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Töpf, Ana

https://orcid.org/0000-0002-9227-2526

Mayo Clinic

Newcastle University

Citations 1

The E3 ligase HECTD1 controls skeletal muscle sarcomere and mitochondrial integrity
Ruas, Jorge L. , Červenka, Igor , Leuchtmann, Aurel B. , Jannig, Paulo R. , Naddaf, Elie, Kokesh, Elieen, Murgia, Marta , Sereiva, Tadas , Li, Bo , Yang, Feikun , Jude, Baptiste , Rumyantseva, Anastasia , Azzolini, Michelle, Porsmyr‐Palmertz, Margareta, Yang, Wenli , Mann, Matthias, Töpf, Ana , Straub, Volker, Naddaf, Elie , Naddaf, Elie , Ducommun, Serge , Correia, Jorge C. , Mann, Matthias , Freyer, Christoph , Wredenberg, Anna , Lanner, Johanna T. , Hahn, A. , Straub, Volker

No container title available | March 8, 2026 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.21203/rs.3.rs-8663318/v1 Get It

Abstract Sarcomeres are the fundamental functional units of skeletal muscle, essential for both force generation and metabolic homeostasis. While sarcomere degradation has been extensively studied, the mechanisms that preserve its integrity remain poorly defined. Here, we identify HECTD1 as an E3 ubiquitin ligase required for sarcomere maintenance and mitochondrial integrity. We show that HECTD1 ubiquitylates and stabilizes the chaperones KLHL40/41, which protect thin-filament components from misfolding and degradation. Consequently, reducing Hectd1 expression in myotubes coordinately decreases the levels of multiple sarcomere proteins. Skeletal muscle–specific Hectd1 knockout mice ( Hectd1 mKO) show severe sarcomere and mitochondrial disorganization and dysfunction, progressive muscle weakness, exercise and glucose intolerance, and unresolved tissue remodeling. Importantly, human iPSC-derived myotubes carrying a patient-associated HECTD1 mutation, recapitulate key molecular features of the Hectd1 mKO. These findings establish HECTD1 as a central regulator linking sarcomere proteostasis to mitochondrial function and identify its dysfunction as a cause of myopathy with mitochondriopathy.