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DC Field | Value | Language |
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dc.citation.endPage | 3988 | - |
dc.citation.number | 11 | - |
dc.citation.startPage | 3976 | - |
dc.citation.title | MOLECULAR BIOLOGY OF THE CELL | - |
dc.citation.volume | 13 | - |
dc.contributor.author | Han, Jung Min | - |
dc.contributor.author | Kim, Yong | - |
dc.contributor.author | Lee, Jun Sung | - |
dc.contributor.author | Lee, Chang Sup | - |
dc.contributor.author | Lee, Byoung Dae | - |
dc.contributor.author | Ohba, Motoi | - |
dc.contributor.author | Kuroki, Toshio | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Ryu, Sung Ho | - |
dc.date.accessioned | 2023-12-22T11:36:34Z | - |
dc.date.available | 2023-12-22T11:36:34Z | - |
dc.date.created | 2015-08-19 | - |
dc.date.issued | 2002-11 | - |
dc.description.abstract | Phospholipase D (PLD) has been suggested to mediate epidermal growth factor (EGF) signaling. However, the molecular mechanism of EGF-induced PLD activation has not yet been elucidated. We investigated the importance of the phosphorylation and compartmentalization of PLD1 in EGF signaling. EGF treatment of COS-7 cells transiently expressing PLD1 stimulated PLD1 activity and induced PLD1 phosphorylation. The EGF-induced phosphorylation of threonine147 was completely blocked and the activity of PLD1 attenuated by point mutations (S2A/T147A/S561A) of PLD1 phosphorylation sites. The expression of a dominant negative PKCalpha mutant by adenovirus-mediated gene transfer greatly inhibited the phosphorylation and activation of PLD1 induced by EGF in PLD1-transfected COS-7 cells. EGF-induced PLD1 phosphorylation occurred primarily in the caveoil-enriched membrane (CEM) fraction, and the kinetics of PLD1 phosphorylation. in the CEM were strongly correlated with PLD1 phosphorylation in the total membrane. Interestingly, EGF-induced PLD1 phosphorylation and activation and the coimmunoprecipitation of PLD1 with caveohn-1 and the EGF receptor in the CEM were significantly attenuated in the palmitoylation-deficient C240S/C241S mutant, which did not localize to the CEM. Immunocytochemical analysis revealed that wild-type PLD1 colocalized with caveohn-1 and the EGF receptor and that phosphorylated PLD1 was localized exclusively in the plasma membrane, although some PLD1 was also detected in vesicular structures. Transfection of wild-type PLD1 but not of C240S/C241S mutant increased EGF-induced raf-1 translocation to the CEM and ERK phosphorylation. This study shows, for the first time, that EGF-induced PLD1 phosphorylation and activation occur in the CEM and that the correct localization of PLD1 to the CEM via palmitoylation is critical for EGF signaling | - |
dc.identifier.bibliographicCitation | MOLECULAR BIOLOGY OF THE CELL, v.13, no.11, pp.3976 - 3988 | - |
dc.identifier.doi | 10.1091/mbc.E02-02-0100 | - |
dc.identifier.issn | 1059-1524 | - |
dc.identifier.scopusid | 2-s2.0-0036854304 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/16472 | - |
dc.identifier.url | http://www.molbiolcell.org/content/13/11/3976.long | - |
dc.identifier.wosid | 000179568500019 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC CELL BIOLOGY | - |
dc.title | Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: Implications for epidermal growth factor signaling | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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