ArticleProceedings of the National Academy of Sciences of the United States of America2015
Unique COPII component AtSar1a/AtSec23a pair is required for the distinct function of protein ER export in Arabidopsis thaliana.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 86 citations in OpenAlex.
- SIB1-SEC23A undergo ER to chloroplast relocalization to mediate immunity in Arabidopsis thaliana.Journal of integrative plant biology · 2026Article
- Eukaryotic chaperonin coordinates root meristem activity by regulating SEC31B-dependent COPII vesicle trafficking of PIN auxin efflux carrier in Arabidopsis.Journal of integrative plant biology · 2026Article
- Interaction with COPII Member SAR1 Is Critical for the Delivery ofPlants (Basel, Switzerland) · 2026Article
- Chloroplast Stress Signals Orchestrate Epidermis-Specific Remodeling of Mitochondria and ER Under High Light.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Defender or accomplice? Dual roles of plant vesicle trafficking in restricting and enabling geminiviral systemic infection.The New phytologist · 2026Article
- Vacuolar sorting receptors coordinate lytic vacuolar and autophagic transport for plant effector-triggered immunity.Nature plants · 2025Article
- The MON1-CCZ1 complex plays dual roles in autophagic degradation and vacuolar protein transport in rice.Journal of integrative plant biology · 2025Article
- A cargo sorting receptor mediates chloroplast protein trafficking through the secretory pathway.The Plant cell · 2024Article
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- Arabidopsis Sar1b is critical for pollen tube growth.Plant molecular biology · 2024Article
- An Overview of Protein Secretion in Plant Cells.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Article
- Arabidopsis Sar1 isoforms play redundant roles in female gametophytic development.Plant reproduction · 2023Article
- A CYP78As-small grain4-coat protein complex Ⅱ pathway promotes grain size in rice.The Plant cell · 2023Article
- A deleterious Sar1c variant in rice inhibits export of seed storage proteins from the endoplasmic reticulum.Plant molecular biology · 2023Article
- CRISPR-Cas-mediated unfolded protein response control for enhancing plant stress resistance.Frontiers in plant science · 2023Review
- Protein Analysis ofNanomaterials (Basel, Switzerland) · 2022Article
- Conserved exchange of paralog proteins during neuronal differentiation.Life science alliance · 2022Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- COPII Sec23 proteins form isoform-specific endoplasmic reticulum exit sites with differential effects on polarized growth.The Plant cell · 2022Article
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Secretory proteins traffic from endoplasmic reticulum (ER) to Golgi via the coat protein complex II (COPII) vesicle, which consists of five cytosolic components (Sar1, Sec23-24, and Sec13-31). In eukaryotes, COPII transport has diversified due to gene duplication, creating multiple COPII paralogs. Evidence has accumulated, revealing the functional heterogeneity of COPII paralogs in protein ER export. Sar1B, the small GTPase of COPII machinery, seems to be specialized for large cargo secretion in mammals. Arabidopsis contains five Sar1 and seven Sec23 homologs, and AtSar1a was previously shown to exhibit different effects on α-amylase secretion. However, mechanisms underlying the functional diversity of Sar1 paralogs remain unclear in higher organisms. Here, we show that the Arabidopsis Sar1 homolog AtSar1a exhibits distinct localization in plant cells. Transgenic Arabidopsis plants expressing dominant-negative AtSar1a exhibit distinct effects on ER cargo export. Mutagenesis analysis identified a single amino acid, Cys84, as being responsible for the functional diversity of AtSar1a. Structure homology modeling and interaction studies revealed that Cys84 is crucial for the specific interaction of AtSar1a with AtSec23a, a distinct Arabidopsis Sec23 homolog. Structure modeling and coimmunoprecipitation further identified a corresponding amino acid, Cys484, on AtSec23a as being essential for the specific pair formation. At the cellular level, the Cys484 mutation affects the distinct function of AtSec23a on vacuolar cargo trafficking. Additionally, dominant-negative AtSar1a affects the ER export of the transcription factor bZIP28 under ER stress. We have demonstrated a unique plant pair of COPII machinery function in ER export and the mechanism underlying the functional diversity of COPII paralogs in eukaryotes.
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