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dc.contributor.authorHolton, Marylouisa
dc.contributor.authorYang, Di
dc.contributor.authorWang, Weiguang
dc.contributor.authorMohamed, Tamer M. A.
dc.contributor.authorNeyses, Ludwig
dc.contributor.authorArmesilla, Angel Luis
dc.date.accessioned2008-07-31T13:39:02Z
dc.date.available2008-07-31T13:39:02Z
dc.date.issued2007
dc.identifier.citationFEBS Letters, 581(21): 4115-4119
dc.identifier.issn0014-5793
dc.identifier.pmid17689535
dc.identifier.doi10.1016/j.febslet.2007.07.054
dc.identifier.urihttp://hdl.handle.net/2436/33739
dc.description.abstractPlasma membrane calcium/calmodulin-dependent ATPases (PMCAs) are high affinity calcium pumps that extrude calcium from the cell. Emerging evidence suggests a novel role for PMCAs as regulators of calcium/calmodulin-dependent signal transduction pathways via interaction with specific partner proteins. In this work, we demonstrate that endogenous human PMCA2 and -4 both interact with the signal transduction phosphatase, calcineurin, whereas, no interaction was detected with PMCA1. The strongest interaction was observed between PMCA2 and calcineurin. The domain of PMCA2 involved in the interaction is equivalent to that reported for PMCA4b. PMCA2-calcineurin interaction results in inhibition of the calcineurin/nuclear factor of activated T-cells signalling pathway.
dc.language.isoen
dc.publisherElsevier
dc.relation.urlhttp://www.febsletters.org/article/S0014-5793(07)00831-9/abstract
dc.subjectPMCA
dc.subjectCalcineurin
dc.subjectInteraction
dc.subjectMCF-7
dc.subjectSignalling
dc.subjectNFAT
dc.subject.meshBreast Neoplasms
dc.subject.meshCalcineurin
dc.subject.meshCalmodulin
dc.subject.meshCell Line, Tumor
dc.subject.meshCell Membrane
dc.subject.meshHumans
dc.subject.meshIsoenzymes
dc.subject.meshNFATC Transcription Factors
dc.subject.meshNeoplasm Proteins
dc.subject.meshPlasma Membrane Calcium-Transporting ATPases
dc.subject.meshProtein Binding
dc.subject.meshProtein Structure, Tertiary
dc.subject.meshSignal Transduction
dc.titleThe interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells
dc.typeJournal article
dc.identifier.journalFEBS Letters
html.description.abstractPlasma membrane calcium/calmodulin-dependent ATPases (PMCAs) are high affinity calcium pumps that extrude calcium from the cell. Emerging evidence suggests a novel role for PMCAs as regulators of calcium/calmodulin-dependent signal transduction pathways via interaction with specific partner proteins. In this work, we demonstrate that endogenous human PMCA2 and -4 both interact with the signal transduction phosphatase, calcineurin, whereas, no interaction was detected with PMCA1. The strongest interaction was observed between PMCA2 and calcineurin. The domain of PMCA2 involved in the interaction is equivalent to that reported for PMCA4b. PMCA2-calcineurin interaction results in inhibition of the calcineurin/nuclear factor of activated T-cells signalling pathway.


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