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Modulation of the ABCA1 transporter activity by protein kinase CK2

par Roosbeek, Stein;Peelman, Frank;Caster, Hans;Lensink, Marc ;Vandekerckhove, Joël;Chimini, Giovanna;Tavernier, Jan;Rosseneu, Maryvonne
Référence International congress series, 1262, page (574-577)
Publication Publié, 2004

Article révisé par les pairs

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Résumé :

We identified putative protein kinase CK2 phosphorylation sites in the cytoplasmic R1 and R2 domains, downstream of nucleotide binding domains (NBD) of the ABCA1 transporter, and tested their functional significance. In vitro, the recombinant ABCA1 NBD1+R1 domain, and not the NBD2+R2 domain, was phosphorylated by CK2. We identified T1242, T1243 and S1255 as the phosphorylated residues in the R1 domain. In HEK-293 cells, ABCA1 flippase activity, apolipoproteins AI and AII binding to the cell, and cellular phospholipid and cholesterol efflux were enhanced by mutations preventing CK2 phosphorylation of the threonine residues. Mutants mimicking threonine phosphorylation had activities close to that of WTABCA1. Our data therefore suggest that protein kinase CK2 might regulate the transport activity of ABCA1 in vivo.D2003 Published by Elsevier B.V.