Degradation of Proteins by Ubiquitin‑Proteasome Pathway

Authors: J. Matějíková 1;  L. Kubiczková 1,2;  L. Sedlaříková 1;  A. Potáčová 1;  R. Hájek 1,2;  S. Ševčíková 1,2
Authors‘ workplace: Babákova myelomová skupina, Ústav patologické fyziologie, LF MU, Brno2 Oddělení klinické hematologie, FN Brno 1
Published in: Klin Onkol 2013; 26(4): 251-256
Category: Reviews


All intracellular and some extracellular proteins are continually degraded and replaced by synthesis of new proteins. Both these processes need to stay in equilibrium since their balance may lead to emergence of diseases. Cells contain many proteolytic systems that ensure highly specific and controlled degradation of proteins. One of these systems is the proteasome, a very complex molecular engine allowing degradation of proteins conjugated to ubiquitin. Since the first isolation of proteasome in 1968, many details about its function have been uncovered. In 2004, Nobel Prize for chemistry was awarded for these discoveries. In our review article, we aimed to summarize information about the mechanism of highly selective degradation of proteins by the ubiquitin‑proteasome pathway. Individual parts of the paper summarize cur­rent knowledge about highly selective degradation of proteins by the ubiquitin‑proteasome system, mechanisms of protein degradation regulation and bio­logical effects of proteasome inhibitors.

Key words:
proteasome – ubiquitin – NF-kappa B – proteasome inhibitors – protein degradation


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