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Publication : Regulation of ubiquitin ligase dynamics by the nucleolus.

First Author  Mekhail K Year  2005
Journal  J Cell Biol Volume  170
Issue  5 Pages  733-44
PubMed ID  16129783 Mgi Jnum  J:100984
Mgi Id  MGI:3590350 Doi  10.1083/jcb.200506030
Citation  Mekhail K, et al. (2005) Regulation of ubiquitin ligase dynamics by the nucleolus. J Cell Biol 170(5):733-44
abstractText  Cellular pathways relay information through dynamic protein interactions. We have assessed the kinetic properties of the murine double minute protein (MDM2) and von Hippel-Lindau (VHL) ubiquitin ligases in living cells under physiological conditions that alter the stability of their respective p53 and hypoxia-inducible factor substrates. Photobleaching experiments reveal that MDM2 and VHL are highly mobile proteins in settings where their substrates are efficiently degraded. The nucleolar architecture converts MDM2 and VHL to a static state in response to regulatory cues that are associated with substrate stability. After signal termination, the nucleolus is able to rapidly release these proteins from static detention, thereby restoring their high mobility profiles. A protein surface region of VHL's beta-sheet domain was identified as a discrete [H+]-responsive nucleolar detention signal that targets the VHL/Cullin-2 ubiquitin ligase complex to nucleoli in response to physiological fluctuations in environmental pH. Data shown here provide the first evidence that cells have evolved a mechanism to regulate molecular networks by reversibly switching proteins between a mobile and static state.
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