Journal
PLOS ONE
Volume 12, Issue 1, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0169626
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Funding
- THALIS Program
- European Union (ESF)
- Greek national funds (Education and Lifelong Learning-NSRF)
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The lamin B receptor (LBR) is a multi-spanning membrane protein of the inner nuclear membrane that is often employed as a reporter of nuclear envelope dynamics. We show here that the diffusional mobility of full-length LBR exhibits significant regional variation along the nuclear envelope, consistent with the existence of discrete LBR microdomains and the occurrence of multiple, asymmetrically-spaced anastomoses along the nuclear envelope-endoplasmic reticulum interface. Interestingly, a commonly used fusion protein that contains the amino-terminal region and the first transmembrane domain of LBR exhibits reduced mobility at the nuclear envelope, but behaves similarly to full-length LBR in the endoplasmic reticulum. On the other hand, carboxy-terminally truncated mutants that retain the first four transmembrane domains and a part or the whole of the amino-terminal region of LBR are generally hyper-mobile. These results suggest that LBR dynamics is structure and compartment specific. They also indicate that native LBR is probably configured by long-range interactions that involve the loops between adjacent transmembrane domains and parts of the amino-terminal region.
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