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- Cambridge University Press
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- © Cambridge University Press 2005
- eISSN
- 1462-3994
- DOI
- 10.1017/S1462399405009294
- Publisher site
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Abstract
expert reviews http://www.expertreviews.org/ in molecular medicine a Nesprin-1 isoforms kDa *Nesprin-1α 2 112 CH domain SR-like rod domain Nesprin-1α 1 112 Klarsicht-like domain Nesprin-1β Nesprin-1β 380 Nesprin-1γ Nesprin-1 giant CPG2 110 ENAPTIN-165 165 b Nesprin-2 isoforms kDa Nesprin-2α 2 48 *Nesprin-2α 1 62 Nesprin-2β Nesprin-2β Nesprin-2γ Nesprin-2 giant Nesprin-2α2∆ TM Nesprin-2∆ TM1 80 Domain structure of some of the major isoforms generated from the nesprin-1 and nesprin-2 genes Expert Reviews in Molecular Medicine 2005 Cambridge University Press (part a only) Figure 1. Domain structure of some of the major isoforms generated from the nesprin-1 and nesprin-2 genes. Isoforms are generated by alternative initiation and termination of transcription; thus, isoforms represent portions of the giant proteins (Refs 12, 14, 15, 17, 18, 22, 23, 25). Many other isoforms (not shown) are generated by the insertion, in a tissue-specific pattern, of several alternative coding exons (Refs 12, 14). The addition of these protein domains does not interrupt the continuous nature of the central rod domain of the nesprin isoforms. The asterisks denote muscle-specific isoforms. Illustration in part b modified from Ref. 14, with permission from The Company of Biologists Ltd. Accession information: Vol. 7; Issue 11; 14 June 2005 ©2005 Cambridge University Press Domain structure of some of the major isoforms generated from the nesprin-1 and nesprin-2 genes
Journal
Expert Reviews in Molecular Medicine – Cambridge University Press
Published: Jun 13, 2005
Keywords: nesprins; nuclear envelope; actin; laminopathy; lamin; emerin; muscle; syne proteins; nuance; enaptin