Lamin B Receptor

Authors

Ada L. Olins, University of New EnglandFollow
Gale Rhodes
David B. Mark Welch
Monika Zwerger
Donald E. Olins, University of New EnglandFollow

Document Type

Article

Publication Date

1-1-2010

Abstract

Lamin B Receptor (LBR) is an integral membrane protein of the interphase nuclear envelope (NE). The N-terminal end resides in the nucleoplasm, binding to lamin B and heterochromatin, with the interactions disrupted during mitosis. The C-terminal end resides within the inner nuclear membrane, retreating with the ER away from condensing chromosomes during mitotic NE breakdown. Some of these properties are interpretable in terms of our current structural knowledge of LBR, but many of the structural features remain unknown. LBR apparently has an evolutionary history which brought together at least two ancient conserved structural domains (i.e. Tudor and sterol reductase). This convergence may have occurred with the emergence of the chordates and echinoderms. It is not clear what survival values have maintained LBR structure during evolution. But it seems likely that roles in post-mitotic nuclear reformation, interphase NE growth and compartmentalization of nuclear architecture might have provided some evolutionary advantage to preservation of the LBR gene.

Comments

Article originally published by Taylor & Francis Group in Nucleus on 01/01/10, available online: http://www.tandfonline.com/10.4161/nucl.1.1.10515

Copyright © 2010 Landes Bioscience

This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.

Recommended Citation

Olins, Ada L.; Rhodes, Gale; Mark Welch, David B.; Zwerger, Monika; and Olins, Donald E., "Lamin B Receptor" (2010). Pharmaceutical Sciences Faculty Publications. 21.
https://dune.une.edu/pharmsci_facpubs/21