ArticlePlant physiology2005
Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 308 papers.
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Who cites it
308 citing papers in PubMed, 600 citations in OpenAlex.
- Pepper RING-type E3 ligase, CaANKR1, negatively regulates drought tolerance by modulating CaMAPK1 stability.The Plant journal : for cell and molecular biology · 2026Article
- Ubiquitination plays a key role in an insecticide resistance fitness cost.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- RING-type E3 ligase RhSAREL promotes flower senescence by differentially regulating two TMBIM family members, RhTMBIM1 and RhTMBIM7, in Rosa hybrida.Plant physiology · 2026Article
- Identification of the RING-HCa E3 Ligase Gene Family and Functional Characterization ofCurrent issues in molecular biology · 2026Article
- The feedback regulation between DREB2C and E3 ligases DEL1/DEL2 for balancing the initial growth and ABA signaling in Arabidopsis.The New phytologist · 2026Article
- Comprehensive genome-wide analysis of DUF668 gene family in potato reveals roles in growth and stress responses.Journal of applied genetics · 2026Article
- Article
- Genetic Mapping and Functional Characterisation of GhCUP Regulating Leaf Curling in Cotton.Plant biotechnology journal · 2026Article
- Review
- Genome-wide identification and expression analysis of RBR-type ubiquitin ligase family genes reveal the role of ZmIBR10 in maize disease resistance.BMC plant biology · 2026Article
- Genome-wide identification and immunological expression analysis of the C3HC4-type zinc finger protein genes in the silkworm, Bombyx Mori.BMC genomics · 2026Article
- The transcription factor ANAC017 links mitochondrial retrograde signaling with the ubiquitin-proteasome system to control mitochondrial function in Arabidopsis.Plant communications · 2026Article
- Ubiquitin-Mediated Proteolysis as a Regulator of the Plant Defense-Growth Balance.Plants (Basel, Switzerland) · 2026Review
- Genome-wide identification and analysis ofFrontiers in plant science · 2026Article
- Genome-wide association study identifies candidate genes associated with leaf morphological traits in grape (Frontiers in plant science · 2026Article
- Heterologous expression of soybean E3 ubiquitin ligase Glycine max Ring Zinc Finger 1-Like 1 (GmRZFL1) negatively responds to osmotic stress by participating in the abscisic acid signaling pathway in Arabidopsis.BMC plant biology · 2025Article
- A genetic screen identifies the E3 ubiquitin ligase MPSR1 as a suppressor of early flowering of the sensitivity to red light reduced 1 mutant.Scientific reports · 2025Article
- RING-Between-RING-Type E3 Ligase Ariadne-Like Protein 8 Negatively Regulates Plant Virus Infection by Targeting a Viral Movement Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Rice RING E3 Ligase OsRMT1 Negatively Regulates Salt Tolerance by Degrading the Canonical Salt-Responsive Protein OsMBL1.Plant biotechnology journal · 2025Article
- Genome-Wide Identification and Expression Analysis of thePlants (Basel, Switzerland) · 2025Article
248 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Approximately 5% of the Arabidopsis (Arabidopsis thaliana) proteome is predicted to be involved in the ubiquitination/26S proteasome pathway. The majority of these predicted proteins have identity to conserved domains found in E3 ligases, of which there are multiple types. The RING-type E3 is characterized by the presence of a cysteine-rich domain that coordinates two zinc atoms. Database searches followed by extensive manual curation identified 469 predicted Arabidopsis RING domain-containing proteins. In addition to the two canonical RING types (C3H2C3 or C3HC4), additional types of modified RING domains, named RING-v, RING-D, RING-S/T, RING-G, and RING-C2, were identified. The modified RINGs differ in either the spacing between metal ligands or have substitutions at one or more of the metal ligand positions. The majority of the canonical and modified RING domain-containing proteins analyzed were active in in vitro ubiquitination assays, catalyzing polyubiquitination with the E2 AtUBC8. To help identity regions of the proteins that may interact with substrates, domain analyses of the amino acids outside the RING domain classified RING proteins into 30 different groups. Several characterized protein-protein interaction domains were identified, as well as additional conserved domains not described previously. The two largest classes of RING proteins contain either no identifiable domain or a transmembrane domain. The presence of such a large and diverse number of RING domain-containing proteins that function as ubiquitin E3 ligases suggests that target-specific proteolysis by these E3 ligases is a complex and important part of cellular regulation in Arabidopsis.
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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.