What Can Study of Oligomerization of Proteinsin the Process of Oncogenesis Bring Us?

Czech version

Authors: D. Coufalová; B. Vojtěšek; L. Hernychová
Authors‘ workplace: Regionální centrum aplikované molekulární onkologie, Masarykův onkologický ústav, Brno
Published in: Klin Onkol 2015; 28(Supplementum 2): 6-10
doi: https://doi.org/10.14735/amko20152S6

Overview

Many cellular proteins form oligomers. The equilibrium between monomeric and oligomeric states of these proteins is important for the regulation of protein activity. Modulation of the oligomerization equilibrium could be an interesting approach in the development of new therapeutic agents. This review summarizes information about protein oligomerization and modulation of this process, demonstrating the role of oligomerization in oncogenesis by tumor suppressor protein p53, which forms tetrameric structure. Today, many studies focus on finding compounds that stabilize its tetramers. Among the methods for studying oligomerization, we present hydrogen/ deuterium exchange method coupled with mass spectrometry which is suitable for the detection of protein‑protein interaction and analysis of oligomerization dynamics.

Key words:
proteomics – drug design – tumor suppressor protein p53 – oligomerization – hydrogen/ deuterium exchange

This study was supported by the European Regional Development Fund and the State Budget of the Czech Republic (RECAMO, CZ.1.05/2.1.00/03.0101), MEYS – NPS I – LO1413, MH CZ – DRO (MMCI, 00209805) and BBMRI_CZ (LM2010004).

The authors declare they have no potential confl icts of interest concerning drugs, products, or services used in the study.

The Editorial Board declares that the manuscript met the ICMJE “uniform requirements” for biomedical papers.

Submitted:
9. 4. 2015

Accepted:
15. 6. 2015

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