Fatty acid acylation of lens fiber plasma membrane proteins: MP26 and α-crystallin are palmitoylated

We describe in this report the fatty acylation of some of the main polypeptides from the eye lens fibers. MP26, the major lens fiber plasma membrane protein, and probably MP22, its natural degradation product, are palmitoylated in a post-translational process. This is also the case for α-crystallin,...

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Bibliographic Details
Published in:FEBS letters 1990-03, Vol.262 (2), p.356-358
Main Authors: Manenti, Stéphane, Dunia, Irène, Benedetti, E.Lucio
Format: Article
Language:English
Subjects:
a-crystallin
Acylation
alpha -crystallin
Analytical, structural and metabolic biochemistry
Animals
Aquaporins
Biological and medical sciences
Cell Membrane - metabolism
Crystallins - metabolism
Eye Proteins - metabolism
Fatty acylation
Fundamental and applied biological sciences. Psychology
Lens fiber
Lens, Crystalline - metabolism
Membrane Glycoproteins
membrane proteins
Membrane Proteins - metabolism
Miscellaneous
MP26
MP26protein
Myristates - metabolism
Palmitic Acid
Palmitic Acids - metabolism
plasma membranes
Proteins
Rats
Citations: Items that this one cites
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Summary:We describe in this report the fatty acylation of some of the main polypeptides from the eye lens fibers. MP26, the major lens fiber plasma membrane protein, and probably MP22, its natural degradation product, are palmitoylated in a post-translational process. This is also the case for α-crystallin, a major cytoplasmic structural protein shown to interact directly with the plasma membrane. Furthermore, a 65 kDa non-identified polypeptide and a high molecular weight component are also modified in the same way.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)80228-B