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Reviews in Molecular Medicine: http://www.expertreviews.org/
DOI: 10.1017/S1462399405009294; 14 June 2005
Citation details: Derek T. Warren, Qiuping Zhang, Peter L. Weissberg and Catherine
M. Shanahan (2005) Nesprins: intracellular scaffolds that maintain cell architecture
and coordinate cell function?
Expert Rev. Mol. Med. Vol. 7, Issue 11, DOI: 10.1017/S1462399405009294
Nesprins:
intracellular scaffolds that maintain cell architecture and coordinate cell
function?
Derek T. Warren, Qiuping
Zhang, Peter L. Weissberg and Catherine M. Shanahan
Author
contact details
Nesprins
are a recently discovered family of ubiquitously expressed intracellular proteins.
Through alternative transcriptional initiation, termination and splicing, two
genes – nesprin-1 and nesprin-2 (also known as syne-1 and syne-2) –
give rise to many protein isoforms that vary markedly in size. The largest of
these isoforms comprise a C-terminal transmembrane domain (the KLS domain) linked
by a spectrin-repeat rod domain to an N-terminal paired, actin-binding, calponin-homology
domain. This structure suggests that they are well suited to orchestrate signalling
between cell membranes and the cytoskeleton. Other isoforms have variable lengths
of this rod domain linked to either end of the protein. Smaller isoforms with
the KLS domain are localised at the inner nuclear membrane, where they bind
lamin A/C and emerin. Larger nesprin isoforms link the outer nuclear membrane
with intracellular organelles and the actin cytoskeleton and are thought to
regulate nuclear anchorage and organelle migration. Thus, nesprins might have
a variety of fundamental roles in cells, particularly muscle cells where they
are highly expressed. We speculate that nesprin mutations might contribute to
a broad range of human disease syndromes, including laminopathies.
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Figure 1. Domain structure of some of the major isoforms generated from
the nesprin-1 and nesprin-2 genes.
Web, PDF
Figure 2. Subcellular
localisations of nesprin-1 revealed by immunofluorescence.
Web, PDF
Figure 3. Model
of potential nesprin functions.
Web, PDF
Table 1. Nesprin
isoform nomenclature.
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Table 2. Subcellular
localisations of nesprins.
Web, PDF
Table 3. Nesprin
binding partners.
Web, PDF
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