ArticlePlant physiology2007
In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy.
Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- The nuclear dynamic of CDC48 is affected during the immune response in plants.Plant signaling & behavior · 2025Article
- The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly.Biophysical reviews · 2023Review
- Exploring the Binding Affinity of the ARR2 GARP DNA Binding Domain via Comparative Methods.Genes · 2023Article
- Quantitative Fluorescence Resonance Energy Transfer Analysis on the Direct Interaction of Activation-2b with Histone H3/Switch-3B Protein in Arabidopsis Mesophyll Protoplasts.Journal of fluorescence · 2021Article
- A Label-free Mass Spectrometry Method to Predict Endogenous Protein Complex Composition.Molecular & cellular proteomics : MCP · 2019Article
- Controlling the Revolving and Rotating Motion Direction of Asymmetric Hexameric Nanomotor by Arginine Finger and Channel Chirality.ACS nano · 2019Review
- How to prove the existence of metabolons?Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2018Review
- Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017Review
- Review
- Discovery of a new method for potent drug development using power function of stoichiometry of homomeric biocomplexes or biological nanomotors.Expert opinion on drug delivery · 2016Article
- New approach to develop ultra-high inhibitory drug using the power function of the stoichiometry of the targeted nanomachine or biocomplex.Nanomedicine (London, England) · 2015Article
- Plasma Membranes Are Subcompartmentalized into a Plethora of Coexisting and Diverse Microdomains in Arabidopsis and Nicotiana benthamiana.The Plant cell · 2014Article
- Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation.Virology · 2013Review
- Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta.Plant physiology · 2013Article
- Control of Tobacco mosaic virus movement protein fate by CELL-DIVISION-CYCLE protein48.Plant physiology · 2012Article
- The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates the p97 ATPase and resides at the endoplasmic reticulum-golgi intermediate compartment.The Journal of biological chemistry · 2012Article
- Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF).Biochimica et biophysica acta · 2012Review
- Identification of imprinted genes subject to parent-of-origin specific expression in Arabidopsis thaliana seeds.BMC plant biology · 2011Article
- In silico and in vivo investigations of proteins of a minimized eukaryotic cytoplasm.Genome biology and evolution · 2011Article
- Dissecting the N-ethylmaleimide-sensitive factor: required elements of the N and D1 domains.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Arabidopsis (Arabidopsis thaliana) AAA ATPase CDC48A was fused to cerulean fluorescent protein and yellow fluorescent protein. AAA ATPases like CDC48 are only active in hexameric form. Förster resonance energy transfer-based fluorescence lifetime imaging microscopy using CDC48A-cerulean fluorescent protein and CDC48A-yellow fluorescent protein showed interaction between two adjacent protomers, demonstrating homo-oligomerization occurs in living plant cells. Interaction between CDC48A and the SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 (SERK1) transmembrane receptor occurs in very restricted domains at the plasma membrane. In these domains the predominant form of the fluorescently tagged CDC48A protein is a hexamer, suggesting that SERK1 is associated with the active form of CDC48A in vivo. SERK1 trans-phosphorylates CDC48A on Ser-41. Förster resonance energy transfer-fluorescence lifetime imaging microscopy was used to show that in vivo the C-terminal domains of CDC48A stay in close proximity. Employing fluorescence correlation spectroscopy, it was shown that CDC48A hexamers are part of larger complexes.
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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.