The nesprins [also known as SYNEs (synaptic nuclear envelope proteins)] are a family of type II transmembrane proteins implicated in the tethering of membrane-bound organelles and in the genetic aetiology of cerebellar ataxia and Emery–Dreifuss muscular dystrophy. They are characterized by a common structure of an SR (spectrin repeat) rod domain and a C-terminal transmembrane KLS (klarsicht)/KASH [klarsicht/ANC-1 (anchorage 1)/SYNE homology] domain which interacts with SUN [Sad1p/UNC (uncoordinated)-84] proteins in the nuclear envelope; most nesprins also have N-terminal actin-binding CH (calponin homology) domains. The genes encoding the three vertebrate nesprins (five in bony fish) and the small transmembrane actin-binding protein calmin are related to each other by ancient duplications and rearrangements. In the present paper, we collate sequence data for nesprins and calmins across the vertebrate clade and use these to study evolutionary constraints acting on their genes. We show that the rod domains of the larger nesprins are composed almost entirely of unbroken SR-like structures (74 in nesprin-1 and 56 in nesprin-2) and that these range from poorly conserved purely structural elements to highly conserved regions with a presumed protein–protein interaction function. The analysis suggests several interesting regions for future study. We also assess the evolutionary and EST (expressed sequence tag) expression support for nesprin isoforms, both known and novel; our findings suggest that substantial reassessment is required.
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Conference Article|
November 19 2008
Patterns of evolutionary conservation in the nesprin genes highlight probable functionally important protein domains and isoforms
Jennifer G. Simpson;
Jennifer G. Simpson
1Department of Medical and Molecular Genetics, King's College London, 8th Floor, Tower Wing, Guy's Hospital, London SE1 9RT, U.K.
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Roland G. Roberts
Roland G. Roberts
1
1Department of Medical and Molecular Genetics, King's College London, 8th Floor, Tower Wing, Guy's Hospital, London SE1 9RT, U.K.
1To whom correspondence should be addressed (email roli.roberts@genetics.kcl.ac.uk).
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Publisher: Portland Press Ltd
Received:
July 28 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (6): 1359–1367.
Article history
Received:
July 28 2008
Citation
Jennifer G. Simpson, Roland G. Roberts; Patterns of evolutionary conservation in the nesprin genes highlight probable functionally important protein domains and isoforms. Biochem Soc Trans 1 December 2008; 36 (6): 1359–1367. doi: https://doi.org/10.1042/BST0361359
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