Cyclic AMP-dependent proteolysis of GATA-6 expressed on the intracellular membrane
| Autor: | Kae Uetani, Takeshi Tsuge, Masatomo Maeda, Ayako Ohashi-Kobayashi, Ryuichiro Sato |
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| Rok vydání: | 2008 |
| Předmět: |
Recombinant Fusion Proteins
Proteolysis Lactacystin CHO Cells Endoplasmic Reticulum medicine.disease_cause chemistry.chemical_compound Cricetulus Cricetinae GATA6 Transcription Factor Cyclic AMP medicine Animals Humans Moiety Enzyme Inhibitors medicine.diagnostic_test Endoplasmic reticulum Cholera toxin Intracellular Membranes Cell Biology General Medicine Fusion protein Cell biology Cholesterol Bucladesine Proteasome chemistry Biochemistry Cytoplasm Sterol Regulatory Element Binding Protein 2 |
| Zdroj: | Cell Biology International. 32:298-303 |
| ISSN: | 1065-6995 |
| DOI: | 10.1016/j.cellbi.2007.10.005 |
| Popis: | Cyclic AMP-dependent proteolysis of GATA-6 was characterized by fusing GATA-6 with the carboxyl-terminal membrane domain of SREBP-2. When the fusion protein was stably expressed in CHO-K1 cells, it was recovered in the ER membrane. This protein was processed in a similar manner to SREBP-2 upon cholesterol starvation, and the GATA-6 moiety moved into the nucleus. The GATA-6 moiety on the membrane became undetectable in the presence of dbcAMP or cholera toxin. However, H-89, K-252a, MG115 and lactacystin inhibited this decrease, suggesting that the cytoplasmic GATA-6 moiety of the fusion protein was degraded by proteasomes though A-kinase upon elevation of the cellular cAMP concentration. |
| Databáze: | OpenAIRE |
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