ArticleThe Journal of biological chemistry2008
Thyroid hormone receptor alpha1 follows a cooperative CRM1/calreticulin-mediated nuclear export pathway.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- Let go or retain: role of calmodulin in orchestrating nuclear protein transport in eukaryotes.Plant cell reports · 2026Review
- Nuclear receptor corepressor 1 levels differentially impact the intracellular dynamics of mutant thyroid hormone receptors associated with resistance to thyroid hormone syndrome.Molecular and cellular endocrinology · 2024Article
- SIRT1 activation synergizes with FXR agonism in hepatoprotectionActa pharmaceutica Sinica. B · 2023Article
- HIF-1-regulated expression of calreticulin promotes breast tumorigenesis and progression through Wnt/β-catenin pathway activation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Transportin-2 plays a critical role in nucleocytoplasmic shuttling of oestrogen receptor-α.Scientific reports · 2020Article
- Mediator subunit MED1 modulates intranuclear dynamics of the thyroid hormone receptor.Journal of cellular biochemistry · 2020Article
- α-Synuclein Translocates to the Nucleus to Activate Retinoic-Acid-Dependent Gene Transcription.iScience · 2020Article
- Mislocalization of Cancer-associated Thyroid Hormone Receptor Mutants.Nuclear receptor research · 2020Article
- Targeting XPO1 and PAK4 in 8505C Anaplastic Thyroid Cancer Cells: Putative Implications for Overcoming Lenvatinib Therapy Resistance.International journal of molecular sciences · 2019Article
- Acetylation modulates thyroid hormone receptor intracellular localization and intranuclear mobility.Molecular and cellular endocrinology · 2019Article
- High content screen for identifying small-molecule LC3B-localization modulators in a renal cancer cell line.Scientific data · 2018Article
- Thyroid hormone receptor localization in target tissues.The Journal of endocrinology · 2018Review
- Expanded polyalanine tracts function as nuclear export signals and promote protein mislocalization via eEF1A1 factor.The Journal of biological chemistry · 2017Article
- Nuclear Import of Hepatitis B Virus Capsids and Genome.Viruses · 2017Review
- Nuclear import of the thyroid hormone receptor α1 is mediated by importin 7, importin β1, and adaptor importin α1.Molecular and cellular endocrinology · 2016Article
- Multiple exportins influence thyroid hormone receptor localization.Molecular and cellular endocrinology · 2015Article
- Components and regulation of nuclear transport processes.The FEBS journal · 2015Review
- Multiple novel signals mediate thyroid hormone receptor nuclear import and export.The Journal of biological chemistry · 2012Article
- Move or die: the fate of the Tax oncoprotein of HTLV-1.Viruses · 2011Review
- Heterokaryon technique for analysis of cell type-specific localization.Journal of visualized experiments : JoVE · 2011Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The thyroid hormone receptor alpha1 (TRalpha) exhibits a dual role as an activator or repressor of its target genes in response to thyroid hormone (T(3)). Previously, we have shown that TRalpha, formerly thought to reside solely in the nucleus bound to DNA, actually shuttles rapidly between the nucleus and cytoplasm. An important aspect of the shuttling activity of TRalpha is its ability to exit the nucleus through the nuclear pore complex. TRalpha export is not sensitive to treatment with the CRM1-specific inhibitor leptomycin B (LMB) in heterokaryon assays, suggesting a role for an export receptor other than CRM1. Here, we have used a combined approach of in vivo fluorescence recovery after photobleaching experiments, in vitro permeabilized cell nuclear export assays, and glutathione S-transferase pull-down assays to investigate the export pathway used by TRalpha. We show that, in addition to shuttling in heterokaryons, TRalpha shuttles rapidly in an unfused monokaryon system as well. Furthermore, our data show that TRalpha directly interacts with calreticulin, and point to the intriguing possibility that TRalpha follows a cooperative export pathway in which both calreticulin and CRM1 play a role in facilitating efficient translocation of TRalpha from the nucleus to cytoplasm.
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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.