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PMID: 16314286 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Dissociation of nuclear import cargo complexes by the protein Ran: a fluorescence correlation spectroscopy study.

Comptes rendus biologies ·Vol. 328 ·No. 12 ·2005-12-00 ·Pages 1073-82

Fradin C, Zbaida D, Elbaum M

Abstract

In nucleated cells, proteins designed for nuclear import form complexes with soluble nuclear transport receptors prior to translocation across the nuclear envelope. The directionality of transport is due to the asymmetric distribution of the protein Ran, which dissociates import cargo complexes only in its nuclear RanGTP form. Using fluorescence correlation spectroscopy, we have studied the stability of cargo complexes in solution in the presence and in the absence of RanGTP. We find that RanGTP has a higher affinity for the major import receptor, the importin alpha/beta heterodimer, when importin alpha does not carry a cargo, suggesting that some nuclear transport targets might be preferentially released.

MeSH Terms
Amino Acid Sequence Cell Nucleus/metabolism Humans Karyopherins/metabolism Kinetics Models, Biological Models, Theoretical Peptide Fragments/chemistry,metabolism Protein Transport/physiology Spectrometry, Fluorescence/methods ran GTP-Binding Protein/metabolism
Chemicals
Karyopherins Peptide Fragments ran GTP-Binding Protein
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fradin Cécile
Department of Physics and Astronomy, 1280 Main St. W, Hamilton, ON, L8S4M1, Canada. fradin@physics.mcmaster.ca
Zbaida David
Elbaum Michael
Article Info
Journal
Comptes rendus biologies
Abbr.
C R Biol
ISSN
1631-0691
Published
2005-12-00
Epub
2005-00-02
Pages
1073-82
Language
English
Region
France
NLM ID
101140040
Subset
IM
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