Publication:
Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?

cris.virtualsource.author-orcid083943e3-ae7a-4391-91d3-91bed86ab50e
cris.virtualsource.author-orcidb4c31f46-29ab-4035-a115-1542a94c1d9a
datacite.rightsmetadata.only
dc.contributor.authorBabiichuk, Eduard
dc.contributor.authorDraeger, Annette
dc.date.accessioned2024-10-13T13:34:49Z
dc.date.available2024-10-13T13:34:49Z
dc.date.issued2006
dc.description.abstractThe spatial segregation of the plasma membrane plays a prominent role in distinguishing and sorting a large number of signals a cell receives simultaneously. The plasma membrane comprises regions known as lipid rafts, which serve as signal-transduction hubs and platforms for sorting membrane-associated proteins. Ca(2+)-binding proteins of the annexin family have been ascribed a role in the regulation of raft dynamics. Glycosylphosphatidylinositol-anchored 5'-nucleotidase is an extracellular, raft-associated enzyme responsible for conversion of extracellular ATP into adenosine. Our results point to a regulation of ecto-5'-nucleotidase activity by Ca(2+)-dependent, annexin-mediated stabilization of membrane rafts.
dc.description.numberOfPages3
dc.description.sponsorshipInstitut für Anatomie, Zellbiologie
dc.description.sponsorshipInstitut für Anatomie
dc.identifier.isi000238630000011
dc.identifier.pmid16709165
dc.identifier.urihttps://boris-portal.unibe.ch/handle/20.500.12422/92701
dc.language.isoen
dc.publisherPortland Press
dc.publisher.placeLondon
dc.relation.isbn16709165
dc.relation.ispartofBiochemical Society transactions
dc.relation.issn0300-5127
dc.relation.organizationDCD5A442BD6DE17DE0405C82790C4DE2
dc.relation.organizationDCD5A442BCD7E17DE0405C82790C4DE2
dc.titleRegulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?
dc.typearticle
dspace.entity.typePublication
oaire.citation.endPage6
oaire.citation.issuePt 3
oaire.citation.startPage374
oaire.citation.volume34
oairecerif.author.affiliationInstitut für Anatomie, Zellbiologie
oairecerif.author.affiliationInstitut für Anatomie
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.description.ispublishedpub
unibe.eprints.legacyId18923
unibe.journal.abbrevTitleBIOCHEM SOC T
unibe.subtype.articlecontribution

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