{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T14:03:07Z","timestamp":1789740187958,"version":"4.0.1"},"reference-count":72,"publisher":"Rockefeller University Press","issue":"6","license":[{"start":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T00:00:00Z","timestamp":1789689600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/rupress.org\/pages\/terms102024"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R15GM155848"],"award-info":[{"award-number":["R15GM155848"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,11,2]]},"abstract":"<jats:p>Neuroendocrine ATP-sensitive K+ channels (KATP) comprise four pore-forming subunits (Kir6.2), each associated with a modulatory sulfonylurea receptor subunit (SUR1). ATP\/ADP binding to Kir6.2 inhibits KATP; MgATP\/MgADP binding to two different sites on SUR1 promotes activation. As SUR1 is a member of the ABC transporter family of proteins, it can potentially hydrolyze MgATP to MgADP. Whether this activity is required for KATP activation remains controversial. Previous studies demonstrated that non-hydrolyzable ATP analogs do not activate KATP, which may reflect an inability of these compounds to bind to SUR1, their inability to promote a conformational change in SUR1 that leads to channel activation, or a requirement for ATP hydrolysis during channel gating. To explore this further, we synthesized a fluorescent trinitrophenyl (TNP) derivative of the non-hydrolyzable ATP analog \u03b2,\u03b3-methyleneadenosine 5\u2032-triphosphate (AMP-PCP). Synthesis was verified by UV-visible absorbance, fluorescence spectroscopy, 1H NMR, and mass spectrometry. Purity was assessed by reversed-phase HPLC. Real-time nucleotide binding to intact KATP channels in cell membranes was measured using FRET between channels labeled with a fluorescent, noncanonical amino acid and TNP-nucleotide derivatives. This technique provides sufficient spatial resolution to discriminate between binding to each site on KATP. Using this approach, we first established that TNP-ATP can bind to nucleotide-binding site (NBS) 1 on SUR1 in fluorescently labeled Kir6.2\/SUR1 channels in unroofed membranes of HEK293T cells. We subsequently demonstrated that TNP-AMP-PCP binds to both NBSs on SUR1 in the absence of Mg2+. AMP-PCP was able to compete with TNP-ATP for binding to NBS2, suggesting that it, too, binds NBS2. We conclude that the failure of non-hydrolyzable ATP analogs to activate KATP does not stem from an inability of these nucleotides to bind to the channel.<\/jats:p>","DOI":"10.1085\/jgp.202513840","type":"journal-article","created":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T06:20:31Z","timestamp":1787293231000},"update-policy":"https:\/\/doi.org\/10.1085\/jgp.crossmarkpolicy","source":"Crossref","is-referenced-by-count":0,"title":["A fluorescent non-hydrolyzable probe for the nucleotide-binding sites of KATP"],"prefix":"10.1085","volume":"158","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-7264-2418","authenticated-orcid":true,"given":"Priscilla","family":"Rubio","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03j3dbz94","id-type":"ROR","asserted-by":"publisher"}],"name":"Neuroscience Program, Trinity College 1 , Hartford, CT,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-1110-7739","authenticated-orcid":true,"given":"Shayla Q.","family":"Whitaker","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03j3dbz94","id-type":"ROR","asserted-by":"publisher"}],"name":"Neuroscience Program, Trinity College 1 , Hartford, CT,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9379-4377","authenticated-orcid":true,"given":"Jonathan","family":"Ashby","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03j3dbz94","id-type":"ROR","asserted-by":"publisher"}],"name":"Trinity College 2 Department of Chemistry, , Hartford, CT,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9335-0936","authenticated-orcid":true,"given":"Michael C.","family":"Puljung","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03j3dbz94","id-type":"ROR","asserted-by":"publisher"}],"name":"Neuroscience Program, Trinity College 1 , Hartford, CT,","place":["USA"]},{"id":[{"id":"https:\/\/ror.org\/03j3dbz94","id-type":"ROR","asserted-by":"publisher"}],"name":"Trinity College 2 Department of Chemistry, , Hartford, CT,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2026,9,18]]},"reference":[{"key":"2026091809175626800_bib1","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1126\/science.7716547","article-title":"Cloning of the beta cell high-affinity sulfonylurea receptor: A regulator of insulin secretion","volume":"268","author":"Aguilar-Bryan","year":"1995","journal-title":"Science"},{"key":"2026091809175626800_bib2","doi-asserted-by":"publisher","first-page":"15419","DOI":"10.1074\/jbc.M111713200","article-title":"The first nucleotide binding domain of cystic fibrosis transmembrane conductance regulator is a site of stable nucleotide interaction, whereas the second is a site of rapid turnover","volume":"277","author":"Aleksandrov","year":"2002","journal-title":"J. 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