Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells

Abstract Expression of cofilin is directly associated with metastatic activity in many tumors. Here, we studied the role of Latent Membrane Protein 2 A (LMP2A) of Epstein-Barr Virus (EBV) in the accumulation of cofilin observed in nasopharyngeal cancer (NPC) tumor cells. We used LMP2A transformed NP...

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Autores principales:	Murat R. Gainullin, Ilya Yu Zhukov, Xiaoying Zhou, Yingxi Mo, Lidiia Astakhova, Ingemar Ernberg, Liudmila Matskova
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/41a7fdc60fbc4b3b8fa6d0711f9d76f6
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spelling	oai:doaj.org-article:41a7fdc60fbc4b3b8fa6d0711f9d76f62021-12-02T12:30:36ZDegradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells10.1038/s41598-017-09540-32045-2322https://doaj.org/article/41a7fdc60fbc4b3b8fa6d0711f9d76f62017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-09540-3https://doaj.org/toc/2045-2322Abstract Expression of cofilin is directly associated with metastatic activity in many tumors. Here, we studied the role of Latent Membrane Protein 2 A (LMP2A) of Epstein-Barr Virus (EBV) in the accumulation of cofilin observed in nasopharyngeal cancer (NPC) tumor cells. We used LMP2A transformed NPC cell lines to analyze cofilin expression. We used mutation analysis, ectopic expression and down-regulation of Cbl, AIP4 and Syk in these cell lines to determine the effect of the LMP2A viral protein on cofilin degradation and its role in the assembly of a cofilin degrading protein complex. The LMP2A of EBV was found to interfer with cofilin degradation in NPC cells by accelerating the proteasomal degradation of Cbl and Syk. In line with this, we found significantly higher cofilin expression in NPC tumor samples as compared to the surrounding epithelial tissues. Cofilin, as an actin severing protein, influences cellular plasticity, and facilitates cellular movement in response to oncogenic stimuli. Thus, under relaxed cellular control, cofilin facilitates tumor cell movement and dissemination. Interference with its degradation may enhance the metastatic potential of NPC cells.Murat R. GainullinIlya Yu ZhukovXiaoying ZhouYingxi MoLidiia AstakhovaIngemar ErnbergLiudmila MatskovaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Murat R. Gainullin Ilya Yu Zhukov Xiaoying Zhou Yingxi Mo Lidiia Astakhova Ingemar Ernberg Liudmila Matskova Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells
description	Abstract Expression of cofilin is directly associated with metastatic activity in many tumors. Here, we studied the role of Latent Membrane Protein 2 A (LMP2A) of Epstein-Barr Virus (EBV) in the accumulation of cofilin observed in nasopharyngeal cancer (NPC) tumor cells. We used LMP2A transformed NPC cell lines to analyze cofilin expression. We used mutation analysis, ectopic expression and down-regulation of Cbl, AIP4 and Syk in these cell lines to determine the effect of the LMP2A viral protein on cofilin degradation and its role in the assembly of a cofilin degrading protein complex. The LMP2A of EBV was found to interfer with cofilin degradation in NPC cells by accelerating the proteasomal degradation of Cbl and Syk. In line with this, we found significantly higher cofilin expression in NPC tumor samples as compared to the surrounding epithelial tissues. Cofilin, as an actin severing protein, influences cellular plasticity, and facilitates cellular movement in response to oncogenic stimuli. Thus, under relaxed cellular control, cofilin facilitates tumor cell movement and dissemination. Interference with its degradation may enhance the metastatic potential of NPC cells.
format	article
author	Murat R. Gainullin Ilya Yu Zhukov Xiaoying Zhou Yingxi Mo Lidiia Astakhova Ingemar Ernberg Liudmila Matskova
author_facet	Murat R. Gainullin Ilya Yu Zhukov Xiaoying Zhou Yingxi Mo Lidiia Astakhova Ingemar Ernberg Liudmila Matskova
author_sort	Murat R. Gainullin
title	Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells
title_short	Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells
title_full	Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells
title_fullStr	Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells
title_full_unstemmed	Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells
title_sort	degradation of cofilin is regulated by cbl, aip4 and syk resulting in increased migration of lmp2a positive nasopharyngeal carcinoma cells
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/41a7fdc60fbc4b3b8fa6d0711f9d76f6
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Degradation of cofilin is regulated by Cbl, AIP4 and Syk resulting in increased migration of LMP2A positive nasopharyngeal carcinoma cells

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