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Título: | Testing the function of calmodulin (CaM) in epidermal growth factor signaling using conditional CaM-knockout cells |
Autor: | Berchtold, Martin W.; Panina, Svetlana; Stateva, Silvia R. CSIC; Villalobo, Antonio CSIC ORCID | Fecha de publicación: | 2013 | Citación: | Symposium on PI 3-Kinase and Interplay with Other Signaling Pathways (2013) | Resumen: | Calmodulin (CaM) is a major regulator of Ca2+-dependent cellular processes including phosphatidyl inositol-3 kinase related signaling. In contrast to lower eukaryotes, phylogenetically higher organisms have two or three functional genes encoding distinct transcripts for the expression of a single CaM protein sequence identical in all vertebrates. This has been a challenge for achieving conditional CaM-knockout mutants cell lines from vertebrates. Recently, we have described CaM-knockout chicken B lymphoma DT40 cell lines expressing a rat CaM transgene, which is repressible by tetracycline. These cell lines have been shown to be useful to study the functionality of CaM mutants lacking the ability of binding Ca2+ in one or multiple Ca2+-binding sites on the cell viability and proliferative capacity. Using this CaM knock out system we have demonstrated that CaM activates the epidermal growth factor receptor (EGFR) tyrosine kinase by direct binding to the receptor. Although the EGFR expressed in these cells is under the control of an exogenous promoter unrelated to the endogenous one, the expression of the transcript as well as the EGFR protein were found to be regulated by CaM in a biphasic manner. This points to the possibility of using these conditional CaM-knockout cells to study putative CaM-regulated transcriptional and translational events. We have previously demonstrated that CaM is phosphorylated at tyrosine residues by the EGFR. Thus, we are also pursuing studies in these cells on the action of transfected non-phosphorylatable and phosphomimetic CaM mutants on the functionality of the EGFR. Our novel genetic system offers the unique opportunity to study the function of CaM in connection with the multitude of CaM targets in signaling process without the use of pharmacological inhibitors, which are frequently unspecific. | Descripción: | Resumen del póster presentado al Keystone Symposium on PI 3-Kinase and Interplay with Other Signaling Pathways celebrado en Keystone-Colorado (US) del 24 de febrero al 1 de marzo de 2013. | URI: | http://hdl.handle.net/10261/125293 |
Aparece en las colecciones: | (IIBM) Comunicaciones congresos |
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