Open AccessLenticular intermediate-sized filaments: biosynthesis and interaction with plasma membrane.
Author(s) -
Frans C.S. Ramaekers,
I. Dunia,
H. Dodemont,
E.L. Benedetti,
H. Bloemendal
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.10.3208
Subject(s) - membrane , cytoskeleton , vimentin , intermediate filament , bilayer , lens fiber , polysome , biophysics , reticulocyte , biochemistry , lipid bilayer , chemistry , biology , microbiology and biotechnology , lysis , ribosome , cell , rna , nucleus , immunohistochemistry , gene , immunology
Electron microscopical features of the lens fiber plasma membrane-cytoskeleton complex are suggestive of an intimate association between the intermediate-sized filaments (IF) and the lipid bilayer. Biochemical analysis of this complex reveals the occurrence of an appreciable amount of vimentin as a protein subunit of lenticular IF. Additional evidence for association between IF and membranes is provided by the observation that newly synthesized vimentin is associated with plasma membranes added to a reticulocyte lysate programmed with lens polyribosomes. Concomitantly alpha-crystallin polypeptide chains (alpha A2) are also found associated with the plasma membrane together with a hitherto unidentified 47-kilodalton protein. Once associated with the lipid bilayer, the vimentin polypeptide resists urea treatment, suggesting that it has become an integral constituent associated with part of the membrane.