title: Fatty acid acylation of lens fiber plasma membrane proteins. MP26 and alpha-crystallin are palmitoylated.
abstract: 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 alpha-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.
authors.affiliation: Institut Jacques Monod, Université Paris VII, CNRS, France.
authors.forename: S
authors.initials: S
authors.lastname: Manenti
authors.forename: I
authors.initials: I
authors.lastname: Dunia
authors.forename: E L
authors.initials: EL
authors.lastname: Benedetti
mesh_terms: D000215:Acylation; D000818:Animals; D020346:Aquaporins; D002462:Cell Membrane / Q000378:metabolism; D003459:Crystallins / Q000378:metabolism*; D005136:Eye Proteins / Q000378:metabolism*; D007908:Lens, Crystalline / Q000378:metabolism*; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000378:metabolism*; D009226:Myristates / Q000378:metabolism; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism*; D051381:Rats
chemical_list: D020346:Aquaporins; D003459:Crystallins; D005136:Eye Proteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009226:Myristates; D010169:Palmitic Acids; C030328:aquaporin 0; D019308:Palmitic Acid