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Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1
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| Zeitschriftentitel: | Journal of Neurochemistry |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Journal of Neurochemistry, 75, 2000, 1, S. 48-55 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Kurtzman, Aaron L. Gregori, Luisa Haas, Arthur L. Schechter, Nisson Kurtzman, Aaron L. Gregori, Luisa Haas, Arthur L. Schechter, Nisson |
|---|---|
| author |
Kurtzman, Aaron L. Gregori, Luisa Haas, Arthur L. Schechter, Nisson |
| spellingShingle |
Kurtzman, Aaron L. Gregori, Luisa Haas, Arthur L. Schechter, Nisson Journal of Neurochemistry Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 Cellular and Molecular Neuroscience Biochemistry |
| author_sort |
kurtzman, aaron l. |
| spelling |
Kurtzman, Aaron L. Gregori, Luisa Haas, Arthur L. Schechter, Nisson 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1046/j.1471-4159.2000.0750048.x <jats:p> <jats:bold>Abstract</jats:bold> : Vsx‐1 is a <jats:italic>paired</jats:italic>‐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<jats:sub>n</jats:sub> 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.</jats:p> Ubiquitination and Degradation of the Zebrafish <i>Paired</i>‐Like Homeobox Protein V<scp>sx</scp>‐1 Journal of Neurochemistry |
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Journal of Neurochemistry |
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| title |
Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_unstemmed |
Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_full |
Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_fullStr |
Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_full_unstemmed |
Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_short |
Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_sort |
ubiquitination and degradation of the zebrafish <i>paired</i>‐like homeobox protein v<scp>sx</scp>‐1 |
| topic |
Cellular and Molecular Neuroscience Biochemistry |
| url |
http://dx.doi.org/10.1046/j.1471-4159.2000.0750048.x |
| publishDate |
2000 |
| physical |
48-55 |
| description |
<jats:p> <jats:bold>Abstract</jats:bold> : Vsx‐1 is a <jats:italic>paired</jats:italic>‐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<jats:sub>n</jats:sub> 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.</jats:p> |
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| author | Kurtzman, Aaron L., Gregori, Luisa, Haas, Arthur L., Schechter, Nisson |
| author_facet | Kurtzman, Aaron L., Gregori, Luisa, Haas, Arthur L., Schechter, Nisson, Kurtzman, Aaron L., Gregori, Luisa, Haas, Arthur L., Schechter, Nisson |
| author_sort | kurtzman, aaron l. |
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| description | <jats:p> <jats:bold>Abstract</jats:bold> : Vsx‐1 is a <jats:italic>paired</jats:italic>‐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<jats:sub>n</jats:sub> 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.</jats:p> |
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| imprint_str_mv | Wiley, 2000 |
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| spelling | Kurtzman, Aaron L. Gregori, Luisa Haas, Arthur L. Schechter, Nisson 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1046/j.1471-4159.2000.0750048.x <jats:p> <jats:bold>Abstract</jats:bold> : Vsx‐1 is a <jats:italic>paired</jats:italic>‐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<jats:sub>n</jats:sub> 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.</jats:p> Ubiquitination and Degradation of the Zebrafish <i>Paired</i>‐Like Homeobox Protein V<scp>sx</scp>‐1 Journal of Neurochemistry |
| spellingShingle | Kurtzman, Aaron L., Gregori, Luisa, Haas, Arthur L., Schechter, Nisson, Journal of Neurochemistry, Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1, Cellular and Molecular Neuroscience, Biochemistry |
| title | Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_full | Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_fullStr | Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_full_unstemmed | Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_short | Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| title_sort | ubiquitination and degradation of the zebrafish <i>paired</i>‐like homeobox protein v<scp>sx</scp>‐1 |
| title_unstemmed | Ubiquitination and Degradation of the Zebrafish Paired‐Like Homeobox Protein Vsx‐1 |
| topic | Cellular and Molecular Neuroscience, Biochemistry |
| url | http://dx.doi.org/10.1046/j.1471-4159.2000.0750048.x |