Characterization of a fold in TANGO1 evolved from SH3 domains for the export of bulky cargos

  • Bulky cargos like procollagens, apolipoproteins, and mucins exceed the size of conventional COPII vesicles. During evolution a process emerged in metazoans, predominantly governed by the TANGO1 protein family, that organizes cargo at the exit sites of the endoplasmic reticulum and facilitates export by the formation of tunnel-like connections between the ER and Golgi. Hitherto, cargo-recognition appeared to be mediated by an SH3-like domain. Based on structural and dynamic data as well as interaction studies from NMR spectroscopy and microscale thermophoresis presented here, we show that the luminal cargo-recognition domain of TANGO1 adopts a new functional fold for which we suggest the term MOTH (MIA, Otoraplin, TALI/TANGO1 homology) domain. These MOTH domains, as well as an evolutionary intermediate found in invertebrates, constitute a distinct domain family that emerged from SH3 domains and acquired the ability to bind collagen.

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Author:Oliver ArnoldsORCiD, Raphael StollORCiDGND
Parent Title (English):Nature communications
Publisher:Nature Publishing Group UK
Place of publication:London
Document Type:Article
Date of Publication (online):2024/02/08
Date of first Publication:2023/04/20
Publishing Institution:Ruhr-Universität Bochum, Universitätsbibliothek
Tag:Open Access Fonds
Issue:Article 2273
First Page:2273-1
Last Page:2273-12
Article Processing Charge funded by the Deutsche Forschungsgemeinschaft (DFG) and the Open Access Publication Fund of Ruhr-Universität Bochum.
Institutes/Facilities:Lehrstuhl Biochemie II, Arbeitsgruppe Biomolekulare NMR-Spektroskopie
Dewey Decimal Classification:Naturwissenschaften und Mathematik / Chemie, Kristallographie, Mineralogie
open_access (DINI-Set):open_access
faculties:Fakultät für Chemie und Biochemie
Licence (English):License LogoCreative Commons - CC BY 4.0 - Attribution 4.0 International