tailieunhanh - Báo cáo khoa học: The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids

Unusually among ATP-binding cassette proteins, the sulfonylurea receptor (SUR) acts as a channel regulator. ATP-sensitive potassium channels are octameric complexes composed of four pore-forming subunits and four regulatory SUR subunits. Two different genes encode SUR1 (ABCC8) and SUR2 (ABCC9), with the latter being differentially spliced to give SUR2A and SUR2B, which differ only in their C-terminal 42 amino acids. | The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids Heidi de Wet Constantina Fotinou Nawaz Amad Matthias Dreger and Frances M. Ashcroft Department of Physiology Anatomy and Genetics University of Oxford UK Keywords ATP-binding cassette transporter KATP channel sulfonylurea receptor SUR2A SUR2B Correspondence F. M. Ashcroft Department of Physiology Anatomy and Genetics Parks Road Oxford OX1 3PT UK Fax 44 1865 285812 Tel 44 1865 285810 E-mail Received 23 January 2010 revised 26 March 2010 accepted 8 April2010 doi Unusually among ATP-binding cassette proteins the sulfonylurea receptor SUR acts as a channel regulator. ATP-sensitive potassium channels are octameric complexes composed of four pore-forming subunits and four regulatory SUR subunits. Two different genes encode SUR1 ABCC8 and SUR2 ABCC9 with the latter being differentially spliced to give SUR2A and SUR2B which differ only in their C-terminal 42 amino acids. ATP-sensitive potassium channels containing these different SUR2 isoforms are differentially modulated by MgATP with SUR2B being activated more than SUR2A. We show here that purified SUR2B has a lower ATPase activity and a 10-fold lower Km for MgATP than SUR2A. Similarly the isolated nucleotide-binding domain NBD 2 of SUR2B was less active than that of SUR2A. We further found that the NBDs of SUR2B interact and that the activity of full-length SUR cannot be predicted from that of either the isolated NBDs or NBD mixtures. Notably deletion of the last 42 amino acids from NBD2 of SUR2 resulted in ATPase activity resembling that of NBD2 of SUR2A rather than that of NBD2 of SUR2B this might indicate that these amino acids are responsible for the lower ATPase activity of SUR2B and the isolated NBD2 of SUR2B. We suggest that the lower ATPase activity of SUR2B may result in enhanced duration of the .

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