English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance The underlying mechanisms causing the functional diversity of small GTPase Sar1 paralogs in coat protein complex II-mediated protein endoplasmic reticulum (ER) export remain elusive in higher organisms.Arabidopsis contains five Sar1 homologs. In this study, we show that AtSar1a exhibits a distinct localization and effects on ER cargo export in plants through a unique interaction with the COPII coat protein AtSec23a. This specific pairing is required for the distinct function in ER export under ER stress inArabidopsis . Our results point to a mechanism underlying the functional diversity of COPII paralogs in eukaryotes.

Unique COPII component AtSar1a/AtSec23a pair is required for the distinct function of protein ER export in Arabidopsis thaliana