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DC Field | Value | Language |
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dc.citation.endPage | 2370 | - |
dc.citation.number | 12 | - |
dc.citation.startPage | 2363 | - |
dc.citation.title | CELLULAR SIGNALLING | - |
dc.citation.volume | 27 | - |
dc.contributor.author | Lee, Chang Sup | - |
dc.contributor.author | Kim, Jong Min | - |
dc.contributor.author | Ghim, Jaewang | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Ryu, Sung Ho | - |
dc.date.accessioned | 2023-12-22T00:17:58Z | - |
dc.date.available | 2023-12-22T00:17:58Z | - |
dc.date.created | 2016-01-25 | - |
dc.date.issued | 2015-12 | - |
dc.description.abstract | Phospholipase D (PLD) is one of the key enzymes to mediate a variety of cellular phenomena including endocytosis, actin rearrangement, proliferation, differentiation, and migration. Dynamin as a PLD-interacting partner is a large GTP binding protein that has been considered a mechanochemical enzyme involved in endocytosis by hydrolyzing GTP. Although both PLD and dynamin have been implicated in the regulation of actin cytoskeleton, it is not known how they have a link to regulate fibronectin (FN)-induced cell spreading. Furthermore, it is unknown whether dynamin can work as a GTP-dependent regulator through its interaction with other proteins. Here, we demonstrate that PLD can be regulated by dynamin in a GTP-dependent manner and that this is critical for FN-mediated cell spreading. First, we verified that GTP-loaded dynamin can mediate the cell spreading by FN by using dynamin's GTP binding deficient mutant (K44A). Also, we confirmed that blocking the PLD activity inhibited FN-induced cell spreading, not cell adhesion. Moreover, PLD interacted with dynamin in a GTP-dependent manner in FN signaling, and this interaction was crucial for FN-induced PLD activation and cell spreading. Also, we found that PLD mutant (R128K) that didn't have GAP activity increased the GTP-dependent interaction between PLD and dynamin; it also increased PLD activity and cell spreading. These findings suggest that the observed increase in PLD activity was through boosting the binding of PLD with dynamin and it facilitated FN-induced cell spreading. These results imply that GTP-loaded dynamin, like a small GTPase could mediate a "switch on" signaling via interaction with PLD that has a role as an effector. (C) 2015 Elsevier Inc. All rights reserved | - |
dc.identifier.bibliographicCitation | CELLULAR SIGNALLING, v.27, no.12, pp.2363 - 2370 | - |
dc.identifier.doi | 10.1016/j.cellsig.2015.08.019 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.scopusid | 2-s2.0-84941313291 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/18203 | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S0898656815002508 | - |
dc.identifier.wosid | 000367486400005 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE INC | - |
dc.title | GTP-dependent interaction between phospholipase D and dynamin modulates fibronectin-induced cell spreading | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Phospholipase D | - |
dc.subject.keywordAuthor | GTPase | - |
dc.subject.keywordAuthor | GTPase activating protein | - |
dc.subject.keywordAuthor | Dynamin | - |
dc.subject.keywordAuthor | Spreading | - |
dc.subject.keywordAuthor | Interaction | - |
dc.subject.keywordPlus | ACTIVATING PROTEIN | - |
dc.subject.keywordPlus | PHOSPHATIDIC-ACID | - |
dc.subject.keywordPlus | ENDOCYTOSIS | - |
dc.subject.keywordPlus | KINASE | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | GAP | - |
dc.subject.keywordPlus | MEMBRANE | - |
dc.subject.keywordPlus | PARTNERS | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | CANCER | - |
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