Characterization Of A Protein-protein Interaction Network Of The Cbl-interacting Protein Kinase 8 From Sugarcane.

dc.creatorFarani, T F
dc.creatorGentile, A
dc.creatorTavares, R G
dc.creatorRibeiro, C
dc.creatorMenossi, M
dc.date2015
dc.date2015-11-27T13:46:18Z
dc.date2015-11-27T13:46:18Z
dc.date.accessioned2018-03-29T01:23:43Z
dc.date.available2018-03-29T01:23:43Z
dc.identifierGenetics And Molecular Research : Gmr. v. 14, n. 1, p. 483-91, 2015.
dc.identifier1676-5680
dc.identifier10.4238/2015.January.26.1
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/25729982
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/202171
dc.identifier25729982
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1302404
dc.descriptionPlants are sessile organisms and have evolved to tolerate a constantly changing environment. After the onset of different stress conditions, calcineurin B-like (CBL) proteins can sense calcium signals and activate CBL-interacting protein kinase (CIPK) proteins, which can phosphorylate downstream proteins to reestablish plant homeostasis. Previous studies in the bioenergy crop sugarcane showed that the ScCIPK8 gene is induced by drought stress and is also related to sucrose content. Here, we have characterized the protein-protein interactions of ScCIPK8 with six CBL proteins (ScCBL1, ScCBL2, ScCBL3, ScCBL6, ScCBL9, and ScCBL10). Yeast two-hybrid assays showed that ScCIPK8 interacts with ScCBL1, ScCBL3, and ScCBL6. Bimolecular fluorescence complementation assays confirmed in planta the interactions that were observed in yeast cells. These findings give insights on the regulatory networks related to sugar accumulation and drought stress responses in sugarcane.
dc.description14
dc.description483-91
dc.languageeng
dc.relationGenetics And Molecular Research : Gmr
dc.relationGenet. Mol. Res.
dc.rightsaberto
dc.rights
dc.sourcePubMed
dc.titleCharacterization Of A Protein-protein Interaction Network Of The Cbl-interacting Protein Kinase 8 From Sugarcane.
dc.typeArtículos de revistas


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