Selective loss of a LAP1 isoform causes a muscle-specific nuclear envelopathy.


Journal

Neurogenetics
ISSN: 1364-6753
Titre abrégé: Neurogenetics
Pays: United States
ID NLM: 9709714

Informations de publication

Date de publication:
03 2021
Historique:
received: 14 10 2020
accepted: 24 12 2020
pubmed: 7 1 2021
medline: 19 11 2021
entrez: 6 1 2021
Statut: ppublish

Résumé

The nuclear envelope (NE) separates the nucleus from the cytoplasm in all eukaryotic cells. A disruption of the NE structure compromises normal gene regulation and leads to severe human disorders collectively classified as nuclear envelopathies and affecting skeletal muscle, heart, brain, skin, and bones. The ubiquitous NE component LAP1B is encoded by TOR1AIP1, and the use of an alternative start codon gives rise to the shorter LAP1C isoform. TOR1AIP1 mutations have been identified in patients with diverging clinical presentations such as muscular dystrophy, progressive dystonia with cerebellar atrophy, and a severe multi-systemic disorder, but the correlation between the mutational effect and the clinical spectrum remains to be determined. Here, we describe a novel TOR1AIP1 patient manifesting childhood-onset muscle weakness and contractures, and we provide clinical, histological, ultrastructural, and genetic data. We demonstrate that the identified TOR1AIP1 frameshift mutation leads to the selective loss of the LAP1B isoform, while the expression of LAP1C was preserved. Through comparative review of all previously reported TOR1AIP1 cases, we delineate a genotype/phenotype correlation and conclude that LAP1B-specific mutations cause a progressive skeletal muscle phenotype, while mutations involving a loss of both LAP1B and LAP1C isoforms induce a syndromic disorder affecting skeletal muscle, brain, eyes, ear, skin, and bones.

Identifiants

pubmed: 33405017
doi: 10.1007/s10048-020-00632-3
pii: 10.1007/s10048-020-00632-3
doi:

Substances chimiques

Nuclear Proteins 0
Protein Isoforms 0
Class I Phosphatidylinositol 3-Kinases EC 2.7.1.137
PIK3CA protein, human EC 2.7.1.137

Types de publication

Case Reports Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

33-41

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Auteurs

Xavière Lornage (X)

Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Inserm U1258, CNRS UMR7104, Strasbourg University, Illkirch, France.

Martial Mallaret (M)

Centre de Compétences des Maladies neuro-musculaires, CHU Grenoble Alpes, Grenoble, France.

Roberto Silva-Rojas (R)

Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Inserm U1258, CNRS UMR7104, Strasbourg University, Illkirch, France.

Valérie Biancalana (V)

Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Inserm U1258, CNRS UMR7104, Strasbourg University, Illkirch, France.
Laboratoire de Diagnostic Génétique, Faculté de Médecine, CHRU, Strasbourg, France.

Diane Giovannini (D)

Département d'Anatomie et Cytologie Pathologiques, CHU Grenoble Alpes, Grenoble, France.

Klaus Dieterich (K)

Institute for Advanced Biosciences (IAB), Inserm U1209, CHU Grenoble Alpes, Université Grenoble Alpes, Grenoble, France.

Safaa Saker (S)

Banque d'ADN et de cellules du Généthon, Evry, France.

Jean-François Deleuze (JF)

National Genotyping Center, Genomics Institute, Office of Atomic Energy and Alternative Energies, Evry, France.

Bernard Wuyam (B)

Pôle Thorax et Vaisseaux, Clinique Physiologie, Sommeil et Exercice, Grenoble Alpes University Hospital, Grenoble, France.

Jocelyn Laporte (J)

Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Inserm U1258, CNRS UMR7104, Strasbourg University, Illkirch, France. jocelyn@igbmc.fr.

Johann Böhm (J)

Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Inserm U1258, CNRS UMR7104, Strasbourg University, Illkirch, France. johann@igbmc.fr.

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