Premium
Fatty acid acylation of lens fiber plasma membrane proteins
Author(s) -
Manenti Stéphane,
Dunia Irène,
Benedetti E.Lucio
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80228-b
Subject(s) - acylation , lens (geology) , membrane , chemistry , fatty acid , lens fiber , biochemistry , cytoplasm , crystallin , fiber , biophysics , biology , organic chemistry , paleontology , catalysis
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.