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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: Implications for epidermal growth factor signaling

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dc.contributor.author Han, Jung Min ko
dc.contributor.author Kim, Yong ko
dc.contributor.author Lee, Jun Sung ko
dc.contributor.author Lee, Chang Sup ko
dc.contributor.author Lee, Byoung Dae ko
dc.contributor.author Ohba, Motoi ko
dc.contributor.author Kuroki, Toshio ko
dc.contributor.author Suh, Pann-Ghill ko
dc.contributor.author Ryu, Sung Ho ko
dc.date.available 2015-09-01T08:02:25Z -
dc.date.created 2015-08-19 ko
dc.date.issued 2002-11 ko
dc.identifier.citation MOLECULAR BIOLOGY OF THE CELL, v.13, no.11, pp.3976 - 3988 ko
dc.identifier.issn 1059-1524 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/16472 -
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 ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher AMER SOC CELL BIOLOGY ko
dc.title Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: Implications for epidermal growth factor signaling ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0036854304 ko
dc.identifier.wosid 000179568500019 ko
dc.type.rims ART ko
dc.description.wostc 40 *
dc.description.scopustc 39 *
dc.date.tcdate 2015-12-28 *
dc.date.scptcdate 2015-11-04 *
dc.identifier.doi 10.1091/mbc.E02-02-0100 ko
dc.identifier.url http://www.molbiolcell.org/content/13/11/3976.long ko
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