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Visualization of ligand-induced transmembrane signaling in the full-length human insulin receptor.
J. Cell Biol. 217, 1643-1649 (2018)
Publ. Version/Full Text
Research data
DOI
PMC
Insulin receptor (IR) signaling plays a critical role in the regulation of metabolism and growth in multicellular organisms. IRs are unique among receptor tyrosine kinases in that they exist exclusively as covalent (αβ)homodimers at the cell surface. Transmembrane signaling by the IR can therefore not be based on ligand-induced dimerization as such but must involve structural changes within the existing receptor dimer. In this study, using glycosylated full-length human IR reconstituted into lipid nanodiscs, we show by single-particle electron microscopy that insulin binding to the dimeric receptor converts its ectodomain from an inverted U-shaped conformation to a T-shaped conformation. This structural rearrangement of the ectodomain propagates to the transmembrane domains, which are well separated in the inactive conformation but come close together upon insulin binding, facilitating autophosphorylation of the cytoplasmic kinase domains.
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Publication type
Article: Journal article
Document type
Scientific Article
ISSN (print) / ISBN
0021-9525
e-ISSN
1540-8140
Journal
Journal of Cell Biology, The
Quellenangaben
Volume: 217,
Issue: 5,
Pages: 1643-1649
Publisher
Rockefeller University Press
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute for Pancreatic Beta Cell Research (IPI)