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PMID: 6954471 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Lenticular intermediate-sized filaments: biosynthesis and interaction with plasma membrane.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 79 ·No. 10 ·1982-05-00 ·Pages 3208-12

Ramaekers FC, Dunia I, Dodemont HJ, Benedetti EL, Bloemendal H

Abstract

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.

MeSH Terms
Animals Cattle Cell Fractionation/methods Cell Membrane/ultrastructure Crystallins/metabolism Cytoskeleton/metabolism,ultrastructure Lens, Crystalline/ultrastructure Microscopy, Electron Molecular Weight Muscle Proteins/metabolism Vimentin
Chemicals
Crystallins Muscle Proteins Vimentin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ramaekers F C
Dunia I
Dodemont H J
Benedetti E L
Bloemendal H
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29 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.79.10.3208
Published
1982-05-00
Pages
3208-12
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC346384
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.79.10.3208 PMC Full Text View journal details
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