Dissociation of beta(2)m from MHC class I triggers formation of noncovalent transient heavy chain dimers
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dc.contributor.author | Dirscherl, Cindy | |
dc.contributor.author | Loechte, Sara | |
dc.contributor.author | Hein, Zeynep | |
dc.contributor.author | Kopicki, Janine-Denise | |
dc.contributor.author | Harders, Antonia Regina | |
dc.contributor.author | Linden, Noemi | |
dc.contributor.author | Karner, Andreas | |
dc.contributor.author | Preiner, Johannes | |
dc.contributor.author | Weghuber, Julian | |
dc.contributor.author | Garcia-Alai, Maria | |
dc.contributor.author | Uetrecht, Charlotte | |
dc.contributor.author | Zacharias, Martin | |
dc.contributor.author | Piehler, Jacob | |
dc.contributor.author | Lanzerstorfer, Peter | |
dc.contributor.author | Springer, Sebastian | |
dc.date.accessioned | 2023-02-17T11:36:38Z | - |
dc.date.available | 2023-02-17T11:36:38Z | - |
dc.date.issued | 2022 | |
dc.identifier.issn | 0021-9533 | |
dc.identifier.uri | http://osnascholar.ub.uni-osnabrueck.de/handle/unios/65611 | - |
dc.description.abstract | At the plasma membrane of mammalian cells, major histocompatibility complex class I molecules (MHC-I) present antigenic peptides to cytotoxic T cells. Following the loss of the peptide and the light chain beta-2 microglobulin ((beta(2)m, encoded by B2M), the resulting free heavy chains (FHCs) can associate into homotypic complexes in the plasma membrane. Here, we investigate the stoichiometry and dynamics of MHC-I FHCs assemblies by combining a micropattem assay with fluorescence recovery after photobleaching (FRAP) and with single-molecule co-tracking. We identify non-covalent MHC-I FHC dimers, with dimerization mediated by the alpha(3) domain, as the prevalent species at the plasma membrane, leading a moderate decrease in the diffusion coefficient. MHC-I FHC dimers show increased tendency to cluster into higher order oligomers as concluded from an increased immobile fraction with higher single-molecule colocalization. In vitro studies with isolated proteins in conjunction with molecular docking and dynamics simulations suggest that in the complexes, the alpha(3) domain of one FHC binds to another FHC in a manner similar to that seen for beta(2)m. | |
dc.description.sponsorship | Deutsche Forschungsgemeinschaft (DFG) [SP583/7-2, SP583/18-1]; Bundesministerium fur Bildung und Forschung (BMBF) [031A153A]; Tonjes Vagt Foundation (XXXII), iNEXT-Discovery, Jacobs University [11911]; DFG [SFB 944, PI 405/14-1]; province of Upper Austria as a part of the FH Upper Austria Center of Excellence for Technological Innovation in Medicine (TIMed Center); Austrian Science Fund (FWF) [I4972-B]; Christian Doppler Forschungsgesellschaft (Josef Ressel Center for Phytogenic Drug Research); Leibniz Association [SAW-2014-HPI-4]; This work was supported by Deutsche Forschungsgemeinschaft (DFG, SP583/7-2 and SP583/18-1), Bundesministerium fur Bildung und Forschung (BMBF, 031A153A); Tonjes Vagt Foundation (XXXII), iNEXT-Discovery (11911), Jacobs University (all to S.Sp.); DFG (SFB 944, projects P8 and Z, Facility iBiOs, PI 405/14-1) to J. Piehler, P.L. and J.W. acknowledge funding from the province of Upper Austria as a part of the FH Upper Austria Center of Excellence for Technological Innovation in Medicine (TIMed Center), the Austrian Science Fund (FWF, project I4972-B) and the Christian Doppler Forschungsgesellschaft (Josef Ressel Center for Phytogenic Drug Research). C.U. acknowledges funding from the Leibniz Association through grant SAW-2014-HPI-4. | |
dc.language.iso | en | |
dc.publisher | COMPANY BIOLOGISTS LTD | |
dc.relation.ispartof | JOURNAL OF CELL SCIENCE | |
dc.subject | Antigen presentation | |
dc.subject | ASSOCIATION | |
dc.subject | Cell Biology | |
dc.subject | DIMERIZATION | |
dc.subject | HLA CLASS-I | |
dc.subject | Major histocompatibility complex class I | |
dc.subject | MASS | |
dc.subject | MHC-I | |
dc.subject | MOBILITY | |
dc.subject | MOLECULES | |
dc.subject | OPEN CONFORMERS | |
dc.subject | Protein oligomerization | |
dc.subject | PROTEINS | |
dc.subject | RECEPTOR | |
dc.subject | SURFACE | |
dc.title | Dissociation of beta(2)m from MHC class I triggers formation of noncovalent transient heavy chain dimers | |
dc.type | journal article | |
dc.identifier.doi | 10.1242/jcs.259498 | |
dc.identifier.isi | ISI:000798126500013 | |
dc.description.volume | 135 | |
dc.description.issue | 9 | |
dc.contributor.orcid | 0000-0002-1991-7922 | |
dc.contributor.orcid | 0000-0002-6755-6543 | |
dc.contributor.orcid | 0000-0001-5035-6716 | |
dc.contributor.orcid | 0000-0001-9806-5352 | |
dc.contributor.orcid | 0000-0002-5527-6149 | |
dc.contributor.orcid | 0000-0002-4014-5605 | |
dc.contributor.orcid | 0000-0002-2143-2270 | |
dc.contributor.orcid | 0000-0001-6312-4666 | |
dc.contributor.researcherid | D-1883-2010 | |
dc.identifier.eissn | 1477-9137 | |
dc.publisher.place | BIDDER BUILDING, STATION RD, HISTON, CAMBRIDGE CB24 9LF, ENGLAND | |
dcterms.isPartOf.abbreviation | J. Cell Sci. | |
dcterms.oaStatus | Green Submitted | |
local.import.remains | affiliations : Jacobs University; University Osnabruck; University Osnabruck; Heinrich Pette Institute; European Molecular Biology Laboratory (EMBL); European XFEL; Technical University of Munich | |
local.import.remains | web-of-science-index : Science Citation Index Expanded (SCI-EXPANDED) | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0002-2143-2270 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | PiJa938 | - |
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geprüft am 20.05.2024