Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex
| dc.contributor.author | Fujita, Yasuyuki | |
| dc.contributor.author | Krause, Gerd | |
| dc.contributor.author | Scheffner, Martin | |
| dc.contributor.author | Zechner, Dietmar | |
| dc.contributor.author | Leddy, Hugo E Molina | |
| dc.contributor.author | Behrens, Jürgen | |
| dc.contributor.author | Sommer, Thomas | |
| dc.contributor.author | Birchmeier, Walter | |
| dc.date.accessioned | 2018-05-29T14:06:17Z | |
| dc.date.available | 2018-05-29T14:06:17Z | |
| dc.date.issued | 2002-03 | eng |
| dc.description.abstract | In epithelial cells, tyrosine kinases induce the tyrosine phosphorylation and ubiquitination of the E-cadherin complex, which induces endocytosis of E-cadherin. With a modified yeast 2-hybrid system, we isolated Hakai, an E-cadherin binding protein, which we have identified as an E3 ubiquitin-ligase. Hakai contains SH2, RING, zinc-finger and proline-rich domains, and interacts with E-cadherin in a tyrosine phosphorylation-dependent manner, inducing ubiquitination of the E-cadherin complex. Expression of Hakai in epithelial cells disrupts cell--cell contacts and enhances endocytosis of E-cadherin and cell motility. Through dynamic recycling of E-cadherin, Hakai can thus modulate cell adhesion, and could participate in the regulation of epithelial--mesenchymal transitions in development or metastasis. | eng |
| dc.description.version | published | eng |
| dc.identifier.doi | 10.1038/ncb758 | eng |
| dc.identifier.pmid | 11836526 | eng |
| dc.identifier.uri | https://kops.uni-konstanz.de/handle/123456789/42453 | |
| dc.language.iso | eng | eng |
| dc.subject.ddc | 570 | eng |
| dc.title | Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex | eng |
| dc.type | JOURNAL_ARTICLE | eng |
| dspace.entity.type | Publication | |
| kops.citation.bibtex | @article{Fujita2002-03Hakai-42453,
year={2002},
doi={10.1038/ncb758},
title={Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex},
number={3},
volume={4},
issn={1465-7392},
journal={Nature cell biology},
pages={222--231},
author={Fujita, Yasuyuki and Krause, Gerd and Scheffner, Martin and Zechner, Dietmar and Leddy, Hugo E Molina and Behrens, Jürgen and Sommer, Thomas and Birchmeier, Walter}
} | |
| kops.citation.iso690 | FUJITA, Yasuyuki, Gerd KRAUSE, Martin SCHEFFNER, Dietmar ZECHNER, Hugo E Molina LEDDY, Jürgen BEHRENS, Thomas SOMMER, Walter BIRCHMEIER, 2002. Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. In: Nature cell biology. 2002, 4(3), pp. 222-231. ISSN 1465-7392. eISSN 1476-4679. Available under: doi: 10.1038/ncb758 | deu |
| kops.citation.iso690 | FUJITA, Yasuyuki, Gerd KRAUSE, Martin SCHEFFNER, Dietmar ZECHNER, Hugo E Molina LEDDY, Jürgen BEHRENS, Thomas SOMMER, Walter BIRCHMEIER, 2002. Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. In: Nature cell biology. 2002, 4(3), pp. 222-231. ISSN 1465-7392. eISSN 1476-4679. Available under: doi: 10.1038/ncb758 | eng |
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<dcterms:abstract xml:lang="eng">In epithelial cells, tyrosine kinases induce the tyrosine phosphorylation and ubiquitination of the E-cadherin complex, which induces endocytosis of E-cadherin. With a modified yeast 2-hybrid system, we isolated Hakai, an E-cadherin binding protein, which we have identified as an E3 ubiquitin-ligase. Hakai contains SH2, RING, zinc-finger and proline-rich domains, and interacts with E-cadherin in a tyrosine phosphorylation-dependent manner, inducing ubiquitination of the E-cadherin complex. Expression of Hakai in epithelial cells disrupts cell--cell contacts and enhances endocytosis of E-cadherin and cell motility. Through dynamic recycling of E-cadherin, Hakai can thus modulate cell adhesion, and could participate in the regulation of epithelial--mesenchymal transitions in development or metastasis.</dcterms:abstract>
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| kops.sourcefield | Nature cell biology. 2002, <b>4</b>(3), pp. 222-231. ISSN 1465-7392. eISSN 1476-4679. Available under: doi: 10.1038/ncb758 | deu |
| kops.sourcefield.plain | Nature cell biology. 2002, 4(3), pp. 222-231. ISSN 1465-7392. eISSN 1476-4679. Available under: doi: 10.1038/ncb758 | deu |
| kops.sourcefield.plain | Nature cell biology. 2002, 4(3), pp. 222-231. ISSN 1465-7392. eISSN 1476-4679. Available under: doi: 10.1038/ncb758 | eng |
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