A complex of Shc and Ran-GTPase localises to the cell nucleus |
| |
| Authors: | R. George H.-L. Chan Z. Ahmed K. M. Suen C. N. Stevens J. A. Levitt K. Suhling J. Timms J. E. Ladbury |
| |
| Affiliation: | (1) Department of Biochemistry and Molecular Biology, University College London, Gower Street, London, WC1E 6BT, UK;(2) Cancer Proteomics Laboratory, EGA Institute for Women’s Health, University College London, Cruciform Building 1.1, Gower Street, London, WC1E 6BT, UK;(3) Department of Physics, Kings College London, Strand, London, WC2 2LS, UK |
| |
| Abstract: | The three isoforms of the adaptor protein Shc play diverse roles in cell signalling. For example, the observation of p46 Shc in the nuclei of hepatocellular carcinoma cells suggests a function quite distinct from the better characterised cytoplasmic role. Ligands responsible for the transport of various Shc isoforms into organelles such as the nucleus have yet to be reported. To identify such ligands a far western approach was used to determine the p52 Shc interactome. The Ran-GTPase nuclear transport protein was identified and found to bind to p52 Shc in vitro with low micromolar affinity. Co-immunoprecipitation, pull down and fluorescence lifetime imaging microscopy experiments in stable cells confirmed cellular interaction and nuclear localisation. The nuclear transport factor protein NTF2, which functions in cohort with Ran, was shown to form a complex with both RAN and Shc, suggesting a mechanism for Shc entry into the nucleus as part of a tertiary complex. Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. Received 20 October 2008; received after revision 04 December 2008; accepted 15 December 2008 |
| |
| Keywords: | KeywordHeading" >. Nuclear localisation protein complex FLIM nuclear transport proteomics |
| 本文献已被 SpringerLink 等数据库收录！ |
|
