Differential regulation of c-Jun and JunD by ubiquitin-dependent protein degradation

AM Musti, M Treier, FA Peverali… - … Chemistry Hoppe-Seyler, 1996 - degruyter.com
AM Musti, M Treier, FA Peverali, D Bohmann
Biological Chemistry Hoppe-Seyler, 1996degruyter.com
* Corresponding author c-Jun and JunD are two closely related members of the Jun family of
transcription factors which markedly differ in their biological functions. Whereas c-Jun
behaves as a positive regulator of cell growth and may cause cell transformation when
overexpressed, JunD antagonizes both of these effects. To better understand how the
activities of c-Jun and JunD are controlled, we investigated how their stabilities within the
cell are determined. We show that, in contrast to c-Jun which is degraded following multi …
* Corresponding author c-Jun and JunD are two closely related members of the Jun family of transcription factors which markedly differ in their biological functions. Whereas c-Jun behaves as a positive regulator of cell growth and may cause cell transformation when overexpressed, JunD antagonizes both of these effects. To better understand how the activities of c-Jun and JunD are controlled, we investigated how their stabilities within the cell are determined. We show that, in contrast to c-Jun which is degraded following multi ubiquitination, JunD is not efficiently ubiquitinated and exhibits a correspondingly longer half-life. Mutational analysis reveals that the determinant for the difference in ubiquitination resides in the NH2-terminal regions of the proteins which in c-Jun contains the-domain.
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