ArticleJournal of experimental botany2012
Coupled transport of Arabidopsis p24 proteins at the ER-Golgi interface.
Article in Journal of experimental botany, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- TMED9 coordinates the clearance of misfolded GPI-anchored proteins out of the ER and into the Golgi.PLoS biology · 2025Article
- p24-Tango1 interactions ensure ER-Golgi interface stability and efficient transport.The Journal of cell biology · 2024Article
- An Overview of Protein Secretion in Plant Cells.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Genome-Wide Analysis of theInternational journal of molecular sciences · 2022Article
- Expression of TMED3 is independently associated with colorectal cancer prognosis.Experimental and therapeutic medicine · 2022Article
- Differential Involvement ofCells · 2022Article
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- Characterization ofFrontiers in plant science · 2022Article
- High-quality reference genome of Fasciola gigantica: Insights into the genomic signatures of transposon-mediated evolution and specific parasitic adaption in tropical regions.PLoS neglected tropical diseases · 2021Article
- p24 Family Proteins Are Involved in Transport to the Plasma Membrane of GPI-Anchored Proteins in Plants.Plant physiology · 2020Article
- Cell-surface receptors enable perception of extracellular cytokinins.Nature communications · 2020Article
- Cytokinin fluoroprobe reveals multiple sites of cytokinin perception at plasma membrane and endoplasmic reticulum.Nature communications · 2020Article
- Transmembrane emp24 domain proteins in development and disease.Genetics research · 2019Review
- RAB21 interacts with TMED10 and modulates its localization and abundance.Biology open · 2019Article
- Subcellular Localization of Arabidopsis Pathogenesis-Related 1 (PR1) Protein.International journal of molecular sciences · 2017Article
- α2-COP is involved in early secretory traffic in Arabidopsis and is required for plant growth.Journal of experimental botany · 2017Article
- Sorting Motifs Involved in the Trafficking and Localization of the PIN1 Auxin Efflux Carrier.Plant physiology · 2016Article
- p24 family proteins: key players in the regulation of trafficking along the secretory pathway.Protoplasma · 2016Review
- Isoform-selective oligomer formation of Saccharomyces cerevisiae p24 family proteins.The Journal of biological chemistry · 2013Article
- Putative p24 complexes in Arabidopsis contain members of the delta and beta subfamilies and cycle in the early secretory pathway.Journal of experimental botany · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies. It has previously been shown that transiently expressed red fluorescent protein (RFP)-p24δ5 localizes to the endoplasmic reticulum (ER) as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. Using specific antibodies, endogenous p24δ5 has now been localized to the ER and p24β2 to the Golgi apparatus in Arabidopsis root tip cells by immunogold electron microscopy. The relative contributions of the cytosolic tail and the luminal domains to p24δ5 trafficking have also been characterized. It is demonstrated that whereas the dilysine motif in the cytoplasmic tail determines the location of p24δ5 in the early secretory pathway, the luminal domain may contribute to its distribution downstream of the Golgi apparatus. By using knock-out mutants and co-immunoprecipitation experiments, it is shown that p24δ5 and p24β2 interact with each other. Finally, it is shown that p24δ5 and p24β2 exhibit coupled trafficking at the ER-Golgi interface. It is proposed that p24δ5 and p24β2 interact with each other at ER export sites for ER exit and coupled transport to the Golgi apparatus. Once in the Golgi, p24δ5 interacts very efficiently with the COPI machinery for retrograde transport back to the ER.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.