Cargando…
c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides
The oncoprotein c-Fos is a well-recognized AP-1 transcription factor. In addition, this protein associates with the endoplasmic reticulum and activates the synthesis of phospholipids. However, the mechanism by which c-Fos stimulates the synthesis of phospholipids in general and the specific lipid pa...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3237616/ https://www.ncbi.nlm.nih.gov/pubmed/21998197 http://dx.doi.org/10.1091/mbc.E11-03-0259 |
_version_ | 1782218925904232448 |
---|---|
author | Alfonso Pecchio, Adolfo R. Cardozo Gizzi, Andrés M. Renner, Marianne L. Molina-Calavita, María Caputto, Beatriz L. |
author_facet | Alfonso Pecchio, Adolfo R. Cardozo Gizzi, Andrés M. Renner, Marianne L. Molina-Calavita, María Caputto, Beatriz L. |
author_sort | Alfonso Pecchio, Adolfo R. |
collection | PubMed |
description | The oncoprotein c-Fos is a well-recognized AP-1 transcription factor. In addition, this protein associates with the endoplasmic reticulum and activates the synthesis of phospholipids. However, the mechanism by which c-Fos stimulates the synthesis of phospholipids in general and the specific lipid pathways activated are unknown. Here we show that induction of quiescent cells to reenter growth promotes an increase in the labeling of polyphosphoinositides that depends on the expression of c-Fos. We also investigated whether stimulation by c-Fos of the synthesis of phosphatidylinositol and its phosphorylated derivatives depends on the activation of enzymes of the phosphatidylinositolphosphate biosynthetic pathway. We found that c-Fos activates CDP-diacylglycerol synthase and phosphatidylinositol (PtdIns) 4-kinase II α in vitro, whereas no activation of phosphatidylinositol synthase or of PtdIns 4-kinase II β was observed. Both coimmunoprecipitation and fluorescence resonance energy transfer experiments consistently showed a physical interaction between the N-terminal domain of c-Fos and the enzymes it activates. |
format | Online Article Text |
id | pubmed-3237616 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-32376162012-03-01 c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides Alfonso Pecchio, Adolfo R. Cardozo Gizzi, Andrés M. Renner, Marianne L. Molina-Calavita, María Caputto, Beatriz L. Mol Biol Cell Articles The oncoprotein c-Fos is a well-recognized AP-1 transcription factor. In addition, this protein associates with the endoplasmic reticulum and activates the synthesis of phospholipids. However, the mechanism by which c-Fos stimulates the synthesis of phospholipids in general and the specific lipid pathways activated are unknown. Here we show that induction of quiescent cells to reenter growth promotes an increase in the labeling of polyphosphoinositides that depends on the expression of c-Fos. We also investigated whether stimulation by c-Fos of the synthesis of phosphatidylinositol and its phosphorylated derivatives depends on the activation of enzymes of the phosphatidylinositolphosphate biosynthetic pathway. We found that c-Fos activates CDP-diacylglycerol synthase and phosphatidylinositol (PtdIns) 4-kinase II α in vitro, whereas no activation of phosphatidylinositol synthase or of PtdIns 4-kinase II β was observed. Both coimmunoprecipitation and fluorescence resonance energy transfer experiments consistently showed a physical interaction between the N-terminal domain of c-Fos and the enzymes it activates. The American Society for Cell Biology 2011-12-15 /pmc/articles/PMC3237616/ /pubmed/21998197 http://dx.doi.org/10.1091/mbc.E11-03-0259 Text en © 2011 Alfonso Pecchio et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Alfonso Pecchio, Adolfo R. Cardozo Gizzi, Andrés M. Renner, Marianne L. Molina-Calavita, María Caputto, Beatriz L. c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides |
title | c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides |
title_full | c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides |
title_fullStr | c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides |
title_full_unstemmed | c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides |
title_short | c-Fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides |
title_sort | c-fos activates and physically interacts with specific enzymes of the pathway of synthesis of polyphosphoinositides |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3237616/ https://www.ncbi.nlm.nih.gov/pubmed/21998197 http://dx.doi.org/10.1091/mbc.E11-03-0259 |
work_keys_str_mv | AT alfonsopecchioadolfor cfosactivatesandphysicallyinteractswithspecificenzymesofthepathwayofsynthesisofpolyphosphoinositides AT cardozogizziandresm cfosactivatesandphysicallyinteractswithspecificenzymesofthepathwayofsynthesisofpolyphosphoinositides AT rennermariannel cfosactivatesandphysicallyinteractswithspecificenzymesofthepathwayofsynthesisofpolyphosphoinositides AT molinacalavitamaria cfosactivatesandphysicallyinteractswithspecificenzymesofthepathwayofsynthesisofpolyphosphoinositides AT caputtobeatrizl cfosactivatesandphysicallyinteractswithspecificenzymesofthepathwayofsynthesisofpolyphosphoinositides |