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Cells 2017, 6(3), 28;

Lamin B Receptor: Interplay between Structure, Function and Localization

Laboratory of Biochemistry, Department of Chemistry, Aristotelian University, Thessaloniki 54124, Greece
Laboratory of Biochemistry, Faculty of Medicine, University of Thessaly, Panepistimiou 3 BIOPOLIS, Larissa 41500, Greece
Author to whom correspondence should be addressed.
Received: 24 July 2017 / Revised: 28 August 2017 / Accepted: 30 August 2017 / Published: 31 August 2017
(This article belongs to the Collection Lamins and Laminopathies)
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Lamin B receptor (LBR) is an integral protein of the inner nuclear membrane, containing a hydrophilic N-terminal end protruding into the nucleoplasm, eight hydrophobic segments that span the membrane and a short, nucleoplasmic C-terminal tail. Two seemingly unrelated functions have been attributed to LBR. Its N-terminal domain tethers heterochromatin to the nuclear periphery, thus contributing to the shape of interphase nuclear architecture, while its transmembrane domains exhibit sterol reductase activity. Mutations within the transmembrane segments result in defects in cholesterol synthesis and are associated with diseases such as the Pelger–Huët anomaly and Greenberg skeletal dysplasia, whereas no such harmful mutations related to the anchoring properties of LBR have been reported so far. Recent evidence suggests a dynamic regulation of LBR expression levels, structural organization, localization and function, in response to various signals. The molecular mechanisms underlying this dynamic behavior have not yet been fully unraveled. Here, we provide an overview of the current knowledge of the interplay between the structure, function and localization of LBR, and hint at the interconnection of the two distinct functions of LBR. View Full-Text
Keywords: lamin B receptor; LBR; RS domain; SRPK1; Akt; heterochromatin; nuclear envelope lamin B receptor; LBR; RS domain; SRPK1; Akt; heterochromatin; nuclear envelope

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Nikolakaki, E.; Mylonis, I.; Giannakouros, T. Lamin B Receptor: Interplay between Structure, Function and Localization. Cells 2017, 6, 28.

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