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First published online 29 January 2008
doi: 10.1242/jcs.019281

Journal of Cell Science 121, 536-548 (2008)
Published by The Company of Biologists 2008
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Research Article

LUMA interacts with emerin and influences its distribution at the inner nuclear membrane

Luiza Bengtsson* and Henning Otto{ddagger}

Freie Universität Berlin, Institut für Chemie und Biochemie, Thielallee 63, 14195 Berlin, Germany

{ddagger} Author for correspondence (e-mail: h.otto{at}biochemie.fu-berlin.de)

Accepted 19 November 2007

We present here a first characterization of LUMA, an unique integral inner nuclear membrane (INM) protein. LUMA is a highly conserved protein even in some bacteria and shares a PFAM domain of unknown function with orthologs from many species. Assessing LUMA topology by using protease protection of membrane-inserted LUMA and antibody epitope accessibility assays reveals that LUMA contains four transmembrane domains and a large hydrophilic domain located between membrane spans 1 and 2. The large hydrophilic domain is exposed to the perinuclear space whereas both LUMA termini reside cyto- or nucleoplasmically. Nuclear envelope targeting of LUMA mainly depends on the membrane spans. LUMA's transmembrane domains also promote homooligomerization. LUMA binds A- and B-type lamins and depends on A-type lamins for its INM localization. Furthermore, it interacts with emerin. Both downregulation of LUMA and overexpression of dominant-negative acting LUMA fragments causes redistribution of emerin. We propose that LUMA functions as a tetraspanin-like membrane organizer and has the potential to contribute to the pathomechanism of dystrophic diseases, such as Emery-Dreifuss muscular dystrophy.

Key words: Emerin, Emery-Dreifuss muscular dystrophy, Lamins, LUMA, Nuclear envelope


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