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

Oliver Arnolds and Raphael Stoll ()
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Oliver Arnolds: Ruhr University of Bochum
Raphael Stoll: Ruhr University of Bochum

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: Abstract 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.

Date: 2023
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DOI: 10.1038/s41467-023-37705-4

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