ArticleThe Journal of biological chemistry2012
Identification of a nuclear localization sequence in β-arrestin-1 and its functional implications.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 62 citations in OpenAlex.
- Monoclonal Antibody 5F1 Modulates Formyl Peptide Receptor 1 Conformation for Transmembrane Signaling.FASEB bioAdvances · 2025Article
- Neurokinin 1 receptor inhibition alleviated mitochondrial dysfunctionActa pharmaceutica Sinica. B · 2025Article
- Anti-lymphoma peptide is inspired by mapping a sequence of four amino acids of KRAI motif as nuclear localization signal of Crlz-1.Molecular therapy. Oncology · 2025Article
- Mast Cells and Mas-related G Protein-coupled Receptor X2: Itching for Novel Pathophysiological Insights to Clinical Relevance.Current allergy and asthma reports · 2024Review
- The Ubiquitination of Arrestin3 within the Nucleus Triggers the Nuclear Export of Mdm2, Which, in Turn, Mediates the Ubiquitination of GRK2 in the Cytosol.International journal of molecular sciences · 2024Article
- The multifaceted functions of β-arrestins and their therapeutic potential in neurodegenerative diseases.Experimental & molecular medicine · 2024Review
- Distinct activation mechanisms of β-arrestin-1 revealed byNature communications · 2023Article
- GPCR kinases generate an APH1A phosphorylation barcode to regulate amyloid-β generation.Cell reports · 2022Article
- Double life: How GRK2 and β-arrestin signaling participate in diseases.Cellular signalling · 2022Review
- Role of ARRB1 in prognosis and immunotherapy: A Pan-Cancer analysis.Frontiers in molecular biosciences · 2022Article
- Review
- Phosphorylation of NF-κBp65 drives inflammation-mediated hepatocellular carcinogenesis and is a novel therapeutic target.Journal of experimental & clinical cancer research : CR · 2021Article
- β-Arrestin-1 is required for adaptive β-cell mass expansion during obesity.Nature communications · 2021Article
- Key Metabolic Functions of β-Arrestins: Studies with Novel Mouse Models.Trends in endocrinology and metabolism: TEM · 2021Review
- Relevance of Peroxisome Proliferator Activated Receptors in Multitarget Paradigm Associated with the Endocannabinoid System.International journal of molecular sciences · 2021Review
- Beta-Arrestins and Receptor Signaling in the Vascular Endothelium.Biomolecules · 2020Review
- β-arrestin-1 suppresses myogenic reprogramming of brown fat to maintain euglycemia.Science advances · 2020Article
- β-arrestin1/YAP/mutant p53 complexes orchestrate the endothelin A receptor signaling in high-grade serous ovarian cancer.Nature communications · 2019Article
- New Routes in GPCR/β-Arrestin-Driven Signaling in Cancer Progression and Metastasis.Frontiers in pharmacology · 2019Review
- CCR2 Signaling Selectively Regulates IFN-α: Role of β-Arrestin 2 in IFNAR1 Internalization.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
A mounting body of evidence suggests that β-arrestin-1 plays important roles in the nucleus, but how β-arrestin-1 enters the nucleus remains unclear because no nuclear import signal has been identified in the β-arrestins. We sought to characterize the cellular localization of wild type β-arrestin-1 and a series of N domain mutants to determine the structural basis and functional implications of β-arrestin-1 nuclear localization. A seven-residue candidate nuclear localization sequence (NLS) was identified based on sequence analysis. Mutation of the NLS led to a loss of β-arrestin-1 nuclear localization in transfected cells. Exogenous expression of wild type β-arrestin-1 enhanced the transcriptional activity of nuclear factor κB (NF-κB) induced by bradykinin, whereas mutation of the NLS reduced this effect by two-thirds relative to wild type controls. Loss of β-arrestin-1 nuclear localization was accompanied by reduced recruitment of the CREB-binding protein and altered post-translational modification profile of p65/RelA. Further mutational analysis identified Lys(157) within the putative NLS as being critical to nuclear localization of β-arrestin-1. Substitution of Lys(157) to Ala led to reduced nuclear localization, decreased promoter binding by p65/RelA and decreased IL-1β gene transcription. These results demonstrate a critical role for β-arrestin-1 nuclear localization in scaffolding and transcriptional regulation.
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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.