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Cancers 2016, 8(3), 37; doi:10.3390/cancers8030037

Proteomics Analysis Reveals Novel RASSF2 Interaction Partners

1
Department of Biochemistry and Molecular Genetics, University of Louisville, Louisville, KY 40202, USA
2
Department of Medicine, James Graham Brown Cancer Center, Molecular Targets Program, University of Louisville, Louisville, KY 40202, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Reinhard Dammann
Received: 14 January 2016 / Revised: 18 February 2016 / Accepted: 9 March 2016 / Published: 16 March 2016
(This article belongs to the Special Issue RASSF Signalling in Cancer)
View Full-Text   |   Download PDF [1865 KB, uploaded 16 March 2016]   |  

Abstract

RASSF2 is a tumor suppressor that shares homology with other Ras-association domain (RASSF) family members. It is a powerful pro-apoptotic K-Ras effector that is frequently inactivated in many human tumors. The exact mechanism by which RASSF2 functions is not clearly defined, but it likely acts as a scaffolding protein, modulating the activity of other pro-apoptotic effectors, thereby regulating and integrating tumor suppressor pathways. However, only a limited number of RASSF2 interacting partners have been identified to date. We used a proteomics based approach to identify additional RASSF2 interactions, and thereby gain a better insight into the mechanism of action of RASSF2. We identified several proteins, including C1QBP, Vimentin, Protein phosphatase 1G and Ribonuclease inhibitor that function in diverse biological processes, including protein post-translational modifications, epithelial-mesenchymal transition, cell migration and redox homeostasis, which have not previously been reported to interact with RASSF2. We independently validated two of these novel interactions, C1QBP and Vimentin and found that the interaction with C1QBP was enhanced by K-Ras whereas, interestingly, the Vimentin interaction was reduced by K-Ras. Additionally, RASSF2/K-Ras regulated the acetylation of Vimentin. Our data thus reveal novel mechanisms by which RASSF2 may exert its functions, several of which may be Ras-regulated. View Full-Text
Keywords: RASSF2; Vimentin; K-Ras; acetylation; SIRT1 RASSF2; Vimentin; K-Ras; acetylation; SIRT1
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Barnoud, T.; Wilkey, D.W.; Merchant, M.L.; Clark, J.A.; Donninger, H. Proteomics Analysis Reveals Novel RASSF2 Interaction Partners. Cancers 2016, 8, 37.

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