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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,6,9]]},"abstract":"<jats:p>\n                    Myotrem is an untreatable, early-onset, congenital myopathy characterized by hypotonia, muscle weakness, skeletal deformities, dysmorphia, respiratory insufficiency, and myogenic tremor (V. Shashi\n                    <jats:italic toggle=\"yes\">et al., Hum Mutat<\/jats:italic>\n                    , 2019 and J. Stavusis\n                    <jats:italic toggle=\"yes\">et al.,<\/jats:italic>\n                    <jats:italic toggle=\"yes\">Ann. Neurol.<\/jats:italic>\n                    , 2019). It is associated with dominant variants in the pivotal M-domain of slow-skeletal Myosin Binding Protein-C (sMyBP-C) that modulates the dynamic binding to myosin and actin filaments and thereby crossbridge formation and kinetics. Herein, we report a nonmissense Myotrem variant, c.795_803dup p.(Leu266_Arg268dup), referred to as LKR-duplication. Our comprehensive studies, integrating clinical findings with biophysical, structural, and computational approaches, uncover the previously unreported structure and properties of the slow-skeletal M-domain, while elucidating the impact of the LKR-duplication. We show that the LKR-duplication stabilizes local helicity but alters global domain dynamics, leading to increased myosin binding, while impairing myosin-ATPase activity and crossbridge cycling. Critically, we pinpoint the specific amino acid residues facilitating the M-domain\/myosin interaction and demonstrate that the LKR-duplicated residues not only directly contribute to myosin binding but also enhance the myosin interacting capability of neighboring and distant residues. Our multimodal approach sheds light on aspects of the pathobiology of the slow-skeletal M-domain\u2014the Myotrem hotspot\u2014by unveiling underlying pathogenic etiologies thereby paving the way for the development of targeted treatments.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2529897123","type":"journal-article","created":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T19:33:41Z","timestamp":1780342421000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":1,"title":["From bedside to bench: A multimodal approach uncovering the molecular basis of the\n                    <i>MYBPC1<\/i>\n                    -linked Myotrem myopathy"],"prefix":"10.1073","volume":"123","author":[{"given":"Aishwarya S.","family":"Iyer","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Maryland School of 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France"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fran\u00e7ois","family":"Constant Boyer","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01jbb3w63","id-type":"ROR","asserted-by":"publisher"}],"name":"Neuromuscular diseases Reference Center, Department of Physical and Rehabilitation Medicine, Reims University Hospital, Sebastopol Hospital, Centre Hospitalier Universitaire de Reims, UR3797, VieFra, Reims Champagne-Ardenne University","place":["Reims, France"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charlotte","family":"Pineau","sequence":"additional","affiliation":[{"name":"Pediatric Electrophysiology Department, Reims University Hospital","place":["Reims, France"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lindsey","family":"Hensley","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/028pmsz77","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Chemistry and 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