A signal motif retains Arabidopsis ER-α-mannosidase I in the cis-Golgi and prevents enhanced glycoprotein ERAD.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
16 08 2019
16 08 2019
Historique:
received:
11
12
2018
accepted:
01
07
2019
entrez:
18
8
2019
pubmed:
20
8
2019
medline:
18
12
2019
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31420549
doi: 10.1038/s41467-019-11686-9
pii: 10.1038/s41467-019-11686-9
pmc: PMC6697737
doi:
Substances chimiques
Arabidopsis Proteins
0
Glycoproteins
0
Plant Proteins
0
Protein Kinases
EC 2.7.-
BRI1 protein, Arabidopsis
EC 2.7.11.1
alpha-Mannosidase
EC 3.2.1.24
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3701Subventions
Organisme : Austrian Science Fund FWF
ID : P 28218
Pays : Austria
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