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• W2004339976 abstract "Nesprin-1 and nesprin-2 (also known as Syne-1 and Syne-2,) are large (∼3300-residue) vertebrate proteins associated with emerin and lamin A at the nuclear envelope of muscle cells and other cell types. We show that the previously described nesprins are short isoforms of giant proteins comprising an actin-binding amino-terminus connected to a carboxy-terminal klarsicht-related transmembrane domain by a massive (∼6000–8000 amino acid) spectrin-like rod domain, making full-length nesprin-1, at one megadalton, the largest non-titin protein hitherto described in humans. We find that MSP-300, a 7000-residue Drosophila melanogaster protein whose disruption results in defects of muscle development, corresponds to the N-terminal two-thirds of the Drosophila nesprin ortholog. A nesprin-like protein is also encoded by the nematode genome. Moreover, we demonstrate that the larger isoforms of nesprin-1, like MSP-300, are localized to the sarcomeric Z-line of both skeletal and cardiac muscle. The recognition that a characteristic muscle-specific mutant phenotype in the fly results from a disruption of its nesprin ortholog reinforces the candidacy of the human proteins for involvement in genetic diseases of skeletal and cardiac muscle." @default.
• W2004339976 created "2016-06-24" @default.
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• W2004339976 date "2002-11-01" @default.
• W2004339976 modified "2023-10-01" @default.
• W2004339976 title "The Nesprins Are Giant Actin-Binding Proteins, Orthologous to Drosophila melanogaster Muscle Protein MSP-300" @default.
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• W2004339976 doi "https://doi.org/10.1006/geno.2002.6859" @default.
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