Syntaxin-1A Inhibits Cardiac KATP Channels by Its Actions on Nucleotide Binding Folds 1 and 2 of Sulfonylurea Receptor 2A

ATP-sensitive potassium (KATP) channels couple the metabolic status of the cell to its membrane potential to regulate a number of cell actions, including secretion (neurons and neuroendocrine cells) and muscle contractility (skeletal, cardiac, and vascular smooth muscle). KATP channels consist of regulatory sulfonylurea receptors (SUR) and pore-forming (Kir6.X) subunits. We recently reported (Pasyk, E. A., Kang, Y., Huang, X., Cui, N., Sheu, L., and Gaisano, H. Y. (2004) J. Biol. Chem. 279, 4234–4240) that syntaxin-1A (Syn-1A), known to mediate exocytotic fusion, was capable of binding the nucleotide binding folds (NBF1 and C-terminal NBF2) of SUR1 to inhibit the KATP channels in insulin-secreting pancreatic islet beta cells. This prompted us to examine whether Syn-1A might modulate cardiac SUR2A/KATP channels. Here, we show that Syn-1A is present in the plasma membrane of rat cardiac myocytes and binds the SUR2A protein (of rat brain, heart, and human embryonic kidney 293 cells expressing SUR2A/Kir6. 2) at its NBF1 and NBF2 domains to decrease KATP channel activation. Unlike islet beta cells, in which Syn-1A inhibition of the channel activity was apparently mediated only via NBF1 and not NBF2 of SUR1, NBF1 and NBF2 of SUR2A to the of Syn-1A KATP channels in rat cardiac myocytes and cells expressing that Syn-1A binds of SUR1 and SUR2A to NBF2 of in the KATP channels in islet beta cells and cardiac ATP-sensitive potassium (KATP) channels couple the metabolic status of the cell to its membrane potential to regulate a number of cell actions, including secretion (neurons and neuroendocrine cells) and muscle contractility (skeletal, cardiac, and vascular smooth muscle). KATP channels consist of regulatory sulfonylurea receptors (SUR) and pore-forming (Kir6.X) subunits. We recently reported (Pasyk, E. A., Kang, Y., Huang, X., Cui, N., Sheu, L., and Gaisano, H. Y. (2004) J. Biol. Chem. 279, 4234–4240) that syntaxin-1A (Syn-1A), known to mediate exocytotic fusion, was capable of binding the nucleotide binding folds (NBF1 and C-terminal NBF2) of SUR1 to inhibit the KATP channels in insulin-secreting pancreatic islet beta cells. This prompted us to examine whether Syn-1A might modulate cardiac SUR2A/KATP channels. Here, we show that Syn-1A is present in the plasma membrane of rat cardiac myocytes and binds the SUR2A protein (of rat brain, heart, and human embryonic kidney 293 cells expressing SUR2A/Kir6. 2) at its NBF1 and NBF2 domains to decrease KATP channel activation. Unlike islet beta cells, in which Syn-1A inhibition of the channel activity was apparently mediated only via NBF1 and not NBF2 of SUR1, NBF1 and NBF2 of SUR2A to the of Syn-1A KATP channels in rat cardiac myocytes and cells expressing that Syn-1A binds of SUR1 and SUR2A to NBF2 of in the KATP channels in islet beta cells and cardiac ATP-sensitive potassium (KATP) KATP ATP-sensitive potassium sulfonylurea nucleotide binding protein human embryonic protein of KATP ATP-sensitive potassium sulfonylurea nucleotide binding protein human embryonic protein of channels couple the metabolic status of the cell to its membrane potential to regulate a number of including secretion (neurons and neuroendocrine cells) and muscle (skeletal, cardiac, and vascular smooth J. H. J. KATP channel is a that in a including a regulatory sulfonylurea (SUR) and a J. J. J. J. J. to the protein nucleotide binding folds (NBF1 and C-terminal NBF2) the SUR1 in and neuroendocrine cells islet beta SUR2A in cardiac and in vascular smooth muscle J. J. J. H. J. H. Y. Y. Y. J. Biol. Chem. to the of and of and J. H. J. not the regulatory of the of protein the KATP channel J. H. J. (Syn-1A), a protein known to mediate binds to and channels to regulate secretion Y. H. J. Biol. Chem. J. We recently reported that Syn-1A NBF1 and NBF2 of SUR1 and inhibit pancreatic islet beta cell KATP channels its NBF1 Y. J. Biol. Chem. Syn-1A was reported to present in cardiac myocytes E. Y. J. J. prompted us to whether Syn-1A a cardiac we that present in the plasma membrane of rat cardiac the cardiac KATP channel its NBF1 and NBF2 of and and and was and the Y. J. Biol. Chem. protein and of the protein Syn-1A protein was of of protein was a which was the of the and cells at in in and cells and to cells and in to cells of the of the binding the cells and of and cardiac membrane was to the and rat we the reported J. Biol. in and and and was at at was binding and the cells and in binding and cells and at at binding the of cells, rat and rat Syn-1A of protein in binding was a of of of protein in of binding at in to at binding to membrane and was human protein which is to rat SUR2A and only to of and in and to the of was and in a a was a and a potassium potassium of the was the heart, in of and of was a and at cardiac myocytes and membrane myocytes in at to and at and at the at in a in and a KATP and channel human embryonic kidney 293 cells was in the and we Y. J. Biol. Chem. a and and of SUR2A to the a was membrane potential was at and a of was to the the to at to the the in the of the at KATP to in the that the of membrane to a at the of the was at a potential of and and and at and at in to of in to a was of Syn-1A SUR2A NBF1 SUR2A and was a of the at in the of the and of Syn-1A in rat cardiac is a that Syn-1A and present in rat cell of the the cardiac was to a plasma membrane of the Syn-1A we the of Syn-1A to the plasma membrane of cardiac a the myocytes not is in the plasma membrane of cardiac of Syn-1A and in rat of cardiac of and cardiac membrane of Syn-1A in cardiac to the plasma membrane of a the was not SUR2A at and whether the in rat cardiac muscle and capable of binding the only in in the J. J. Y. Y. Y. J. Biol. Chem. of rat the protein binding in and that Syn-1A rat the of to to rat membrane and cardiac membrane the we a SUR2A and the the rat Y. Y. Y. J. Biol. Chem. in the of SUR2A and H. J. Y. J. Biol. Chem. and not the we only a in and SUR2A is the protein in cardiac J. H. J. Y. Y. Y. J. Biol. Chem. in We the cardiac SUR2A protein in Here, to is to SUR2A the cell This that Syn-1A binding to SUR2A is and not via protein in the We that Syn-1A not and C-terminal domains Y. J. Biol. Chem. pancreatic islet beta cells that Syn-1A binds to NBF1 and NBF2 domains of SUR1 Y. J. Biol. Chem. We whether Syn-1A to the NBF1 and C-terminal NBF2 of and of to to Syn-1A cell and Syn-1A a not and we the of and NBF2 binding to Syn-1A at We that NBF1 and NBF2 Syn-1A of and KATP in NBF1 and NBF2 of show the of the Syn-1A and cardiac and we whether Syn-1A inhibit KATP in rat cardiac myocytes and whether inhibition is via We that the of a cardiac membrane KATP channels to the in the in was of the of KATP channels. to of KATP we to channel to a inhibition of KATP KATP in the of is of Syn-1A to of and not We that Syn-1A pancreatic beta cell KATP binding to the not of SUR1 Y. J. Biol. Chem. We whether SUR2A NBF1 NBF2 mediate Syn-1A inhibition of cardiac KATP in to pancreatic beta cells, of SUR2A NBF1 and NBF2 Syn-1A to and of and and This that not only NBF1 NBF2 of SUR2A Syn-1A inhibition of cardiac KATP SUR2A NBF1 SUR2A NBF2 which and of inhibition of cardiac KATP is mediated SUR2A NBF1 and of membrane cardiac myocytes to that the of membrane to in to to in a of channel the of the channels. of channel and a the at is of Syn-1A SUR2A NBF1 SUR2A NBF2 of in the of the a of the the of of Syn-1A and to and channels J. Y. J. Y. J. Biol. Chem. J. H. Y. H. J. cardiac myocytes not only Syn-1A and H. Y. Gaisano, is that cardiac KATP modulate Syn-1A inhibition of cardiac KATP we and SUR2A in cells to examine the inhibition of cardiac KATP channels cells a the KATP and in a of to in and is the potential of the cells a only at the of the Syn-1A the cell inhibition at and and the of Syn-1A Syn-1A inhibition whether SUR2A NBF1 and NBF2 the we cells. of a KATP that Syn-1A the cardiac KATP channel binding to of inhibition of KATP cells expressing is mediated SUR2A NBF1 and of Syn-1A and SUR2A KATP cells expressing KATP to at to the the in the of the and cell membrane to membrane potential to the Syn-1A is of cells. that not KATP we that Syn-1A the SUR1 to the KATP channel in cells and rat islet beta cells Y. J. Biol. Chem. Here, we show that Syn-1A cardiac SUR2A protein to the KATP that Syn-1A the cardiac KATP channel of This that Syn-1A the cardiac KATP channel a regulatory of KATP channel which in and and which the of and that the of Syn-1A inhibition of islet beta cell channels Y. J. Biol. Chem. including J. J. and the to KATP a of to channel activity and cardiac of Syn-1A the cardiac KATP channels the plasma membrane SUR2A protein Syn-1A was to the SUR2A protein in cells, which in inhibition of KATP SUR2A is the protein in the plasma membrane J. H. J. Y. Y. Y. J. Biol. Chem. E. Y. J. J. we Syn-1A to We that the not Syn-1A Syn-1A inhibition of KATP Y. J. Biol. Chem. Y. J. Biol. Chem. we that only NBF1 the of Syn-1A pancreatic beta cell KATP NBF2 NBF2 binds to Syn-1A in the present we cardiac and that NBF1 and NBF2 of SUR2A in Syn-1A inhibition of the plasma membrane cardiac KATP channels. NBF2 is the at the NBF1 and C-terminal H. J. the C-terminal of the SUR1 is and to of SUR1 SUR2A and J. J. Biol. Chem. the Y. Y. that the Syn-1A binding of NBF2 of SUR2A and SUR1 is at the of and the Syn-1A binding channel the C-terminal in to the of Syn-1A in KATP the the which nucleotide binding to which nucleotide binding KATP channel J. that NBF1 and NBF2 in the cells J. that Syn-1A binds and of SUR2A and SUR1 Y. J. Biol. Chem. that of Syn-1A might to and modulate its that NBF2 is the SUR1 and SUR2A J. H. J. NBF1 a in of the channel NBF2 in SUR1 the channel to the of in the channel is and to Syn-1A to in nucleotide is known to regulate and membrane channels in in the of in cells. Here, we show that Syn-1A in membrane of a muscle the cardiac its the KATP we that modulate channels in smooth J. H. and domains SUR2A and J. H. J. Y. J. Biol. Chem. Syn-1A to the and of which regulate vascular smooth muscle KATP channels. the in the Syn-1A to which in the vascular in the Y. Y. Y. J. Biol. Chem. to to examine the of Syn-1A vascular KATP channel Syn-1A binding to SUR1 Y. J. Biol. Chem. and the of Syn-1A of KATP channels. that in the channel in and KATP channels in the and of the heart, pancreatic islet beta vascular smooth and J. insulin-secreting beta cells, we recently that Syn-1A and plasma membrane domains and channel KATP channel in domains E. J. Biol. Chem. Syn-1A of the which a channel and that membrane of channels and is the and of and cardiac membrane and which in and channel a in the Y. E. H. J. and decrease and to of KATP the potential to and This to and of the of Syn-1A inhibit cardiac KATP channels and activity via potential inhibition a to the of KATP channel activity of metabolic to ATP-sensitive potassium (KATP) KATP ATP-sensitive potassium sulfonylurea nucleotide binding protein human embryonic protein of KATP ATP-sensitive potassium sulfonylurea nucleotide binding protein human embryonic protein of channels couple the metabolic status of the cell to its membrane potential to regulate a number of including secretion (neurons and neuroendocrine cells) and muscle (skeletal, cardiac, and vascular smooth J. H. J. KATP channel is a that in a including a regulatory sulfonylurea (SUR) and a J. J. J. J. J. to the protein nucleotide binding folds (NBF1 and C-terminal NBF2) the SUR1 in and neuroendocrine cells islet beta SUR2A in cardiac and in vascular smooth muscle J. J. J. H. J. H. Y. Y. Y. J. Biol. Chem. to the of and of and J. H. J. not the regulatory of the of protein the KATP channel J. H. J. (Syn-1A), a protein known to mediate binds to and channels to regulate secretion Y. H. J. Biol. Chem. J. We recently reported that Syn-1A NBF1 and NBF2 of SUR1 and inhibit pancreatic islet beta cell KATP channels its NBF1 Y. J. Biol. Chem. Syn-1A was reported to present in cardiac myocytes E. Y. J. J. prompted us to whether Syn-1A a cardiac we that present in the plasma membrane of rat cardiac the cardiac KATP channel its NBF1 and NBF2 of and and and was and the Y. J. Biol. Chem. protein and of the protein Syn-1A protein was of of protein was a which was the of the and cells at in in and cells and to cells and in to cells of the of the binding the cells and of and cardiac membrane was to the and rat we the reported J. Biol. in and and and was at at was binding and the cells and in binding and cells and at at binding the of cells, rat and rat Syn-1A of protein in binding was a of of of protein in of binding at in to at binding to membrane and was human protein which is to rat SUR2A and only to of and in and to the of was and in a a was a and a potassium potassium of the was the heart, in of and of was a and at cardiac myocytes and membrane myocytes in at to and at and at the at in a in and a KATP and channel human embryonic kidney 293 cells was in the and we Y. J. Biol. Chem. a and and of SUR2A to the a was membrane potential was at and a of was to the the to at to the the in the of the at KATP to in the that the of membrane to a at the of the was at a potential of and and and at and at in to of in to a was of Syn-1A SUR2A NBF1 SUR2A and was a of the at and and and was and the Y. J. Biol. Chem. protein and of the protein Syn-1A protein was of of protein was a which was the of the and cells at in in and cells and to cells and in to cells of the of the binding the cells and of and cardiac membrane was to the and rat we the reported J. Biol. in and and and was at at was binding and the cells and in binding and cells and at at binding the of cells, rat and rat Syn-1A of protein in binding was a of of of protein in of binding at in to at binding to membrane and was human protein which is to rat SUR2A and only to of and in and to the of was and in a a was a and a potassium potassium of the was the heart, in of and of was a and at cardiac myocytes and membrane myocytes in at to and at and at the at in a in and a KATP and channel human embryonic kidney 293 cells was in the and we Y. J. Biol. Chem. a and and of SUR2A to the a was membrane potential was at and a of was to the the to at to the the in the of the at KATP to in the that the of membrane to a at the of the was at a potential of and and and at and at in to of in to a was of Syn-1A SUR2A NBF1 SUR2A and was a of the at in the of the and of Syn-1A in rat cardiac is a that Syn-1A and present in rat cell of the the cardiac was to a plasma membrane of the Syn-1A we the of Syn-1A to the plasma membrane of cardiac a the myocytes not SUR2A at and whether the in rat cardiac muscle and capable of binding the only in in the J. J. Y. Y. Y. J. Biol. Chem. of rat the protein binding in and that Syn-1A rat the of to to rat membrane and cardiac membrane the we a SUR2A and the the rat Y. Y. Y. J. Biol. Chem. in the of SUR2A and H. J. Y. J. Biol. Chem. and not the we only a in and SUR2A is the protein in cardiac J. H. J. Y. Y. Y. J. Biol. Chem. in We the cardiac SUR2A protein in Here, to is to SUR2A the cell This that Syn-1A binding to SUR2A is and not via protein in the We that Syn-1A not and C-terminal domains Y. J. Biol. Chem. pancreatic islet beta cells that Syn-1A binds to NBF1 and NBF2 domains of SUR1 Y. J. Biol. Chem. We whether Syn-1A to the NBF1 and C-terminal NBF2 of and of to to Syn-1A cell and Syn-1A a not and we the of and NBF2 binding to Syn-1A at We that NBF1 and NBF2 Syn-1A of and KATP in NBF1 and NBF2 of show the of the Syn-1A and cardiac and we whether Syn-1A inhibit KATP in rat cardiac myocytes and whether inhibition is via We that the of a cardiac membrane KATP channels to the in the in was of the of KATP channels. to of KATP we to channel to a inhibition of KATP KATP in the of is of Syn-1A to of and not We that Syn-1A pancreatic beta cell KATP binding to the not of SUR1 Y. J. Biol. Chem. We whether SUR2A NBF1 NBF2 mediate Syn-1A inhibition of cardiac KATP in to pancreatic beta cells, of SUR2A NBF1 and NBF2 Syn-1A to and of and and This that not only NBF1 NBF2 of SUR2A Syn-1A inhibition of cardiac KATP SUR2A NBF1 SUR2A NBF2 which and of inhibition of cardiac KATP is mediated SUR2A NBF1 and of membrane cardiac myocytes to that the of membrane to in to to in a of channel the of the channels. of channel and a the at is of Syn-1A SUR2A NBF1 SUR2A NBF2 of in the of the a of the the of of Syn-1A and to and channels J. Y. J. Y. J. Biol. Chem. J. H. Y. H. J. cardiac myocytes not only Syn-1A and H. Y. Gaisano, is that cardiac KATP modulate Syn-1A inhibition of cardiac KATP we and SUR2A in cells to examine the inhibition of cardiac KATP channels cells a the KATP and in a of to in and is the potential of the cells a only at the of the Syn-1A the cell inhibition at and and the of Syn-1A Syn-1A inhibition whether SUR2A NBF1 and NBF2 the we cells. of a KATP that Syn-1A the cardiac KATP channel binding to of inhibition of KATP cells expressing is mediated SUR2A NBF1 and of Syn-1A and SUR2A KATP cells expressing KATP to at to the the in the of the and cell membrane to membrane potential to the Syn-1A is of cells. that not KATP in the of the and of Syn-1A in rat cardiac is a that Syn-1A and present in rat cell of the the cardiac was to a plasma membrane of the Syn-1A we the of Syn-1A to the plasma membrane of cardiac a the myocytes not SUR2A at and whether the in rat cardiac muscle and capable of binding the only in in the J. J. Y. Y. Y. J. Biol. Chem. of rat the protein binding in and that Syn-1A rat the of to to rat membrane and cardiac membrane the we a SUR2A and the the rat Y. Y. Y. J. Biol. Chem. in the of SUR2A and H. J. Y. J. Biol. Chem. and not the we only a in and SUR2A is the protein in cardiac J. H. J. Y. Y. Y. J. Biol. Chem. in We the cardiac SUR2A protein in Here, to is to SUR2A the cell This that Syn-1A binding to SUR2A is and not via protein in the We that Syn-1A not and C-terminal domains Y. J. Biol. Chem. pancreatic islet beta cells that Syn-1A binds to NBF1 and NBF2 domains of SUR1 Y. J. Biol. Chem. We whether Syn-1A to the NBF1 and C-terminal NBF2 of and of to to Syn-1A cell and Syn-1A a not and we the of and NBF2 binding to Syn-1A at We that NBF1 and NBF2 Syn-1A of and KATP in NBF1 and NBF2 of show the of the Syn-1A and cardiac and we whether Syn-1A inhibit KATP in rat cardiac myocytes and whether inhibition is via We that the of a cardiac membrane KATP channels to the in the in was of the of KATP channels. to of KATP we to channel to a inhibition of KATP KATP in the of is of Syn-1A to of and not We that Syn-1A pancreatic beta cell KATP binding to the not of SUR1 Y. J. Biol. Chem. We whether SUR2A NBF1 NBF2 mediate Syn-1A inhibition of cardiac KATP in to pancreatic beta cells, of SUR2A NBF1 and NBF2 Syn-1A to and of and and This that not only NBF1 NBF2 of SUR2A Syn-1A inhibition of cardiac KATP SUR2A NBF1 SUR2A NBF2 which and of Syn-1A and to and channels J. Y. J. Y. J. Biol. Chem. J. H. Y. H. J. cardiac myocytes not only Syn-1A and H. Y. Gaisano, is that cardiac KATP modulate Syn-1A inhibition of cardiac KATP we and SUR2A in cells to examine the inhibition of cardiac KATP channels cells a the KATP and in a of to in and is the potential of the cells a only at the of the Syn-1A the cell inhibition at and and the of Syn-1A Syn-1A inhibition whether SUR2A NBF1 and NBF2 the we cells. of a KATP that Syn-1A the cardiac KATP channel binding to of we that Syn-1A the SUR1 to the KATP channel in cells and rat islet beta cells Y. J. Biol. Chem. Here, we show that Syn-1A cardiac SUR2A protein to the KATP that Syn-1A the cardiac KATP channel of This that Syn-1A the cardiac KATP channel a regulatory of KATP channel which in and and which the of and that the of Syn-1A inhibition of islet beta cell channels Y. J. Biol. Chem. including J. J. and the to KATP a of to channel activity and cardiac of Syn-1A the cardiac KATP channels the plasma membrane SUR2A protein Syn-1A was to the SUR2A protein in cells, which in inhibition of KATP SUR2A is the protein in the plasma membrane J. H. J. Y. Y. Y. J. Biol. Chem. E. Y. J. J. we Syn-1A to We that the not Syn-1A Syn-1A inhibition of KATP Y. J. Biol. Chem. Y. J. Biol. Chem. we that only NBF1 the of Syn-1A pancreatic beta cell KATP NBF2 NBF2 binds to Syn-1A in the present we cardiac and that NBF1 and NBF2 of SUR2A in Syn-1A inhibition of the plasma membrane cardiac KATP channels. NBF2 is the at the NBF1 and C-terminal H. J. the C-terminal of the SUR1 is and to of SUR1 SUR2A and J. J. Biol. Chem. the Y. Y. that the Syn-1A binding of NBF2 of SUR2A and SUR1 is at the of and the Syn-1A binding channel the C-terminal in to the of Syn-1A in KATP the the which nucleotide binding to which nucleotide binding KATP channel J. that NBF1 and NBF2 in the cells J. that Syn-1A binds and of SUR2A and SUR1 Y. J. Biol. Chem. that of Syn-1A might to and modulate its that NBF2 is the SUR1 and SUR2A J. H. J. NBF1 a in of the channel NBF2 in SUR1 the channel to the of in the channel is and to Syn-1A to in nucleotide is known to regulate and membrane channels in in the of in cells. Here, we show that Syn-1A in membrane of a muscle the cardiac its the KATP we that modulate channels in smooth J. H. and domains SUR2A and J. H. J. Y. J. Biol. Chem. Syn-1A to the and of which regulate vascular smooth muscle KATP channels. the in the Syn-1A to which in the vascular in the Y. Y. Y. J. Biol. Chem. to to examine the of Syn-1A vascular KATP channel Syn-1A binding to SUR1 Y. J. Biol. Chem. and the of Syn-1A of KATP channels. that in the channel in and KATP channels in the and of the heart, pancreatic islet beta vascular smooth and J. insulin-secreting beta cells, we recently that Syn-1A and plasma membrane domains and channel KATP channel in domains E. J. Biol. Chem. Syn-1A of the which a channel and that membrane of channels and is the and of and cardiac membrane and which in and channel a in the Y. E. H. J. and decrease and to of KATP the potential to and This to and of the of Syn-1A inhibit cardiac KATP channels and activity via potential inhibition a to the of KATP channel activity of metabolic to we that Syn-1A the SUR1 to the KATP channel in cells and rat islet beta cells Y. J. Biol. Chem. Here, we show that Syn-1A cardiac SUR2A protein to the KATP that Syn-1A the cardiac KATP channel of This that Syn-1A the cardiac KATP channel a regulatory of KATP channel which in and and which the of and that the of Syn-1A inhibition of islet beta cell channels Y. J. Biol. Chem. including J. J. and the to KATP a of to channel activity and cardiac of Syn-1A the cardiac KATP channels the plasma membrane SUR2A protein Syn-1A was to the SUR2A protein in cells, which in inhibition of KATP SUR2A is the protein in the plasma membrane J. H. J. Y. Y. Y. J. Biol. Chem. E. Y. J. J. we Syn-1A to We that the not Syn-1A Syn-1A inhibition of KATP Y. J. Biol. Chem. Y. J. Biol. Chem. we that only NBF1 the of Syn-1A pancreatic beta cell KATP NBF2 NBF2 binds to Syn-1A in the present we cardiac and that NBF1 and NBF2 of SUR2A in Syn-1A inhibition of the plasma membrane cardiac KATP channels. NBF2 is the at the NBF1 and C-terminal H. J. the C-terminal of the SUR1 is and to of SUR1 SUR2A and J. J. Biol. Chem. the Y. Y. that the Syn-1A binding of NBF2 of SUR2A and SUR1 is at the of and the Syn-1A binding channel the C-terminal in to the of Syn-1A in KATP the the which nucleotide binding to which nucleotide binding KATP channel J. that NBF1 and NBF2 in the cells J. that Syn-1A binds and of SUR2A and SUR1 Y. J. Biol. Chem. that of Syn-1A might to and modulate its that NBF2 is the SUR1 and SUR2A J. H. J. NBF1 a in of the channel NBF2 in SUR1 the channel to the of in the channel is and to Syn-1A to in nucleotide Syn-1A is known to regulate and membrane channels in in the of in cells. Here, we show that Syn-1A in membrane of a muscle the cardiac its the KATP we that modulate channels in smooth J. H. and domains SUR2A and J. H. J. Y. J. Biol. Chem. Syn-1A to the and of which regulate vascular smooth muscle KATP channels. the in the Syn-1A to which in the vascular in the Y. Y. Y. J. Biol. Chem. to to examine the of Syn-1A vascular KATP channel Syn-1A binding to SUR1 Y. J. Biol. Chem. and the of Syn-1A of KATP channels. that in the channel in and cells. Syn-1A KATP channels in the and of the heart, pancreatic islet beta vascular smooth and J. insulin-secreting beta cells, we recently that Syn-1A and plasma membrane domains and channel KATP channel in domains E. J. Biol. Chem. Syn-1A of the which a channel and that membrane of channels and is the and of and cardiac membrane and which in and KATP channel a in the Y. E. H. J. and decrease and to of KATP the potential to and This to and of the of Syn-1A inhibit cardiac KATP channels and activity via potential inhibition a to the of KATP channel activity of metabolic to We of the

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