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A crosstalk between hSiah2 and Pias E3-ligases modulates Pias-dependent activation
- Source :
- Oncogene. 26:6665-6676
- Publication Year :
- 2007
- Publisher :
- Springer Science and Business Media LLC, 2007.
-
Abstract
- Protein inhibitor of activated STAT (Pias) and human homologues of seven in absentia (hSiah) proteins both exhibit properties of ubiquitin-family peptides conjugating enzymes. Pias present E3-ligase activity for small ubiquitin-related modifiers (Sumo) covalent attachment to their targets. This post-translational modification is responsible for the activation of different transcription factors such as AP1. HSiah proteins possess ubiquitin-E3-ligase activity that triggers their partners to proteasomal-dependent degradation. The present study identifies Pias as a new hSiah2-interacting protein. We demonstrate that hSiah2 regulates specifically the proteasome-dependent degradation of Pias proteins. On reverse, Pias does not prevent hSiah2 degradation. We provide evidences for hSiah2-dependent degradation of Pias as being a mechanism in the regulation of c-jun N-terminal kinase-activating pathways. This report describes a new interconnection between sumoylation and ubiquitination pathways by regulating the levels of the E3-ligases available for these processes.
- Subjects :
- Transcriptional Activation
Proteasome Endopeptidase Complex
Cancer Research
SUMO-1 Protein
MAP Kinase Kinase 4
Proto-Oncogene Proteins c-jun
Ubiquitin-Protein Ligases
SUMO protein
Biology
Cell Line
Ubiquitin
Genetics
Humans
Protein inhibitor of activated STAT
Molecular Biology
Transcription factor
Cell Nucleus
Ubiquitination
Nuclear Proteins
Protein Inhibitors of Activated STAT
Ubiquitin ligase
Cell biology
Gene Expression Regulation
Proteasome
Biochemistry
biology.protein
Subjects
Details
- ISSN :
- 14765594 and 09509232
- Volume :
- 26
- Database :
- OpenAIRE
- Journal :
- Oncogene
- Accession number :
- edsair.doi.dedup.....cde467456f834a3f2230f00f087a0a06