Inhibitor-1 and -2 of PP2A have preference between PP2A complexes
| Autor: | Hirotsugu Hino, Kaori Takaki, Satoru Mochida |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Immunoprecipitation
Protein subunit Parthenogenesis Biophysics Xenopus Gene Expression Xenopus Proteins Biochemistry Xenopus laevis Catalytic Domain Escherichia coli Animals Protein Isoforms Protein Phosphatase 2 Enzyme Inhibitors Interphase Molecular Biology Ovum Binding Sites biology Egg extract Intracellular Signaling Peptides and Proteins Cell Biology Protein phosphatase 2 biology.organism_classification Recombinant Proteins Kinetics Enzyme inhibition Substrate specificity Protein Binding Signal Transduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 467:297-302 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2015.09.168 |
| Popis: | Protein phosphatase 2A (PP2A) forms tens of kinds of complexes with different substrate specificity and functions by using various regulatory B subunits. But how these complexes' activities are regulated separately is not well understood. Here we showed unequal enzyme inhibition of each form by two proteinous PP2A inhibitors, I1(PP2A) and I2(PP2A). Immunoprecipitation assay using Xenopus egg extract showed that I1(PP2A) bound B″/PR48, and I2(PP2A) bound B56γ and B″/PR48 among four B subunits analyzed. Thus I1(PP2A) and I2(PP2A) seem to have B-subunit specificity. These results support the hypothesis that PP2A complexes containing common catalytic subunit are individually regulated for their separate functions in vivo. |
| Databáze: | OpenAIRE |
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