ArticleNature communications2020
Proximity labeling proteomics reveals critical regulators for inner nuclear membrane protein degradation in plants.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.
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Who cites it
38 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.
- A common variant that alters SUN1 degradation associates with hepatic steatosis and metabolic traits in multiple cohorts.Journal of hepatology · 2023Pooled it
- Best practices for biotin ligase-based proximity labeling proteomics in plant systems.The Plant cell · 2026Review
- A redox switch on CDC48 regulates peroxisomal function via controlling peroxisome-associated protein degradation.Nature communications · 2026Article
- Application of Proximity-Labeling Techniques in Plants: A Review of Successful Cases.International journal of molecular sciences · 2026Review
- Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts.Nature communications · 2026Review
- A multiomics atlas of theScience advances · 2026Article
- Plant UBX domain-containing proteins use distinct strategies to stably engage the unfoldase CDC48A.Plant & cell physiology · 2026Article
- The Hrd1-Mediated ERAD Pathway in Plants: Conserved Principles and Plant-Specific Innovations.International journal of molecular sciences · 2026Review
- The Pea Inner Nuclear Membrane SUN Domain Protein Modulates Plant (a)biotic Stress Responses by Regulating Nuclear Dynamics.Molecular plant pathology · 2025Article
- ECLIPSE mediates selective degradation of inner nuclear membrane protein in plants.Journal of experimental botany · 2025Article
- Split-YFP-coupled interaction-dependent TurboID identifies new functions of basal cell polarity inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Proteomics revealed novel functions and drought tolerance of Arabidopsis thaliana protein kinase ATG1.BMC biology · 2025Article
- Unraveling Plant Nuclear Envelope Composition Using Proximity Labeling Proteomics.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Decoding Plant-Pathogen Interactions: A Comprehensive Exploration of Effector-Plant Transcription Factor Dynamics.Molecular plant pathology · 2025Review
- PLASMODESMATA-LOCATED PROTEIN 6 regulates plasmodesmal function in Arabidopsis vasculature.The Plant cell · 2024Article
- Recruitment of Cdc48 to chloroplasts by a UBX-domain protein in chloroplast-associated protein degradation.Nature plants · 2024Article
- Proxiome assembly of the plant nuclear pore reveals an essential hub for gene expression regulation.Nature plants · 2024Article
- Nuclear lamina component KAKU4 regulates chromatin states and transcriptional regulation in the Arabidopsis genome.BMC biology · 2024Article
- A fungal core effector exploits the OsPUX8B.2-OsCDC48-6 module to suppress plant immunity.Nature communications · 2024Article
- Profiling nuclear cysteine ligandability and effects on nuclear localization using proximity labeling-coupled chemoproteomics.Cell chemical biology · 2024Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inner nuclear membrane (INM) selectively accumulates proteins that are essential for nuclear functions; however, overaccumulation of INM proteins results in a range of rare genetic disorders. So far, little is known about how defective, mislocalized, or abnormally accumulated membrane proteins are actively removed from the INM, especially in plants and animals. Here, via analysis of a proximity-labeling proteomic profile of INM-associated proteins in Arabidopsis, we identify critical components for an INM protein degradation pathway. We show that this pathway relies on the CDC48 complex for INM protein extraction and 26S proteasome for subsequent protein degradation. Moreover, we show that CDC48 at the INM may be regulated by a subgroup of PUX proteins, which determine the substrate specificity or affect the ATPase activity of CDC48. These PUX proteins specifically associate with the nucleoskeleton underneath the INM and physically interact with CDC48 proteins to negatively regulate INM protein degradation in plants.
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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.