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Methods. 1999 Nov;19(3):362-72.

Dynamics and mobility of nuclear envelope proteins in interphase and mitotic cells revealed by green fluorescent protein chimeras.

Author information

1
Gene Expression and Cell Biology/Biophysics Programmes, EMBL, Menehofstrasse 1, Heidelberg, D-69117, Germany. Jan.Ellenberg@EMBL-Heidelberg.de

Abstract

Understanding how membrane proteins are targeted to and retained within the nuclear envelope (NE) and the fate of these proteins during NE disassembly/reassembly in mitosis is central for insight into the function of the NE in nuclear organization and dynamics. To address these issues we have attached green fluorescent protein (GFP) to a well-characterized protein of the inner nuclear membrane, lamin B receptor, believed to be one of the major chromatin docking protein in the NE. We have used this construct in a variety of applications, including dual-color GFP time-lapse imaging, to investigate the mechanisms underlying protein targeting to the NE and NE breakdown and reassembly during mitosis. In this review, we present a summary of the results from such studies and discuss the photobleaching and imaging methodology on which they were derived.

PMID:
10579931
DOI:
10.1006/meth.1999.0872
[Indexed for MEDLINE]

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