A novel protein phosphatase 2C family member (PP2Cζ) is able to associate with ubiquitin conjugating enzyme 91
Autor: | Mitsuhiro Kashiwaba, Shinri Tamura, Mutsuo Sasaki, Takayasu Kobayashi, Koji Katsura, Motoko Ohnishi, Hiromitsu Tanaka, Yoshitake Nishimune |
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Rok vydání: | 2003 |
Předmět: |
chemistry.chemical_classification
biology Phosphatase Biophysics SUMO enzymes Cell Biology Protein phosphatase 2 Ubiquitin-conjugating enzyme Biochemistry Molecular biology Amino acid Ubiquitin ligase chemistry Structural Biology Genetics biology.protein Northern blot Molecular Biology Peptide sequence |
Zdroj: | FEBS Letters. 538:197-202 |
ISSN: | 0014-5793 |
DOI: | 10.1016/s0014-5793(03)00153-4 |
Popis: | In this study we have cloned a novel member of mouse protein phosphatase 2C family, PP2Cζ, which is composed of 507 amino acids and has a unique N-terminal region. The overall similarity of the amino acid sequence between PP2Cζ and PP2Cα was 22%. On Northern blot analysis PP2Cζ was found to be expressed specifically in the testicular germ cells. PP2Cζ expressed in COS7 cells was able to associate with ubiquitin conjugating enzyme 9 (UBC9) and the association was enhanced by co-expression of small ubiquitin-related modifier-1 (SUMO-1), suggesting that PP2Cζ exhibits its specific role through its SUMO-induced recruitment to UBC9. |
Databáze: | OpenAIRE |
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