Thèse soutenue

FR
Auteur / Autrice : Dong Liang
Direction : Yinghe HuJean Massoulié
Type : Thèse de doctorat
Discipline(s) : Biologie cellulaire et moléculaire
Date : Soutenance en 2008
Etablissement(s) : Paris 5

Mots clés

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Mots clés contrôlés

Résumé

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Both the catalytic domains and the C-terminal t peptides contribute to the capacity of cholinesterases to form and secrete various oligomers. The AChE-PRiMA complex is at least partially contained in lipid rafts, both in the rat brain and in transfected neuroblastoma and COS cells. The potential phosphorylation sites and palmitoylation sites are not required for recruitment of the complex in the rafts. We undertook a search for such potential partners by two-hybrid strategies, both in yeast and in E. Coli. Five potential partners were obtained several times, and one of those obtained from the yeast screen appeared also positive in the bacterial screen. This corresponds to a zinc-finger rich protein, which may act as a transcriptional regulator but was also shown to bind a short C-terminal peptide from a membrane receptor. The CutA protein affects the processing of proteins in the secretory pathway, facilitating tetramerization of AChEt.