The 44-kDa Pim-1 Kinase Phosphorylates BCRP/ABCG2 and Thereby Promotes Its Multimerization and Drug-resistant Activity in Human Prostate Cancer Cells.

The 44-kDa Pim-1 Kinase Phosphorylates BCRP/ABCG2 and Thereby Promotes Its Multimerization and Drug-resistant Activity in Human Prostate Cancer Cells. Research Abstract Details 

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The 44-kDa Pim-1 Kinase Phosphorylates BCRP/ABCG2 and Thereby Promotes Its Multimerization and Drug-resistant Activity in Human Prostate Cancer Cells. Abstract Text:

Yingqiu Xie,Kexin Xu,Douglas E Linn,Xi Yang,Zhiyong Guo,Hermela Shimelis,Takeo Nakanishi,Douglas D Ross,Hegang Chen,Ladan Fazli,Martin E Gleave,Yun Qiu,Yingqiu Xie,Kexin Xu,Douglas E Linn,Xi Yang,Zhiyong Guo,Hermela Shimelis,Takeo Nakanishi,Douglas D Ross,Hegang Chen,Ladan Fazli,Martin E Gleave,Yun Qiu,

We previously showed that the 44-kDa serine/threonine kinase Pim-1 (Pim-1L) can protect prostate cancer cells from apoptosis induced by chemotherapeutic drugs (Xie, Y., Xu, K., Dai, B., Guo, Z., Jiang, T., Chen, H., and Qiu, Y. (2006) Oncogene 25, 70-78). To further explore the mechanisms of Pim-1L-mediated resistance to chemotherapeutic drugs in prostate cancer cells, we employed a yeast two-hybrid screening to identify cellular proteins that were associated with Pim-1L, and we found the ABC transporter BCRP/ABCG2 as one of the potential interacting partners of Pim-1L. We also showed that the expression level of Pim-1L and BCRP was up-regulated in mitoxantrone and docetaxel-resistant prostate cancer cell lines. Pim-1L was co-localized with BCRP on the plasma membrane and induced phosphorylation of BCRP at threonine 362. Knocking-down Pim-1L expression in the drug-resistant prostate cancer cells abolished multimer formation of endogenous BCRP and resensitized the resistant cells to chemotherapeutic drugs suggesting that BCRP phosphorylation induced by Pim-1L was essential for its functionality. This is further corroborated by our finding that the plasma membrane localization and drug-resistant activity of BCRP were compromised by T362A mutation. Our data suggest that Pim-1L may protect prostate cancer cells from apoptosis, at least in part, through regulation of transmembrane drug efflux pump. These findings may provide a potential therapeutic approach by disrupting Pim-1 signaling to reverse BCRP-mediated multidrug resistance.

The 44-kDa Pim-1 Kinase Phosphorylates BCRP/ABCG2 and Thereby Promotes Its Multimerization and Drug-resistant Activity in Human Prostate Cancer Cells. Publishing Authors By Initials

Y Xie,K Xu,DE Linn,X Yang,Z Guo,H Shimelis,T Nakanishi,DD Ross,H Chen,L Fazli,ME Gleave,Y Qiu,Y Xie,K Xu,DE Linn,X Yang,Z Guo,H Shimelis,T Nakanishi,DD Ross,H Chen,L Fazli,ME Gleave,Y Qiu,

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The 44-kDa Pim-1 Kinase Phosphorylates BCRP/ABCG2 and Thereby Promotes Its Multimerization and Drug-resistant Activity in Human Prostate Cancer Cells. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Journal of biological chemistry

VOLUME: 283

Page Numbers: 3349-56

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 5

MONTH: 12

YEAR: 2007

The 44-kDa Pim-1 Kinase Phosphorylates BCRP/ABCG2 and Thereby Promotes Its Multimerization and Drug-resistant Activity in Human Prostate Cancer Cells. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

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Grant and Affiliation Information for The 44-kDa Pim-1 Kinase Phosphorylates BCRP/ABCG2 and Thereby Promotes Its Multimerization and Drug-resistant Activity in Human Prostate Cancer Cells.

AFFILIATION: Departments of Pharmacology and Experimental Therapeutics, Medicine, Pathology, and Epidemiology & Preventive Medicine.

Country: United States

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MEDLINETA: J Biol Chem

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