Cyclic AMP-dependent protein kinase-induced vimentin filament disassembly involves modification of the N-terminal domain of intermediate filament subunits.
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.
Evans
R M
RM
Department of Pathology, University of Colorado Health Sciences Center, Denver 80262.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D003488:Cyanogen Bromide; D000242:Cyclic AMP / Q000494:pharmacology*; D003599:Cytoskeleton / Q000378:metabolism*; D007382:Intermediate Filaments / Q000378:metabolism*; D007700:Kinetics; D010446:Peptide Fragments / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism; D014746:Vimentin / Q000378:metabolism*
D010446:Peptide Fragments; D014746:Vimentin; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D014357:Trypsin; D003488:Cyanogen Bromide