PuSH - Publikationsserver des Helmholtz Zentrums München

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Abfrage Programm/Institut/Gruppe PSP-Element Kontakt Anhang Verwendung Publikation
Titel:

Visualization of ligand-induced transmembrane signaling in the full-length human insulin receptor.


Titel Pressemitteilung:

So funktioniert der Insulinrezeptor

How the insulin receptor works

Apr 2018 IPI
HDC
SAM
G-502600-002
Dr. Ünal Coskun PDF
PM DE: PDF
PM EN: PDF
PR 2018-02-01
Publikation
Core statement:

The activation mechanism of the fully intact human insulin receptor was directly visualized for the first time.

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)2 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.


Core statement Pressemitteilung:

Knapp 100 Jahre nach der Entdeckung des Insulins konnte ein deutsch-amerikanisches Forscherteam zeigen, wie genau das Hormon seinen Rezeptor aktiviert. Die Ergebnisse und Bilder veröffentlichten die Wissenschaftlerinnen und Wissenschaftler nun im ‚Journal of Cell Biology‘. Für das Projekt hatten Autoren des Paul-Langerhans-Instituts Dresden des Helmholtz Zentrum München am Universitätsklinikum Carl Gustav Carus der TU Dresden mit Kollegen der New Yorker Rockefeller University kooperiert.

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