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First published online January 21, 2009

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A new link for adipogenesis

The nuclear envelope (NE) functions to separate the cytoplasm from the nucleoplasm, and mutations in NE proteins, such as the integral membrane protein emerin, have been implicated in a number of degenerative diseases. Emerin is anchored at the inner nuclear membrane through its interaction with the intermediate-filament-type proteins lamins A/C. Previous work from Ewa Markiewicz and colleagues showed that emerin binds to and regulates the nuclear accumulation of the Wnt-signalling effector β-catenin in a lamin-A-dependent manner. Wnt/β-catenin signalling is known to be associated with adipogenic differentiation of cells, and here, Markiewicz and colleagues (p. 401) examine how the loss of emerin expression affects β-catenin signalling during adipogenesis. Previous reports have shown that there is a balance in the signalling between β-catenin and the nuclear-receptor protein PPAR in adipogenesis, and the authors now show that this balance is intimately linked to the dynamic remodelling of emerin and lamins A/C. Moreover, in the absence of this remodelling, activated β-catenin enhances adipogenesis and accelerates the loss of the cellular phenotype. The authors propose that this new mechanism might help to explain why mutations in NE proteins contribute to some tissue-degeneration phenotypes that are seen in laminopathies.

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Dynamic complexes of A-type lamins and emerin influence adipogenic capacity of the cell via nucleocytoplasmic distribution of β-catenin

Katarzyna Tilgner, Kamila Wojciechowicz, Colin Jahoda, Christopher Hutchison, and Ewa Markiewicz
JCS 2009 122: 401-413. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?