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dc.contributor.authorKillock, DJ
dc.contributor.authorParsons, M
dc.contributor.authorZarrouk, M
dc.contributor.authorAmeer-Beg, SM
dc.contributor.authorRidley, AJ
dc.contributor.authorHaskard, DO
dc.contributor.authorZvelebil, M
dc.contributor.authorIvetic, A
dc.date.accessioned2018-08-30T08:16:33Z
dc.date.issued2009-03
dc.identifier.citationThe Journal of biological chemistry, 2009, 284 (13), pp. 8833 - 8845
dc.identifier.issn0021-9258
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2415
dc.identifier.eissn1083-351X
dc.identifier.doi10.1074/jbc.m806983200
dc.description.abstractL-selectin is a cell adhesion molecule that tethers leukocytes to the luminal walls of venules during inflammation and enables them to roll under the force of blood flow. Clustering of L-selectin during rolling is thought to promote outside-in signals that lead to integrin activation and chemokine receptor expression, ultimately contributing to leukocyte arrest. Several studies have underscored the importance of the L-selectin cytoplasmic tail in functionally regulating adhesion and signaling. Interestingly, the L-selectin tail comprises only 17 amino acids, and yet it is thought to bind simultaneously to several proteins. For example, constitutive association of calmodulin (CaM) and ezrin/radixin/moesin (ERM) to L-selectin confers resistance to proteolysis and microvillar positioning, respectively. In this report we found that recombinant purified CaM and ERM bound non-competitively to the same tail of L-selectin. Furthermore, molecular modeling supported the possibility that CaM, L-selectin, and moesin could form a heterotrimeric complex. Finally, using fluorescence lifetime imaging microscopy to measure fluorescence resonance energy transfer, it was shown that CaM, L-selectin, and ERM could interact simultaneously in vivo. Moreover, L-selectin clustering promoted CaM/ERM interaction in cis (i.e. derived from neighboring L-selectin tails). These results highlight a novel intracellular event that occurs as a consequence of L-selectin clustering, which could participate in transducing signals that promote the transition from rolling to arrest.
dc.formatPrint-Electronic
dc.format.extent8833 - 8845
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0
dc.subjectCOS Cells
dc.subjectU937 Cells
dc.subjectAnimals
dc.subjectHumans
dc.subjectMultiprotein Complexes
dc.subjectMicrofilament Proteins
dc.subjectCalmodulin
dc.subjectCytoskeletal Proteins
dc.subjectL-Selectin
dc.subjectMembrane Proteins
dc.subjectRecombinant Proteins
dc.subjectSignal Transduction
dc.subjectLeukocyte Rolling
dc.subjectProtein Binding
dc.subjectChlorocebus aethiops
dc.titleIn Vitro and in Vivo Characterization of Molecular Interactions between Calmodulin, Ezrin/Radixin/Moesin, and L-selectin.
dc.typeJournal Article
rioxxterms.versionofrecord10.1074/jbc.m806983200
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by-nc/4.0
rioxxterms.licenseref.startdate2009-03
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfThe Journal of biological chemistry
pubs.issue13
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Cancer Informatics
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Cancer Informatics
pubs.publication-statusPublished
pubs.volume284
pubs.embargo.termsNot known
icr.researchteamCancer Informaticsen_US
dc.contributor.icrauthorZvelebil, Marketa Judithaen


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