YDJC Induces Epithelial-Mesenchymal Transition via Escaping from Interaction with CDC16 through Ubiquitination of PP2A

Eun Ji Kim, Mi Kyung Park, Gyeoung Jin Kang, Hyun Jung Byun, Hyun Ji Kim, Lu Yu, Boram Kim, Hee Sung Chae, Young Won Chin, Jae Gal Shim, Ho Lee, Chang Hoon Lee

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Abstract

Lung cancer is the number 1 cause of cancer-related casualties in the world. Appropriate diagnostic markers and novel targets for lung cancer are needed. Chitooligosaccharide deacetylase homolog (YDJC) catalyzes the deacetylation of acetylated carbohydrates; however, the role of YDJC in lung cancer progression has yet to be studied. A549 lung cancer orthotopic mouse model was used for mice experiments. We found that YDJC overexpression contributes to lung cancer progression in an orthotopic mouse model. Long-term treatment (48 h) induces YDJC expression in sphingosylphosphorylcholine (SPC)-induced epithelial-mesenchymal transition (EMT). Gene silencing of YDJC (siYDJC) reduced N-cadherin expression and increased E-cadherin expression in SPC-induced EMT. Overexpression of YDJC reverses them but overexpression of the deacetylase deficient mutant YDJCD13A could not. Interestingly, overexpression of CDC16, a YDJC binding partner, suppressed EMT. ERK2 is activated in siCDC16-induced EMT. YDJC overexpression reduces expression of protein phosphatase 2A (PP2A), whereas CDC16 overexpression induces PP2A expression. YDJC overexpression induced ubiquitination of PP2A but YDJCD13A could not. CDC16 overexpression increased the ubiquitination of YDJC. These results suggest that YDJC contributes to the progression of lung cancer via enhancing EMT by inducing the ubiquitination of PP2A. Therefore, YDJC might be a new target for antitumor therapy against lung cancer.

Original languageEnglish (US)
Article number3542537
JournalJournal of Oncology
Volume2019
DOIs
StatePublished - Jan 1 2019

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Protein Phosphatase 2
Epithelial-Mesenchymal Transition
Ubiquitination
Lung Neoplasms
Cadherins
Gene Silencing
Carbohydrates

PubMed: MeSH publication types

  • Journal Article

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YDJC Induces Epithelial-Mesenchymal Transition via Escaping from Interaction with CDC16 through Ubiquitination of PP2A. / Kim, Eun Ji; Park, Mi Kyung; Kang, Gyeoung Jin; Byun, Hyun Jung; Kim, Hyun Ji; Yu, Lu; Kim, Boram; Chae, Hee Sung; Chin, Young Won; Shim, Jae Gal; Lee, Ho; Lee, Chang Hoon.

In: Journal of Oncology, Vol. 2019, 3542537, 01.01.2019.

Research output: Contribution to journalArticle

Kim, EJ, Park, MK, Kang, GJ, Byun, HJ, Kim, HJ, Yu, L, Kim, B, Chae, HS, Chin, YW, Shim, JG, Lee, H & Lee, CH 2019, 'YDJC Induces Epithelial-Mesenchymal Transition via Escaping from Interaction with CDC16 through Ubiquitination of PP2A', Journal of Oncology, vol. 2019, 3542537. https://doi.org/10.1155/2019/3542537
Kim, Eun Ji ; Park, Mi Kyung ; Kang, Gyeoung Jin ; Byun, Hyun Jung ; Kim, Hyun Ji ; Yu, Lu ; Kim, Boram ; Chae, Hee Sung ; Chin, Young Won ; Shim, Jae Gal ; Lee, Ho ; Lee, Chang Hoon. / YDJC Induces Epithelial-Mesenchymal Transition via Escaping from Interaction with CDC16 through Ubiquitination of PP2A. In: Journal of Oncology. 2019 ; Vol. 2019.
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abstract = "Lung cancer is the number 1 cause of cancer-related casualties in the world. Appropriate diagnostic markers and novel targets for lung cancer are needed. Chitooligosaccharide deacetylase homolog (YDJC) catalyzes the deacetylation of acetylated carbohydrates; however, the role of YDJC in lung cancer progression has yet to be studied. A549 lung cancer orthotopic mouse model was used for mice experiments. We found that YDJC overexpression contributes to lung cancer progression in an orthotopic mouse model. Long-term treatment (48 h) induces YDJC expression in sphingosylphosphorylcholine (SPC)-induced epithelial-mesenchymal transition (EMT). Gene silencing of YDJC (siYDJC) reduced N-cadherin expression and increased E-cadherin expression in SPC-induced EMT. Overexpression of YDJC reverses them but overexpression of the deacetylase deficient mutant YDJCD13A could not. Interestingly, overexpression of CDC16, a YDJC binding partner, suppressed EMT. ERK2 is activated in siCDC16-induced EMT. YDJC overexpression reduces expression of protein phosphatase 2A (PP2A), whereas CDC16 overexpression induces PP2A expression. YDJC overexpression induced ubiquitination of PP2A but YDJCD13A could not. CDC16 overexpression increased the ubiquitination of YDJC. These results suggest that YDJC contributes to the progression of lung cancer via enhancing EMT by inducing the ubiquitination of PP2A. Therefore, YDJC might be a new target for antitumor therapy against lung cancer.",
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AU - Byun, Hyun Jung

AU - Kim, Hyun Ji

AU - Yu, Lu

AU - Kim, Boram

AU - Chae, Hee Sung

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AU - Shim, Jae Gal

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AU - Lee, Chang Hoon

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