{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Weninger G"],"funding":["NIDDK NIH HHS","NHLBI NIH HHS","NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["e2400497121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11228480"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(27)"],"pubmed_abstract":["S100A1, a small homodimeric EF-hand Ca<sup>2+</sup>-binding protein (~21 kDa), plays an important regulatory role in Ca<sup>2+</sup> signaling pathways involved in various biological functions including Ca<sup>2+</sup> cycling and contractile performance in skeletal and cardiac myocytes. One key target of the S100A1 interactome is the ryanodine receptor (RyR), a huge homotetrameric Ca<sup>2+</sup> release channel (~2.3 MDa) of the sarcoplasmic reticulum. Here, we report cryoelectron microscopy structures of S100A1 bound to RyR1, the skeletal muscle isoform, in absence and presence of Ca<sup>2+</sup>. Ca<sup>2+</sup>-free apo-S100A1 binds beneath the bridging solenoid (BSol) and forms contacts with the junctional solenoid and the shell-core linker of RyR1. Upon Ca<sup>2+</sup>-binding, S100"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Structural insights into the regulation of RyR1 by S100A1."],"pmcid":["PMC11228480"],"funding_grant_id":["R01 GM129325","P01 HL164319","R01 NS114570","RF1 NS114570","R01 DK118240","R25 NS076445","R01 HL145473","R01 HL140934","R01 HL142903","T32 HL120826","R25 HL156002"],"pubmed_authors":["Weninger G","Reiken S","Yuan Q","Wronska A","Dridi H","Brandenburg S","Liu Y","Marks AR","Riedemann GC","Chang A","Miotto MC","Lehnart SE","Tchagou C"],"additional_accession":[]},"is_claimable":false,"name":"Structural insights into the regulation of RyR1 by S100A1.","description":"S100A1, a small homodimeric EF-hand Ca<sup>2+</sup>-binding protein (~21 kDa), plays an important regulatory role in Ca<sup>2+</sup> signaling pathways involved in various biological functions including Ca<sup>2+</sup> cycling and contractile performance in skeletal and cardiac myocytes. One key target of the S100A1 interactome is the ryanodine receptor (RyR), a huge homotetrameric Ca<sup>2+</sup> release channel (~2.3 MDa) of the sarcoplasmic reticulum. Here, we report cryoelectron microscopy structures of S100A1 bound to RyR1, the skeletal muscle isoform, in absence and presence of Ca<sup>2+</sup>. Ca<sup>2+</sup>-free apo-S100A1 binds beneath the bridging solenoid (BSol) and forms contacts with the junctional solenoid and the shell-core linker of RyR1. Upon Ca<sup>2+</sup>-binding, S100","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T13:36:00.158Z","creation":"2025-04-04T11:24:08.808Z"},"accession":"S-EPMC11228480","cross_references":{"pubmed":["38917010"],"doi":["10.1073/pnas.2400497121"]}}