N-linked glycosylation of AtVSR1 is important for vacuolar protein sorting in Arabidopsis.
Plant J
; 80(6): 977-92, 2014 Dec.
Article
in En
| MEDLINE
| ID: mdl-25293377
ABSTRACT
Vacuolar sorting receptors (VSRs) in Arabidopsis mediate the sorting of soluble proteins to vacuoles in the secretory pathway. The VSRs are post-translationally modified by the attachment of N-glycans, but the functional significance of such a modification remains unknown. Here we have studied the role(s) of glycosylation in the stability, trafficking and vacuolar protein transport of AtVSR1 in Arabidopsis protoplasts. AtVSR1 harbors three complex-type N-glycans, which are located in the N-terminal 'PA domain', the central region and the C-terminal epidermal growth factor repeat domain, respectively. We have demonstrated that (i) the N-glycans do not affect the targeting of AtVSR1 to pre-vacuolar compartments (PVCs) and its vacuolar degradation; and (ii) N-glycosylation alters the binding affinity of AtVSR1 to cargo proteins and affects the transport of cargo into the vacuole. Hence, N-glycosylation of AtVSR1 plays a critical role in its function as a VSR in plants.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Vacuoles
/
Arabidopsis
/
Arabidopsis Proteins
Language:
En
Journal:
Plant J
Journal subject:
BIOLOGIA MOLECULAR
/
BOTANICA
Year:
2014
Document type:
Article
Affiliation country:
China