Journal
TRENDS IN PLANT SCIENCE
Volume 21, Issue 9, Pages 758-769Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tplants.2016.05.010
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Funding
- Research Grants Council of Hong Kong [CUHK466011, 465112, 466613, CUHK2/CRF/11G, C4011-14R, AoE/M-05/12]
- NSFC/RGC [N_CUHK406/12]
- National Natural Science Foundation of China [31270226, 31470294]
- Chinese Academy of Sciences-Croucher Funding Scheme for Joint Laboratories
- Shenzhen Peacock Project [KQTD201101]
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In eukaryotes, the best-described mechanism of endoplasmic reticulum (ER) export is mediated by coat protein complex II (COPII) vesicles, which comprise five conserved cytosolic components [secretion-associated, Ras-related protein 1 (Sar1), Sec23-24, and Sec13-31]. In higher organisms, multiple paralogs of COPII components are created due to gene duplication. However, the functional diversity of plant COPII subunit isoforms remains largely elusive. Here we summarize and discuss the latest findings derived from studies of various arabidopsis COPII subunit isoforms and their functional diversity. We also put forward testable hypotheses on distinct populations of COPII vesicles performing unique functions in ER export in developmental and stress-related pathways in plants.
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