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The physical and functional interaction of NDRG2 with MSP58 in cells
Jing Zhang1, Junye Liu, Xia Li
1The Department of Biochemistry and Molecular Biology and The State Key Laboratory of Cancer Biology, The Fourth Military Medical University, Xi'an, China 710032, China.
Abstract:
NDRG2, a member of N-Myc downstream regulated gene family, exerts the important functions in cell differentiation and tumor suppression. Although the ectopic expressed Ndrg2 inhibits the proliferation of tumor cells, its intracellular signal transduction pathway is hardly known. Here, we identified MSP58, a 58-kDa microspherule protein, as an interacting partner of human Ndrg2 by using yeast two-hybrid screening. The interaction was confirmed by glutathione S-transferase pull-down assay in vitro and by co-immune-precipitation assay in vivo. The forkhead associated domain of MSP58 is essential for its interaction with Ndrg2. Ndrg2 could co-localize with MSP58 in nuclear of HeLa cell during cell stress. Furthermore, the modulation of Ndrg2 level influences the cell cycle process together with MSP58. In conclusion, the findings offered a novel insight into the physiological roles of Ndrg2.
Insights
This study identifies microspherule protein 58 (MSP58) as a binding partner of N-Myc downstream regulated gene 2 (NDRG2). Their interaction influences cell cycle progression, offering new insights into NDRG2
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- N-Myc downstream regulated gene 2 (NDRG2) plays roles in cell differentiation and tumor suppression.
- The intracellular signaling pathways of NDRG2 are not well understood.
- Understanding NDRG2 interactions is crucial for its role in cellular processes.
Purpose of the Study:
- To identify interacting partners of human NDRG2.
- To elucidate the functional significance of NDRG2 interactions.
- To investigate the role of NDRG2 in cellular signaling pathways.
Main Methods:
- Yeast two-hybrid screening to identify interacting proteins.
- Glutathione S-transferase pull-down assays for in vitro interaction confirmation.
- Co-immunoprecipitation assays for in vivo interaction validation.
- Cellular co-localization studies in HeLa cells under stress conditions.
Main Results:
- Microspherule protein 58 (MSP58) was identified as a binding partner of NDRG2.
- The forkhead-associated domain of MSP58 is critical for NDRG2 interaction.
- NDRG2 and MSP58 co-localize in the nucleus of HeLa cells during stress.
- Modulating NDRG2 levels affects the cell cycle in conjunction with MSP58.
Conclusions:
- MSP58 is a novel interacting partner of NDRG2.
- The NDRG2-MSP58 interaction is functionally relevant to cell cycle regulation.
- This study provides new insights into the physiological roles and signaling mechanisms of NDRG2.
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