Loss of supervillin causes myopathy with myofibrillar disorganization and autophagic vacuoles.

ABSTRACT: The muscle specific isoform of the supervillin protein (SV2), encoded by the SVIL gene, is a large sarcolemmal myosin II- and F-actin-binding protein. Supervillin (SV2) binds and co-localizes with costameric dystrophin and binds nebulin, potentially attaching the sarcolemma to myofibrillar Z-lines. Despite its important role in muscle cell physiology suggested by various in vitro studies, there are so far no reports of any human disease caused by SVIL mutations. We here report four patients from two unrelated, consanguineous families with a childhood/adolescence onset of a myopathy associated with homozygous loss-of-function mutations in SVIL. Wide neck, anteverted shoulders and prominent trapezius muscles together with variable contractures were characteristic features. All patients showe

SUBMITTER: Hedberg-Oldfors C 

PROVIDER: S-EPMC7447519 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature