The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu

6533b873fe1ef96bd12d4e17

RESEARCH PRODUCT

The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu

Sybille Krauß Eva-christina Müller Frank Matthes Melanie Fuchs Andrea Köhler Stephanie Dorn Rainer Schneider Susann Schweiger Erich E. Wanker

subject

metabolism [Microtubule Proteins]Ubiquitin-conjugating enzyme Biochemistry metabolism [Protein Serine-Threonine Kinases]Ubiquitin metabolism [Transcription Factors]Nuclear protein Sonic hedgehog biology metabolism [Protein-Serine-Threonine Kinases]Nuclear Proteins respiratory system Protein-Serine-Threonine Kinases Ubiquitin ligase Gene Expression Regulation Neoplastic GLI3 protein human Biochemistry ddc:540 embryonic structures Microtubule Proteins metabolism [Hedgehog Proteins]Function and Dysfunction of the Nervous System metabolism [Nuclear Proteins]Signal Transduction metabolism [Kruppel-Like Transcription Factors]Proteasome Endopeptidase Complex animal structures STK36 protein human Ubiquitin-Protein Ligases Kruppel-Like Transcription Factors Nerve Tissue Proteins Protein Serine-Threonine Kinases chemistry [Ubiquitin-Protein Ligases]Catalysis Zinc Finger Protein Gli3 Cell Line Tumor GLI3 Humans Hedgehog Proteins metabolism [Proteasome Endopeptidase Complex]metabolism [Cell Nucleus]Molecular Biology chemistry [Lysine]DNA Primers Cell Nucleus metabolism [Nerve Tissue Proteins]Ubiquitin Lysine Ubiquitination Cell Biology Protein phosphatase 2 chemistry [Ubiquitin]Proteasome biology.protein SHH protein human human activities Mid1 protein human HeLa Cells Transcription Factors

description

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.

year	journal	country	edition	language
2014-11-14	Journal of Biological Chemistry

https://doi.org/10.1074/jbc.m113.541219