Interactions of cullin3/KCTD5 complexes with both cytoplasmic and nuclear proteins: Evidence for a role in protein stabilization
Copyright policy )Interactions of cullin3/KCTD5 complexes with both cytoplasmic and nuclear proteins: Evidence for a role in protein stabilization
Based on its specific interaction with cullin3 mediated by an N-terminal BTB/POZ homologous domain, KCTD5 has been proposed to function as substrate adapter for cullin3 based ubiquitin E3 ligases. In the present study we tried to validate this hypothesis through identification and characterization of additional KCTD5 interaction partners. For the replication protein MCM7, the zinc finger protein ZNF711 and FAM193B, a yet poorly characterized cytoplasmic protein, we could demonstrate specific interaction with KCTD5 both in yeast two-hybrid and co-precipitation studies in mammalian cells. Whereas trimeric complexes of cullin3 and KCTD5 with the respective KCTD5 binding partner were formed, KCTD5/cullin3 induced polyubiquitylation and/or proteasome-dependent degradation of these binding partners could not be demonstrated. On the contrary, KCTD5 or Cullin3 overexpression increased ZNF711 protein stability.
Cytoplasm, Potassium Channels, Protein Stability, Ubiquitination, Nuclear Proteins, Cullin Proteins, Minichromosome Maintenance Complex Component 7, Neoplasm Proteins, DNA-Binding Proteins, Protein Transport, Multiprotein Complexes, Two-Hybrid System Techniques, Protein Interaction Mapping, Humans, Cell Division, HeLa Cells
Cytoplasm, Potassium Channels, Protein Stability, Ubiquitination, Nuclear Proteins, Cullin Proteins, Minichromosome Maintenance Complex Component 7, Neoplasm Proteins, DNA-Binding Proteins, Protein Transport, Multiprotein Complexes, Two-Hybrid System Techniques, Protein Interaction Mapping, Humans, Cell Division, HeLa Cells
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