Helmholtz Gemeinschaft


The E3-ubiquitin ligase MID1 catalyzes ubiquitination and cleavage of Fu

[thumbnail of Original article]
PDF (Original article) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader

Item Type:Article
Title:The E3-ubiquitin ligase MID1 catalyzes ubiquitination and cleavage of Fu
Creators Name:Schweiger, S., Dorn, S., Fuchs, M., Köhler, A., Matthes, F., Müller, E.C., Wanker, E., Schneider, R. and Krauß, S.
Abstract:Sonic Hedgehog (SHH)-GLI signalling plays an important role during embryogenesis and in tumorigenesis. The survival and growth of several types of cancer depend on autonomously activated SHH-GLI signalling. A protein complex containing the ubiquitin-ligase MID1 and protein phosphatase 2A (PP2A) regulates the nuclear localization and transcriptional activity of GLI3, a transcriptional effector molecule of SHH, in cancer cell lines with autonomously activated SHH signalling. However, the exact molecular mechanisms that mediate the interaction between MID1 and GLI3 remained unknown. Here, we show that MID1 catalyses the ubiquitination and proteasomal cleavage of the GLI3-regulator Fu. Our data suggest that Fu ubiquitination and cleavage is one of the key elements connecting the MID1/PP2A protein complex with GLI3 activity control.
Keywords:Cancer Biology, Proteasome, Protein Phosphatase 2 (PP2A), Signal Transduction, Ubiquitination, Fu, GLI3, MID1, Proteasomal Cleavage
Source:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology
Page Range:31805-31817
Date:14 November 2014
Official Publication:https://doi.org/10.1074/jbc.M113.541219
PubMed:View item in PubMed

Repository Staff Only: item control page


Downloads per month over past year

Open Access
MDC Library