PUBLICATION
The RING domain of Siaz, the zebrafish homologue of Drosophila seven in absentia, is essential for cellular growth arrest
- Authors
- Ro, H., Jang, Y., and Rhee, M.
- ID
- ZDB-PUB-040402-5
- Date
- 2004
- Source
- Molecules and cells 17(1): 160-165 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Cytoskeletal Proteins/chemistry
- Nuclear Proteins/biosynthesis*
- Nuclear Proteins/chemistry*
- Nuclear Proteins/genetics*
- Nuclear Proteins/metabolism
- Protein Binding
- Blotting, Western
- beta Catenin
- Glutathione Transferase/metabolism
- Animals
- Mitosis
- Transfection
- Trans-Activators/chemistry
- Phosphorylation
- HeLa Cells
- Microscopy, Fluorescence
- DNA/metabolism
- Ubiquitin-Protein Ligases
- Humans
- Protein Structure, Tertiary
- Flow Cytometry
- Trypan Blue/pharmacology
- G2 Phase
- Zebrafish Proteins/biosynthesis*
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics*
- Zebrafish
- Recombinant Fusion Proteins/metabolism
- PubMed
- 15055544
Citation
Ro, H., Jang, Y., and Rhee, M. (2004) The RING domain of Siaz, the zebrafish homologue of Drosophila seven in absentia, is essential for cellular growth arrest. Molecules and cells. 17(1):160-165.
Abstract
Siah is a mammalian homologue of Drosophila seven in absentia (sina) that is required for R7 photoreceptor development. Both the SINA and Siah family interact with ubiquitin-conjugating enzymes via an N-terminal RING domain and the C-terminal domain of SINA/ Siahs interacts with proteins targeted for degradation. Siah induces cell growth arrest by promoting beta-catenin degradation in a phosphorylation-independent manner as a result of indirect binding to beta-catenin. We previously cloned a zebrafish homologue (Siaz) of Siah. Siaz shares high sequence homology with vertebrate Siah-2. We have now examined the role of Siaz in growth regulation using the trypan blue exclusion assay and flow cytometry and found that Siaz induces cellular growth arrest by inhibiting the G2/M transition. The C-terminal domain of Siaz that interacts with target proteins is not required for growth inhibition. We conclude that the N-terminal RING and central domain of Siaz are sufficient to block the G2/M phase transition.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping