{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kostan J"],"funding":["Germany Excellence Strategy","Austrian Science Fund FWF","Interreg","Deutsche Forschungsgemeinschaft","FP7 People: Marie-Curie Actions","Slovenian Research Agency","Vienna Science and Technology Fund","Austrian Federal Ministry of Economy, Family and Youth","Wellcome Trust"],"pagination":["e3001148"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8062120"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(4)"],"pubmed_abstract":["Sarcomeres, the basic contractile units of striated muscle cells, contain arrays of thin (actin) and thick (myosin) filaments that slide past each other during contraction. The Ig-like domain-containing protein myotilin provides structural integrity to Z-discs-the boundaries between adjacent sarcomeres. Myotilin binds to Z-disc components, including F-actin and α-actinin-2, but the molecular mechanism of binding and implications of these interactions on Z-disc integrity are still elusive. To illuminate them, we used a combination of small-angle X-ray scattering, cross-linking mass spectrometry, and biochemical and molecular biophysics approaches. We discovered that myotilin displays conformational ensembles in solution. We generated a structural model of the F-actin:myotilin complex that r"],"journal":["PLoS biology"],"pubmed_title":["Molecular basis of F-actin regulation and sarcomere assembly via myotilin."],"pmcid":["PMC8062120"],"funding_grant_id":["238423","201543","FOR 1352, FOR 2743","Collaborative Award (201543/Z/16)","I525, I1593, P22276, P19060 and W1221","35337, P1-0140","I 525","253275","Chemical Biology project LS17-008","201543/Z/16","390939984","I 1593","Austrian-Slovak Interreg Project B301"],"pubmed_authors":["Sajko S","van der Ven PFM","Kostan J","Djinovic-Carugo K","Pavsic M","Molt S","Drepper F","Svergun DI","Lenarcic B","Schwarz TC","Graewert MA","Puz V","Konrat R","Furst DO","Warscheid B","Onipe A","Schreiner C"],"additional_accession":[]},"is_claimable":false,"name":"Molecular basis of F-actin regulation and sarcomere assembly via myotilin.","description":"Sarcomeres, the basic contractile units of striated muscle cells, contain arrays of thin (actin) and thick (myosin) filaments that slide past each other during contraction. The Ig-like domain-containing protein myotilin provides structural integrity to Z-discs-the boundaries between adjacent sarcomeres. Myotilin binds to Z-disc components, including F-actin and α-actinin-2, but the molecular mechanism of binding and implications of these interactions on Z-disc integrity are still elusive. To illuminate them, we used a combination of small-angle X-ray scattering, cross-linking mass spectrometry, and biochemical and molecular biophysics approaches. We discovered that myotilin displays conformational ensembles in solution. We generated a structural model of the F-actin:myotilin complex that r","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-05-09T08:49:13.095Z","creation":"2022-02-10T09:23:27.356Z"},"accession":"S-EPMC8062120","cross_references":{"pubmed":["33844684"],"doi":["10.1371/journal.pbio.3001148"]}}