EphA8-ephrinA5 Signaling and Clathrin-Mediated Endocytosis Is Regulated by Tiam-1, a Rac-Specific Guanine Nucleotide Exchange Factor
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Yoo, Sooyeon | - |
dc.contributor.author | Shin, Jongdae | - |
dc.contributor.author | Park, Soochul | - |
dc.date.available | 2021-02-22T13:47:52Z | - |
dc.date.issued | 2010-06 | - |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.issn | 0219-1032 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/13200 | - |
dc.description.abstract | Recent studies indicate that endocytosis of Eph-ephrin complexes may be one of the mechanisms by which a high affinity cell-cell adhesion is converted to a repulsive interaction. In this study, we show that EphA8 undergoes clathrin-mediated endocytosis upon treatment with ephrin-A5, and that EphA8 is associated tightly with Tiam-1, a Rac-specific guanine nucleotide exchange factor. Analysis of EphA8 deletion mutants revealed that a juxtamembrane region in EphA8 is critically involved in endocytosis of EphA8-ephrinA5 complexes. An EphA8 mutant lacking this juxtamembrane portion was defective for endocytosis with ephrinA5, and also displayed a weak association with Tiam-1. Expression of an endocytosis-defective version of EphA8 resulted in a low level of Rac activity in response to ephrin-A5 stimulation. More importantly, down-regulation of Tiam-1 resulted in inefficient endocytosis of EphA8-ephrinA5 complexes. These results suggest that Tiam-1 plays a role in clathrin-dependent endocytosis of EphA8-ephrinA5 complexes. | - |
dc.format.extent | 7 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | KOREAN SOC MOLECULAR & CELLULAR BIOLOGY | - |
dc.title | EphA8-ephrinA5 Signaling and Clathrin-Mediated Endocytosis Is Regulated by Tiam-1, a Rac-Specific Guanine Nucleotide Exchange Factor | - |
dc.type | Article | - |
dc.publisher.location | 대한민국 | - |
dc.identifier.doi | 10.1007/s10059-010-0075-2 | - |
dc.identifier.scopusid | 2-s2.0-77955052289 | - |
dc.identifier.wosid | 000279875300010 | - |
dc.identifier.bibliographicCitation | MOLECULES AND CELLS, v.29, no.6, pp 603 - 609 | - |
dc.citation.title | MOLECULES AND CELLS | - |
dc.citation.volume | 29 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 603 | - |
dc.citation.endPage | 609 | - |
dc.type.docType | Article | - |
dc.identifier.kciid | ART001453155 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | EPH RECEPTORS | - |
dc.subject.keywordPlus | NEURAL DEVELOPMENT | - |
dc.subject.keywordPlus | TYROSINE PHOSPHORYLATION | - |
dc.subject.keywordPlus | EPHRINS | - |
dc.subject.keywordPlus | REPULSION | - |
dc.subject.keywordPlus | ADHESION | - |
dc.subject.keywordPlus | CLEAVAGE | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | LIGANDS | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordAuthor | endocytosis | - |
dc.subject.keywordAuthor | EphA8 | - |
dc.subject.keywordAuthor | ephrin-A5 | - |
dc.identifier.url | https://link.springer.com/article/10.1007%2Fs10059-010-0075-2 | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
Sookmyung Women's University. Cheongpa-ro 47-gil 100 (Cheongpa-dong 2ga), Yongsan-gu, Seoul, 04310, Korea02-710-9127
Copyright©Sookmyung Women's University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.