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AuthorSchuhholz, Juliadc.contributor.author
Date of accession2016-03-15T06:24:43Zdc.date.accessioned
Available in OPARU since2016-03-15T06:24:43Zdc.date.available
Year of creation2010dc.date.created
AbstractTransmembrane signaling of chemokines is mediated by chemokine receptors, members of the G protein-coupled receptor family, which are coupled to pertussis toxin-sensitive and certain cases, also to pertussis toxin-insensitive G proteins. We have previously reported that stimulation with CCL2 of the two human CC chemokine receptors CCR2a and CCR2b transiently expressed in COS-7 cells resulted in inositol phosphate formation and serum response factor (SRF)-dependent transcriptional activation of a luciferase reporter gene. We now report that ligand-dependent induction of SRF activity was specifically mediated by Galphaq and Galpha14, but not by Galpha11 and Galpha16 in these cells. Furthermore we identified a juxtamembrane octapeptide that is important for interaction with the previously identified non-G-protein interaction partner tumor protein D52 of CCR2 receptors and that might be critically involved in Gq protein activation and intracellular trafficking of the receptor polypeptides.dc.description.abstract
Languagededc.language.iso
PublisherUniversität Ulmdc.publisher
LicenseStandard (Fassung vom 01.10.2008)dc.rights
Link to license texthttps://oparu.uni-ulm.de/xmlui/license_v2dc.rights.uri
KeywordCCL2dc.subject
KeywordCCR2dc.subject
KeywordG-Protein gekoppelte Rezeptorendc.subject
KeywordSRFdc.subject
KeywordTPD52dc.subject
Dewey Decimal GroupDDC 610 / Medicine & healthdc.subject.ddc
MeSHGTP-binding proteinsdc.subject.mesh
TitleAnalyse des Einflusses von heterotrimeren G-Proteinen und Nicht-G-Protein-Interaktionspartnern auf die hCCR2-vermittelte Signaltransduktiondc.title
Resource typeDissertationdc.type
DOIhttp://dx.doi.org/10.18725/OPARU-2096dc.identifier.doi
PPN637690710dc.identifier.ppn
URNhttp://nbn-resolving.de/urn:nbn:de:bsz:289-vts-73952dc.identifier.urn
GNDChemokinedc.subject.gnd
GNDG-Proteinedc.subject.gnd
FacultyMedizinische Fakultätuulm.affiliationGeneral
Date of activation2010-10-14T08:09:02Zuulm.freischaltungVTS
Peer reviewneinuulm.peerReview
Shelfmark print versionZ: J-H 13.782; W: W-H 12.252uulm.shelfmark
DCMI TypeTextuulm.typeDCMI
VTS-ID7395uulm.vtsID
CategoryPublikationenuulm.category
University Bibliographyjauulm.unibibliographie


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