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(Received for publication, June 13, 1996, and in revised form, September 17, 1996)
From the The ATP binding cassette transporter ABC1 is a
220-kDa glycoprotein expressed by macrophages and required for
engulfment of cells undergoing programmed cell death. Since members of
this family of proteins such as P-glycoprotein and cystic fibrosis transmembrane conductance regulator share the ability to transport anions, we have investigated the transport capability of ABC1 expressed
in Xenopus oocytes using iodide efflux and voltage-clamp techniques. We report here that ABC1 generates an anion flux sensitive to glibenclamide, sulfobromophthalein, and blockers of anion
transporters. The anion flux generated by ABC1 is up-regulated by
orthovanadate, cAMP, protein kinase A, and okadaic acid. In other ABC
transporters, mutating the conserved lysine in the nucleotide binding
folds was found to severely reduce or abolish hydrolysis of ATP, which in turn altered the activity of the transporter. In ABC1, replacement of the conserved lysine 1892 in the Walker A motif of the second nucleotide binding fold increased the basal ionic flux, did not alter
the pharmacological inhibitory profile, but abolished the response to
orthovanadate and cAMP agonists. Therefore, we conclude that ABC1 is a
cAMP-dependent and sulfonylurea-sensitive anion transporter.
Volume 272, Number 5,
Issue of January 31, 1997
pp. 2695-2699
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
and
Laboratoire de Neurobiologie Cellulaire,
CNRS, 31 Chemin J. Aiguier, 13402 Marseille Cedex 20, France and
the § Centre d'Immunologie, INSERM-CNRS de
Marseille-Luminy, Parc Scientifique de Luminy, 13288 Marseille Cedex 9, France
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