Journal
CELL BIOLOGY INTERNATIONAL
Volume 32, Issue 2, Pages 298-303Publisher
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.cellbi.2007.10.005
Keywords
cAMP; A-kinase; GATA-6; SREBP; Proteolysis; CHO-K1
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Funding
- MEXT [14370744]
- Terumo Life Science Foundation
- Grants-in-Aid for Scientific Research [14370744] Funding Source: KAKEN
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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. (C) 2007 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved.
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