Balance of Yin and Yang: ubiquitylation-mediated regulation of p53 and c-Myc.
Protein ubiquitylation has been demonstrated to play a vital role not only in mediating protein turnover but also in modulating protein activity. The stability and activity of the tumor suppressor p53 and of the oncoprotein c-Myc are no exception. Both are regulated through independent ubiquitylation by several E3 ubiquitin ligases. Interestingly, p53 and c-Myc are functionally connected by some of these E3 enzymes and their regulator ARF, although these proteins play opposite roles in controlling cell growth and proliferation. The balance of this complex ubiquitylation network and its disruption during oncogenesis will be the topics of this review.
Dai
Mu-Shui
MS
Department of Biochemistry and Molecular Biology, School of Medicine, Oregon Health and Science University, Portland, OR 97239, USA.
Jin
Yetao
Y
Gallegos
Jayme R
JR
Lu
Hua
H
D049109:Cell Proliferation; D002471:Cell Transformation, Neoplastic; D006801:Humans; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism*; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*; D025801:Ubiquitin / Q000502:physiology*; D043743:Ubiquitin-Protein Ligase Complexes / Q000378:metabolism
D016271:Proto-Oncogene Proteins c-myc; D016159:Tumor Suppressor Protein p53; D025801:Ubiquitin; D043743:Ubiquitin-Protein Ligase Complexes