Differential Regulation of c-Jun and JunD by Ubiquitin-Dependent Protein Degradation
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...
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Published in | Biological Chemistry Vol. 377; no. 10; pp. 619 - 624 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Berlin, New York
Walter de Gruyter, Berlin / New York
01.10.1996
De Gruyter |
Subjects | |
Online Access | Get full text |
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Summary: | 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 delta-domain. |
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Bibliography: | ArticleID:bchm3.1996.377.10.619 ark:/67375/QT4-F10ZS3SV-J istex:311CBE7F2809E6B90AC2581D92289C78333C0CCF bchm3.1996.377.10.619.pdf ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0177-3593 1431-6730 1437-4315 |
DOI: | 10.1515/bchm3.1996.377.10.619 |