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Structural basis for tail-anchored membrane protein biogenesis by the get3-receptor complex

Tail-anchored (TA) proteins are involved in cellular processes including trafficking, degradation, and apoptosis. They contain a C-terminal membrane anchor and are posttranslationally delivered to the endoplasmic reticulum (ER) membrane by the Get3 adenosine triphosphatase interacting with the heter...

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Hauptverfasser: Stefer, Susanne (VerfasserIn) , Reitz, Simon (VerfasserIn) , Wang, Fei (VerfasserIn) , Wild, Klemens (VerfasserIn) , Pang, Yin-Yuin (VerfasserIn) , Schwarz, Daniel (VerfasserIn) , Bomke, Jörg (VerfasserIn) , Hein, Christopher (VerfasserIn) , Löhr, Frank (VerfasserIn) , Bernhard, Frank (VerfasserIn) , Denic, Vladimir (VerfasserIn) , Dötsch, Volker (VerfasserIn) , Sinning, Irmgard (VerfasserIn)
Dokumenttyp: Article (Journal) Kapitel/Artikel
Sprache:Englisch
Veröffentlicht: 30 June 2011
In: Science
Year: 2011, Jahrgang: 333, Heft: 6043, Pages: 758-762
DOI:10.1126/science.1207125
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1126/science.1207125
Verlag, lizenzpflichtig, Volltext: https://www.science.org/doi/10.1126/science.1207125
Volltext
Verfasserangaben:Susanne Stefer, Simon Reitz, Fei Wang, Klemens Wild, Yin-Yuin Pang, Daniel Schwarz, Jörg Bomke, Christopher Hein, Frank Löhr, Frank Bernhard, Vladimir Denic, Volker Dötsch, Irmgard Sinning
Beschreibung
Zusammenfassung:Tail-anchored (TA) proteins are involved in cellular processes including trafficking, degradation, and apoptosis. They contain a C-terminal membrane anchor and are posttranslationally delivered to the endoplasmic reticulum (ER) membrane by the Get3 adenosine triphosphatase interacting with the hetero-oligomeric Get1/2 receptor. We have determined crystal structures of Get3 in complex with the cytosolic domains of Get1 and Get2 in different functional states at 3.0, 3.2, and 4.6 angstrom resolution. The structural data, together with biochemical experiments, show that Get1 and Get2 use adjacent, partially overlapping binding sites and that both can bind simultaneously to Get3. Docking to the Get1/2 complex allows for conformational changes in Get3 that are required for TA protein insertion. These data suggest a molecular mechanism for nucleotide-regulated delivery of TA proteins.
Beschreibung:Gesehen am 21.10.2022
Beschreibung:Online Resource
DOI:10.1126/science.1207125

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