PUBLICATION
Ubiquitination and degradation of the zebrafish paired-like homeobox protein VSX-1
- Authors
- Kurtzman, A.L., Gregori, L., Haas, A.L., Schechter, N.
- ID
- ZDB-PUB-000622-11
- Date
- 2000
- Source
- Journal of neurochemistry 75(1): 48-55 (Journal)
- Registered Authors
- Kurtzman, Aaron, Schechter, Nisson
- Keywords
- retina; bipolar cells; ubiquitin; Chx10; 26S proteasome
- MeSH Terms
-
- Adenosine Triphosphatases/metabolism
- Animals
- COS Cells
- Cysteine Endopeptidases/metabolism
- Electrophoresis, Polyacrylamide Gel
- Eye Proteins/genetics
- Eye Proteins/metabolism*
- Gene Expression
- Homeodomain Proteins/genetics
- Homeodomain Proteins/metabolism*
- Multienzyme Complexes/metabolism
- Proteasome Endopeptidase Complex
- Protein Processing, Post-Translational
- Rabbits
- Reticulocytes/metabolism
- Retina/growth & development
- Transfection
- Ubiquitins/metabolism*
- Zebrafish*
- Zebrafish Proteins*
- PubMed
- 10854246 Full text @ J. Neurochem.
Citation
Kurtzman, A.L., Gregori, L., Haas, A.L., Schechter, N. (2000) Ubiquitination and degradation of the zebrafish paired-like homeobox protein VSX-1. Journal of neurochemistry. 75(1):48-55.
Abstract
:Vsx-1 is a paired-like : CVC homeobox protein dynamically expressed during zebrafish development. Previous results indicate that Vsx-1 influences bipolar cell differentiation and maintenance of these cells in the adult retina. To understand the developmental regulation of this transcription factor, we investigated ubiquitination as a possible posttranslational mechanism. In vitro, Vsx-1 was conjugated with multiple ubiquitin moieties. Proteasome inhibitors and added ubiquitin increased the accumulation of Vsx-1-ubiquitin(n) complexes and stabilized unmodified Vsx-1. Also, in transiently transfected COS-7 cells, Vsx-1 is ubiquitinated, and pulse-chase experiments show that Vsx-1 proteolysis occurs. Vsx-1 proteins with C-terminal deletions retained the capacity for initial modification by ubiquitin but lost the capacity for efficient chain elongation. These results show that Vsx-1 is a substrate of the ubiquitin/proteasome pathway and suggest that C-terminal sequences of Vsx-1 are critical for ubiquitin chain elongation. In addition, our findings suggest that ubiquitin-dependent proteolysis regulates Vsx-1 during zebrafish retinal development.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping