistry , amino acid , peptide sequence , kinase , biology , cytoskeleton , cell , immunohistochemistry , immunology , gene
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 32 P‐labeled species representing amino acid position 14–72, and a minor 32 P‐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.