| Literature DB >> 24368072 |
Nathalie Oulhen1, Thomas M Onorato1, Isabela Ramos1, Gary M Wessel2.
Abstract
Dysferlin is a calcium-binding transmembrane protein involved in membrane fusion and membrane repair. In humans, mutations in the dysferlin gene are associated with muscular dystrophy. In this study, we isolated plasma membrane-enriched fractions from full-grown immature oocytes of the sea star, and identified dysferlin by mass spectrometry analysis. The full-length dysferlin sequence is highly conserved between human and the sea star. We learned that in the sea star Patiria miniata, dysferlin RNA and protein are expressed from oogenesis to gastrulation. Interestingly, the protein is highly enriched in the plasma membrane of oocytes. Injection of a morpholino against dysferlin leads to a decrease of endocytosis in oocytes, and to a developmental arrest during gastrulation. These results suggest that dysferlin is critical for normal endocytosis during oogenesis and for embryogenesis in the sea star and that this animal may be a useful model for studying the relationship of dysferlin structure as it relates to its function.Entities:
Keywords: Dysferlin; Endocytosis; Gastrulation; Oocytes; Plasma membrane; Sea star
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Year: 2013 PMID: 24368072 PMCID: PMC3982204 DOI: 10.1016/j.ydbio.2013.12.018
Source DB: PubMed Journal: Dev Biol ISSN: 0012-1606 Impact factor: 3.582