The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells

2.50
Hdl Handle:
http://hdl.handle.net/2436/33739
Title:
The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells
Authors:
Holton, Marylouisa; Yang, Di; Wang, Weiguang; Mohamed, Tamer M. A.; Neyses, Ludwig; Armesilla, Angel Luis
Abstract:
Plasma 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.
Citation:
FEBS Letters, 581(21): 4115-4119
Publisher:
Elsevier
Journal:
FEBS Letters
Issue Date:
2007
URI:
http://hdl.handle.net/2436/33739
DOI:
10.1016/j.febslet.2007.07.054
PubMed ID:
17689535
Additional Links:
http://www.febsletters.org/article/S0014-5793(07)00831-9/abstract
Type:
Article
Language:
en
ISSN:
0014-5793
Appears in Collections:
Molecular Pharmacology Research Group

Full metadata record

DC FieldValue Language
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): 4115-4119en
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.en
dc.language.isoenen
dc.publisherElsevieren
dc.relation.urlhttp://www.febsletters.org/article/S0014-5793(07)00831-9/abstracten
dc.subjectPMCAen
dc.subjectCalcineurinen
dc.subjectInteractionen
dc.subjectMCF-7en
dc.subjectSignallingen
dc.subjectNFATen
dc.subject.meshBreast Neoplasmsen
dc.subject.meshCalcineurinen
dc.subject.meshCalmodulinen
dc.subject.meshCell Line, Tumoren
dc.subject.meshCell Membraneen
dc.subject.meshHumansen
dc.subject.meshIsoenzymesen
dc.subject.meshNFATC Transcription Factorsen
dc.subject.meshNeoplasm Proteinsen
dc.subject.meshPlasma Membrane Calcium-Transporting ATPasesen
dc.subject.meshProtein Bindingen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshSignal Transductionen
dc.titleThe interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cellsen
dc.typeArticleen
dc.identifier.journalFEBS Lettersen

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