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10.1038/ncomms15976 http://scihub22266oqcxt.onion/10.1038/ncomms15976 C5519985!5519985 !28706306     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28706306 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Nat+Commun 2017 ; 8 (?): 15976 Nephropedia Template TP {{tp|p=28706306 |t=2017. Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments |pdf=|usr=}}{{28706306 }} gab.com Text Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28706306 #FOAvip The 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 signalling. Twit Text FOAVip Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28706306 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28706306 #FOAvip English Wikipedia <ref>{{Cite pmid|28706306 }}</ref> Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments #MMPMID28706306 Richter D ; Moraga I ; Winkelmann H ; Birkholz O ; Wilmes S ; Schulte M ; Kraich M ; Kenneweg H ; Beutel O ; Selenschik P ; Paterok D ; Gavutis M ; Schmidt T ; Garcia KC ; Müller TD ; Piehler J Nat Commun 2017[Jul]; 8 (?): 15976 PMID28706306 show ga The 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 signalling. |Actin Cytoskeleton [MESH] |Cell Compartmentation [MESH] |Cell Membrane/*metabolism [MESH] |Dimerization [MESH] |HeLa Cells [MESH] |Humans [MESH] |Ligands [MESH] |Receptors, Interleukin-4, Type II/agonists/*metabolism [MESH]Ligand-induced type II interleukin-4 receptor dimers are sustained by (epmc).pdf DeepDyve Pubget Overpricing