A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD

Jennifer Schoberer (), Julia König, Christiane Veit, Ulrike Vavra, Eva Liebminger, Stanley W. Botchway, Friedrich Altmann, Verena Kriechbaumer, Chris Hawes and Richard Strasser
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Jennifer Schoberer: University of Natural Resources and Life Sciences, Vienna
Julia König: University of Natural Resources and Life Sciences, Vienna
Christiane Veit: University of Natural Resources and Life Sciences, Vienna
Ulrike Vavra: University of Natural Resources and Life Sciences, Vienna
Eva Liebminger: University of Natural Resources and Life Sciences, Vienna
Stanley W. Botchway: Central Laser Facility, Science and Technology Facilities Council (STFC), Rutherford Appleton Laboratory, Research Complex at Harwell
Friedrich Altmann: University of Natural Resources and Life Sciences, Vienna
Verena Kriechbaumer: Oxford Brookes University, Gipsy Lane, Headington
Chris Hawes: Oxford Brookes University, Gipsy Lane, Headington
Richard Strasser: University of Natural Resources and Life Sciences, Vienna

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract The Arabidopsis ER-α-mannosidase I (MNS3) generates an oligomannosidic N-glycan structure that is characteristically found on ER-resident glycoproteins. The enzyme itself has so far not been detected in the ER. Here, we provide evidence that in plants MNS3 exclusively resides in the Golgi apparatus at steady-state. Notably, MNS3 remains on dispersed punctate structures when subjected to different approaches that commonly result in the relocation of Golgi enzymes to the ER. Responsible for this rare behavior is an amino acid signal motif (LPYS) within the cytoplasmic tail of MNS3 that acts as a specific Golgi retention signal. This retention is a means to spatially separate MNS3 from ER-localized mannose trimming steps that generate the glycan signal required for flagging terminally misfolded glycoproteins for ERAD. The physiological importance of the very specific MNS3 localization is demonstrated here by means of a structurally impaired variant of the brassinosteroid receptor BRASSINOSTEROID INSENSITIVE 1.

Date: 2019
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DOI: 10.1038/s41467-019-11686-9

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