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Proceedings Paper

In vivo mobility of proteins involved in nuclear transport studied by fluorescence correlation spectroscopy
Author(s): Cecile Fradin; Michael Elbaum
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Paper Abstract

Using fluorescence correlation spectroscopy we measured the apparent mobility of a nuclear transport cargo (a streptavidin labeled with a nuclear localization signal) both in the cytoplasm and the nucleus of living cells, and we compared it to the mobility of a streptavidin labeled with mutations of the nuclear localization signal known not to support nuclear import, and with the mobility of a set of inert molecules (dextrans) of different sizes. In the cytoplasm, the mobility of the transport cargo is found to be significantly reduced compared to its mobility in the nucleus, or to the mobility of the streptavidins labeled with a mutant nuclear localization signal. This can be partly explained by the fact that the transport cargo forms a complex with two nuclear import mediator proteins (importin α and importin β) in the cytoplasm, but could also be partly due to specific interactions of this cargo with the cell cytoskeleton.

Paper Details

Date Published: 10 July 2003
PDF: 11 pages
Proc. SPIE 4963, Multiphoton Microscopy in the Biomedical Sciences III, (10 July 2003); doi: 10.1117/12.478003
Show Author Affiliations
Cecile Fradin, Weizmann Institute of Science (Israel)
McMaster Univ. (Canada)
Michael Elbaum, Weizmann Institute of Science (Israel)

Published in SPIE Proceedings Vol. 4963:
Multiphoton Microscopy in the Biomedical Sciences III
Ammasi Periasamy; Peter T. C. So, Editor(s)

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