The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
Using mutagenesis, we investigated the importance of two vimentin domains: (a) a highly conserved segment near the carboxy end of the alpha-helical rod, and (b) the tail, with which the rod end is known to interact. As judged by in vitro filament assembly and expression in transiently transfected cells lacking an endogenous vimentin network, the rod-tail interaction is not essential for 10 nm filament structure in vitro or for formation of fibrous arrays in culture. However, when mutated, amino acid residues within the rod and the tail segments can cause perturbations in IF assembly and in IF network formation. Finally, our studies show that the vimentin tail seems to play a role both in thermodynamically stabilizing IF structure in vitro and in establishing proper IF networks in vivo.
McCormick
M B
MB
Howard Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637.
Kouklis
P
P
Syder
A
A
Fuchs
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D007381:Intermediate Filament Proteins / Q000235:genetics / Q000502:physiology; D007382:Intermediate Filaments / Q000378:metabolism* / Q000648:ultrastructure; D008870:Microtubules / Q000648:ultrastructure; D008969:Molecular Sequence Data; D009154:Mutation; D017354:Point Mutation; D017433:Protein Structure, Secondary; D014162:Transfection; D014746:Vimentin / Q000737:chemistry / Q000235:genetics / Q000502:physiology*
D007381:Intermediate Filament Proteins; D014746:Vimentin