COPII Paralogs in Plants: Functional Redundancy or Diversity?

Trends Plant Sci

Centre for Cell and Developmental Biology and State Key Laboratory of Agrobiotechnology, School of Life Sciences, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong SAR, China. Electronic address:

Published: September 2016

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.

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.tplants.2016.05.010DOI Listing

Publication Analysis

Top Keywords

copii vesicles
8
functional diversity
8
copii subunit
8
subunit isoforms
8
copii
6
copii paralogs
4
paralogs plants
4
plants functional
4
functional redundancy
4
redundancy diversity?
4

Similar Publications

Multifunctional Roles of Sec13 Paralogues in the Euglenozoan .

bioRxiv

December 2024

Department of Microbiology and Immunology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, 955 Main Street, Buffalo NY 14203.

Secretory cargos are exported from the ER via COPII coated vesicles that have an inner matrix of Sec23/Sec24 heterotetramers and an outer cage of Sec13/Sec31 heterotetramers. In addition to COPII, Sec13 is part of the nuclear pore complex (NPC) and the regulatory SEA/GATOR complex in eukaryotes, which typically have one Sec13 orthologue. The kinetoplastid parasite has two paralogues: TbSec13.

View Article and Find Full Text PDF

Protein secretion is an essential process that drives cell growth and communication. Enrichment of soluble secretory proteins into ER-derived transport carriers occurs via transmembrane cargo receptors that connect lumenal cargo to the cytosolic COPII coat. Here, we find that the cargo receptor, SURF4, recruits different SEC24 cargo adaptor paralogs of the COPII coat to export different cargoes.

View Article and Find Full Text PDF

TMEM39A and TMEM131 facilitate bulk transport of ECM proteins through large COPII vesicle formation.

J Genet Genomics

November 2024

Cancer Metastasis Branch, Research Institute, National Cancer Center, 323 Ilsan-ro, Goyang-si, Gyeonggi-do, 10408, Republic of Korea. Electronic address:

The growth of Caenorhabditis elegans involves multiple molting processes, during which old cuticles are shed and new cuticles are rapidly formed. This process requires the regulated bulk secretion of cuticle components. The transmembrane protein-39 (TMEM-39) mutant exhibits distinct dumpy and ruptured phenotypes characterized by notably thin cuticles.

View Article and Find Full Text PDF

Cryo-electron tomography reveals how COPII assembles on cargo-containing membranes.

Nat Struct Mol Biol

November 2024

Institute of Structural and Molecular Biology, Birkbeck College, London, UK.

Proteins traverse the eukaryotic secretory pathway through membrane trafficking between organelles. The coat protein complex II (COPII) mediates the anterograde transport of newly synthesized proteins from the endoplasmic reticulum, engaging cargoes with a wide range of size and biophysical properties. The native architecture of the COPII coat and how cargo might influence COPII carrier morphology remain poorly understood.

View Article and Find Full Text PDF

Thrombopoietin (TPO) is a plasma glycoprotein that binds its receptor on megakaryocytes (MKs) and MK progenitors, resulting in enhanced platelet production. The mechanism by which TPO is secreted from hepatocytes remains poorly understood. Lectin mannose-binding 1 (LMAN1) and multiple coagulation factor deficiency 2 (MCFD2) form a complex at the endoplasmic reticulum membrane, recruiting cargo proteins into COPII vesicles for secretion.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!