ArticleMolecular biology of the cell2000
AtVPS45 complex formation at the trans-Golgi network.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 157 citations in OpenAlex.
- Cargo Sorting Zones in Plant Trans-Golgi Network.Sub-cellular biochemistry · 2026Review
- VPS45 is required for both diffuse and tip growth ofFrontiers in plant science · 2023Article
- The EXO70 inhibitor Endosidin2 alters plasma membrane protein composition in Arabidopsis roots.Frontiers in plant science · 2023Article
- Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components.The Plant cell · 2022Article
- RAB GTPases and SNAREs at the trans-Golgi network in plants.Journal of plant research · 2022Review
- Super resolution live imaging: The key for unveiling the true dynamics of membrane traffic around the Golgi apparatus in plant cells.Frontiers in plant science · 2022Review
- The sorting of cargo proteins in the plantFrontiers in plant science · 2022Review
- MAG2 and MAL Regulate Vesicle Trafficking and Auxin Homeostasis With Functional Redundancy.Frontiers in plant science · 2022Article
- Sphingolipids mediate polar sorting of PIN2 through phosphoinositide consumption at the trans-Golgi network.Nature communications · 2021Article
- Actin and Microtubules Differently Contribute to Vacuolar Targeting Specificity during the Export from the ER.Membranes · 2021Article
- Cargo sorting zones in the trans-Golgi network visualized by super-resolution confocal live imaging microscopy in plants.Nature communications · 2021Article
- Organelle Visualization With Multicolored Fluorescent Markers in Bamboo.Frontiers in plant science · 2021Article
- PI4KIIIβ is a therapeutic target in chromosome 1q-amplified lung adenocarcinoma.Science translational medicine · 2020Article
- Differentiation of Trafficking Pathways at Golgi Entry Core Compartments and Post-Golgi Subdomains.Frontiers in plant science · 2020Review
- Vesicle Transport in Plants: A Revised Phylogeny of SNARE Proteins.Evolutionary bioinformatics online · 2020Article
- Functional diversification ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Lipids at the crossroad: Shaping biological membranes heterogeneity defines trafficking pathways.PLoS biology · 2018Article
- The Plant Trans-Golgi Network: Not Just a Matter of Distinction.Plant physiology · 2018Review
- SCYL2 Genes Are Involved in Clathrin-Mediated Vesicle Trafficking and Essential for Plant Growth.Plant physiology · 2017Article
- Localization of Arabidopsis FORKED1 to a RABA-positive compartment suggests a role in secretion.Journal of experimental botany · 2017Article
16 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Sec1p family of proteins are thought to be involved in the regulation of vesicle fusion reactions through interaction with t-SNAREs (target soluble N-ethylmaleimide-sensitive factor attachment protein receptors) at the target membrane. AtVPS45 is a member of this family from Arabidopsis thaliana that we now demonstrate to be present on the trans-Golgi network (TGN), where it colocalizes with the vacuolar cargo receptor AtELP. Unlike yeast Vps45p, AtVPS45 does not interact with, or colocalize with, the prevacuolar t-SNARE AtPEP12. Instead, AtVPS45 interacts with two t-SNAREs, AtTLG2a and AtTLG2b, that show similarity to the yeast t-SNARE Tlg2p. AtTLG2a and -b each colocalize with AtVPS45 at the TGN; however, AtTLG2a is in a different region of the TGN than AtTLG2b by immunogold electron microscopy. Therefore, we propose that complexes containing AtVPS45 and either AtTLG2a or -b define functional subdomains of the TGN and may be required for different trafficking events. Among other Arabidopsis SNAREs, AtVPS45 antibodies preferentially coprecipitate AtVTI1b over the closely related isoform AtVTI1a, implying that AtVTI1a and AtVTI1b also have distinct functions within the cell. These data point to a functional complexity within the plant secretory pathway, where proteins encoded by gene families have specialized functions, rather than functional redundancy.
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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.