University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Medical Biology
  • Medical Biology - Research Publications
  • View Item
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Medical Biology
  • Medical Biology - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site

    Thumbnail
    Download
    Published version (627.3Kb)

    Citations
    Scopus
    Web of Science
    Altmetric
    55
    51
    Author
    Feng, J; Call, ME; Wucherpfennig, KW
    Date
    2006-05-01
    Source Title
    PLoS Biology
    Publisher
    PUBLIC LIBRARY SCIENCE
    University of Melbourne Author/s
    Call, Matthew
    Affiliation
    Medical Biology (W.E.H.I.)
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Feng, J., Call, M. E. & Wucherpfennig, K. W. (2006). The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site. PLOS BIOLOGY, 4 (5), pp.768-779. https://doi.org/10.1371/journal.pbio.0040142.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/256236
    DOI
    10.1371/journal.pbio.0040142
    Abstract
    The majority of receptors responsible for activation of distinct cell types within the immune system assemble with dimeric signaling modules through interaction of a basic transmembrane residue with a pair of acidic residues of the signaling dimer. Because assembly of other membrane proteins requires specific interactions along extended stretches of transmembrane helices, we examined how transmembrane sequences flanking the polar interaction site contribute to assembly for three receptors that associate with different signaling modules-the natural killer cell receptors KIR and NKG2D and the Fc receptor for IgA, FcalphaRI. The KIR and NKG2D receptors assembled with the DAP12 and DAP10 dimers, respectively, even when the entire KIR or NKG2D transmembrane domains were replaced by polyleucine sequences with a properly positioned basic residue. In contrast, a high degree of specificity for the basic side chain could be observed because the KIR-DAP12 and FcalphaRI-Fcgamma interactions favored lysine or arginine, respectively. Steric hindrance among incompatible extra-membranous domains and competition for signaling modules also contributed to specificity of assembly. These results demonstrate that these interactions are focused on the polar site created by three ionizable transmembrane residues, and explain how the DAP12 and Fcgamma signaling modules can assemble with large, non-overlapping sets of receptors that have highly divergent transmembrane sequences.

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [53102]
    • Medical Biology - Research Publications [1415]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors