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Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments

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https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2018043016999
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dc.creatorRichter, David-
dc.creatorMoraga, Ignacio-
dc.creatorWinkelmann, Hauke-
dc.creatorBirkholz, Oliver-
dc.creatorWilmes, Stephan-
dc.creatorSchulte, Markos-
dc.creatorKraich, Michael-
dc.creatorKenneweg, Hella-
dc.creatorBeutel, Oliver-
dc.creatorSelenschik, Philipp-
dc.creatorPaterok, Dirk-
dc.creatorGavutis, Martynas-
dc.creatorSchmidt, Thomas-
dc.creatorGarcia, K. Christopher-
dc.creatorMüller, Thomas D.-
dc.creatorPiehler, Jacob-
dc.date.accessioned2018-04-30T10:13:11Z-
dc.date.available2018-04-30T10:13:11Z-
dc.date.issued2018-04-30T10:13:11Z-
dc.identifier.citationNature Communications 8:15976 (2017). Springer Nature-
dc.identifier.urihttps://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-2018043016999-
dc.description.abstractThe spatiotemporal organization of cytokine receptors in the plasma membrane is still debated with models ranging from ligand-independent receptor pre-dimerization to ligand-induced receptor dimerization occurring only after receptor uptake into endosomes. Here, we explore the molecular and cellular determinants governing the assembly of the type II interleukin-4 receptor, taking advantage of various agonists binding the receptor subunits with different affinities and rate constants. Quantitative kinetic studies using artificial membranes confirm that receptor dimerization is governed by the two-dimensional ligand– receptor interactions and identify a critical role of the transmembrane domain in receptor dimerization. Single molecule localization microscopy at physiological cell surface expression levels, however, reveals efficient ligand-induced receptor dimerization by all ligands, largely independent of receptor binding affinities, in line with the similar STAT6 activation potencies observed for all IL-4 variants. Detailed spatiotemporal analyses suggest that kinetic trapping of receptor dimers in actin-dependent microcompartments sustains robust receptor dimerization and signallingeng
dc.relationhttps://www.nature.com/articles/ncomms15976.pdf-
dc.rightsNamensnennung 4.0 International-
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/-
dc.subjectType II Interleukin-4 receptoreng
dc.subjectre-associationeng
dc.subjectplasma membraneeng
dc.subjectmicrocompartmentseng
dc.subject.ddc570 - Biowissenschaften, Biologie-
dc.titleLigand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartmentseng
dc.typeEinzelbeitrag in einer wissenschaftlichen Zeitschrift [article]ger
dc.identifier.doi10.1038/ncomms15976-
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