ArticleJournal of biomedical science2017
Adducin family proteins possess different nuclear export potentials.
Article in Journal of biomedical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.
- The correlation between rs2501577 gene polymorphism and biliary atresia: a systematic review and meta-analysis.Pediatric surgery international · 2023Pooled it
- Identification of diagnostic biomarkers and immune cell profiles associated with COPD integrated bioinformatics and machine learning.Journal of cellular and molecular medicine · 2024Article
- Proteomic characterization identifies clinically relevant subgroups of soft tissue sarcoma.Nature communications · 2024Article
- Article
- Single-cell transcriptomics reveals intestinal cell heterogeneity and identifies Ep300 as a potential therapeutic target in mice with acute liver failure.Cell discovery · 2023Article
- Cathepsin B S-nitrosylation promotes ADAR1-mediated editing of its own mRNA transcript via an ADD1/MATR3 regulatory axis.Cell research · 2023Article
- Lack of adducin impairs the stability of endothelial adherens and tight junctions and may be required for cAMP-Rac1-mediated endothelial barrier stabilization.Scientific reports · 2022Article
- A serotonergic axon-cilium synapse drives nuclear signaling to alter chromatin accessibility.Cell · 2022Article
- The accelerated aging model reveals critical mechanisms of late-onset Parkinson's disease.BioData mining · 2020Article
- Adducins inhibit lung cancer cell migration through mechanisms involving regulation of cell-matrix adhesion and cadherin-11 expression.Biochimica et biophysica acta. Molecular cell research · 2019Article
- A Review on Adducin from Functional to Pathological Mechanisms: Future Direction in Cancer.BioMed research international · 2018Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe adducin (ADD) family proteins, namely ADD1, ADD2, and ADD3, are actin-binding proteins that play important roles in the stabilization of membrane cytoskeleton and cell-cell junctions. All the ADD proteins contain a highly conserved bipartite nuclear localization signal (NLS) at the carboxyl termini, but only ADD1 can localize to the nucleus. The reason for this discrepancy is not clear.
methodsTo avoid the potential effect of cell-cell junctions on the distribution of ADD proteins, HA epitope-tagged ADD proteins and mutants were transiently expressed in NIH3T3 fibroblasts and their distribution in the cytoplasm and nucleus was examined by immunofluorescence staining. Several nuclear proteins were identified to interact with ADD1 by mass spectrometry, which were further verified by co-immunoprecipitation.
resultsIn this study, we found that ADD1 was detectable both in the cytoplasm and nucleus, whereas ADD2 and ADD3 were detected only in the cytoplasm. However, ADD2 and ADD3 were partially (~40%) sequestered in the nucleus by leptomycin B, a CRM1/exportin1 inhibitor. Upon the removal of leptomycin B, ADD2 and ADD3 re-distributed to the cytoplasm. These results indicate that ADD2 and ADD3 possess functional NLS and are quickly transported to the cytoplasm upon entering the nucleus. Indeed, we found that ADD2 and ADD3 possess much higher potential to counteract the activity of the NLS derived from Simian virus 40 large T-antigen than ADD1. All the ADD proteins appear to contain multiple nuclear export signals mainly in their head and neck domains. However, except for the leucine-rich motif (
conclusionsOur results suggest that ADD2 and ADD3 possess functional NLS and shuttle between the cytoplasm and nucleus. The discrepancy in the subcellular localization of the ADD isoforms arises due to their different nuclear export capabilities. In addition, the interaction of ADD1 with RNA polymerase II and zinc-finger protein 331 implicates a potential role for ADD1 in the regulation of transcription.
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