Are small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis?
External sugar initiates biosynthesis of the reserve carbohydrate fructan, but the molecular processes mediating this response remain obscure. Previously it was shown that a phosphatase and a general kinase inhibitor hamper fructan accumulation. We use various phosphorylation inhibitors both in barl...
Guardado en:
Autores principales: | , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2009
|
Materias: | |
Acceso en línea: | https://doaj.org/article/48776519bc15441c8d82a87898c150b6 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:48776519bc15441c8d82a87898c150b6 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:48776519bc15441c8d82a87898c150b62021-11-25T06:21:03ZAre small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis?1932-620310.1371/journal.pone.0006605https://doaj.org/article/48776519bc15441c8d82a87898c150b62009-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19672308/?tool=EBIhttps://doaj.org/toc/1932-6203External sugar initiates biosynthesis of the reserve carbohydrate fructan, but the molecular processes mediating this response remain obscure. Previously it was shown that a phosphatase and a general kinase inhibitor hamper fructan accumulation. We use various phosphorylation inhibitors both in barley and in Arabidopsis and show that the expression of fructan biosynthetic genes is dependent on PP2A and different kinases such as Tyr-kinases and PI3-kinases. To further characterize the phosphorylation events involved, comprehensive analysis of kinase activities in the cell was performed using a PepChip, an array of >1000 kinase consensus substrate peptide substrates spotted on a chip. Comparison of kinase activities in sugar-stimulated and mock(sorbitol)-treated Arabidopsis demonstrates the altered phosphorylation of many consensus substrates and documents the differences in plant kinase activity upon sucrose feeding. The different phosphorylation profiles obtained are consistent with sugar-mediated alterations in Tyr phosphorylation, cell cycling, and phosphoinositide signaling, and indicate cytoskeletal rearrangements. The results lead us to infer a central role for small GTPases in sugar signaling.Tita RitsemaDavid BrodmannSander H DiksCarina L BosVinay NagarajCorné M J PieterseThomas BollerAndres WiemkenMaikel P PeppelenboschPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 8, p e6605 (2009) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q Tita Ritsema David Brodmann Sander H Diks Carina L Bos Vinay Nagaraj Corné M J Pieterse Thomas Boller Andres Wiemken Maikel P Peppelenbosch Are small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis? |
description |
External sugar initiates biosynthesis of the reserve carbohydrate fructan, but the molecular processes mediating this response remain obscure. Previously it was shown that a phosphatase and a general kinase inhibitor hamper fructan accumulation. We use various phosphorylation inhibitors both in barley and in Arabidopsis and show that the expression of fructan biosynthetic genes is dependent on PP2A and different kinases such as Tyr-kinases and PI3-kinases. To further characterize the phosphorylation events involved, comprehensive analysis of kinase activities in the cell was performed using a PepChip, an array of >1000 kinase consensus substrate peptide substrates spotted on a chip. Comparison of kinase activities in sugar-stimulated and mock(sorbitol)-treated Arabidopsis demonstrates the altered phosphorylation of many consensus substrates and documents the differences in plant kinase activity upon sucrose feeding. The different phosphorylation profiles obtained are consistent with sugar-mediated alterations in Tyr phosphorylation, cell cycling, and phosphoinositide signaling, and indicate cytoskeletal rearrangements. The results lead us to infer a central role for small GTPases in sugar signaling. |
format |
article |
author |
Tita Ritsema David Brodmann Sander H Diks Carina L Bos Vinay Nagaraj Corné M J Pieterse Thomas Boller Andres Wiemken Maikel P Peppelenbosch |
author_facet |
Tita Ritsema David Brodmann Sander H Diks Carina L Bos Vinay Nagaraj Corné M J Pieterse Thomas Boller Andres Wiemken Maikel P Peppelenbosch |
author_sort |
Tita Ritsema |
title |
Are small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis? |
title_short |
Are small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis? |
title_full |
Are small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis? |
title_fullStr |
Are small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis? |
title_full_unstemmed |
Are small GTPases signal hubs in sugar-mediated induction of fructan biosynthesis? |
title_sort |
are small gtpases signal hubs in sugar-mediated induction of fructan biosynthesis? |
publisher |
Public Library of Science (PLoS) |
publishDate |
2009 |
url |
https://doaj.org/article/48776519bc15441c8d82a87898c150b6 |
work_keys_str_mv |
AT titaritsema aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT davidbrodmann aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT sanderhdiks aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT carinalbos aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT vinaynagaraj aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT cornemjpieterse aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT thomasboller aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT andreswiemken aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis AT maikelppeppelenbosch aresmallgtpasessignalhubsinsugarmediatedinductionoffructanbiosynthesis |
_version_ |
1718413799233421312 |