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- W1975533268 abstract "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." @default.
- W1975533268 created "2016-06-24" @default.
- W1975533268 creator A5020475421 @default.
- W1975533268 creator A5068099600 @default.
- W1975533268 date "2008-02-15" @default.
- W1975533268 modified "2023-09-25" @default.
- W1975533268 title "LUMA interacts with emerin and influences its distribution at the inner nuclear membrane" @default.
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- W1975533268 doi "https://doi.org/10.1242/jcs.019281" @default.
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