Distinct domain utilization by Smad3 and Smad4 for nucleoporin interaction and nuclear import Journal Article
| Authors: | Xu, L.; Alarcón, C.; Col, S.; Massagué, J. |
| Article Title: | Distinct domain utilization by Smad3 and Smad4 for nucleoporin interaction and nuclear import |
| Abstract: | Smad proteins undergo rapid nuclear translocation upon stimulation by transforming growth factor-β (TGFβ) and in so doing transduce the signal into the nucleus. In this report we unraveled nuclear import mechanisms of Smad3 and Smad4 that are dependent on their interaction with FG-repeat-containing nucleoporins such as CAN/Nup214, without the involvement of importin molecules that are responsible for most of the known nuclear import events. A surface hydrophobic corridor within the MH2 domain of Smad3 is critical for association with CAN/Nup214 and nuclear import, whereas Smad4 interaction with CAN/Nup214, and nuclear import requires structural elements present only in the full-length Smad4. As exemplified by the different susceptibility to inhibition of import by cytoplasmic retention factor SARA (Smad anchor for receptor activation), such utilization of distinct domains for nuclear import of Smad3 and Smad4 suggests that nuclear transport of Smad3 and Smad4 is subject to control by different retention factors. |
| Keywords: | unclassified drug; human cell; dna-binding proteins; nonhuman; protein domain; proteins; animal cell; complex formation; enzyme inhibition; smad3 protein; transforming growth factor beta; protein protein interaction; cell line; protein binding; hela cell; animalia; serine endopeptidases; intracellular signaling peptides and proteins; carrier proteins; protein transport; cell strain cos1; active transport, cell nucleus; protein structure, tertiary; binding sites; trans-activators; repetitive sequences, nucleic acid; nuclear pore complex proteins; smad4 protein; hydrophobicity; nucleoporin; smad anchor for receptor activation; growth kinetics; cytoplasm protein; protein nup214; nuclear import; humans; human; priority journal; article; protein can |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 278 |
| Issue: | 43 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2003-10-24 |
| Start Page: | 42569 |
| End Page: | 42577 |
| Language: | English |
| DOI: | 10.1074/jbc.M307601200 |
| PUBMED: | 12917407 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 12 September 2014 -- Source: Scopus |
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