Recessive MYPN mutations cause cap myopathy with occasional nemaline rods.
- Resource Type
- journal article
- Authors
- Lornage, Xavière; Malfatti, Edoardo; Chéraud, Chrystel; Schneider, Raphaël; Biancalana, Valérie; Cuisset, Jean‐Marie; Garibaldi, Matteo; Eymard, Bruno; Fardeau, Michel; Boland, Anne; Deleuze, Jean‐François; Thompson, Julie; Carlier, Robert‐Yves; Böhm, Johann; Romero, Norma B.; Laporte, Jocelyn
- Source
- Annals of Neurology. Mar2017, Vol. 81 Issue 3, p467-473. 7p.
- Subject
- Language
- ISSN
- 0364-5134
Congenital myopathies are phenotypically and genetically heterogeneous. We describe homozygous truncating mutations in MYPN in 2 unrelated families with a slowly progressive congenital cap myopathy. MYPN encodes the Z-line protein myopalladin implicated in sarcomere integrity. Functional experiments demonstrate that the mutations lead to mRNA defects and to a strong reduction in full-length protein expression. Myopalladin signals accumulate in the caps together with alpha-actinin. Dominant MYPN mutations were previously reported in cardiomyopathies. Our data uncover that mutations in MYPN cause either a cardiac or a congenital skeletal muscle disorder through different modes of inheritance. Ann Neurol 2017;81:467-473. [ABSTRACT FROM AUTHOR]