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Ca2+-Mysristoyl switch and membrane binding of chemically acylated neurocalcins+


Type de document : Article de périodique
Langue : anglais

Responsabilité(s) secondaire (s) :



Editeur : AMERCIAN CHEMICAL SOCIETY


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Résumé anglais :

  • Neurocalcin is a member of a novel family of neuronal calcium sensors that belongs to the superfamily of EF-hand Ca2+-binding proteins. Neurocalcin is myristoylated on its N-terminus in vivo and can assoc. with biol. membranes in a calcium and myristoyl-dependent manner. This process known as "Ca2+-myristoyl switch" has been best described for the photoreceptor specific protein, recoverin, as well as for several other neuronal calcium sensors. Here, the authors used reversed micelles to chem. acylate nonmyristoylated neurocalcin at its N-terminus with fatty acids of different lengths (from C12 to C16). This approach allowed the authors to prep. neurocalcin derivs. in which a single fatty acid is selectively linked to the N-terminal glycine of the polypeptide chain through an amide bond. The membrane binding properties of the monoacylated neurocalcins were then examd. by cosedimentation with phospholipid vesicles and direct binding to lipid monolayers by surface plasmon resonance spectroscopy (Biacore). The authors' results show that neurocalcins monoacylated with lauric, myristic, or palmitic acid were able to assoc. with membrane in a calcium-dependent manner. This indicates that the Ca2+-myristoyl switch can function with different lipid moieties and is not strictly restricted to myristate. The ability to modify at will the fatty acid linked to the N-terminal glycine should be useful to analyze the contribution of the fatty acid moiety to the biol. function of this family of neuronal calcium sensors.

Note : Extrait de "BIOCHEMISTRY", Vol. 40, Issue 27, June 16, 2001, Pages 8152-8160


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