ArticleMolecular biology of the cell2010
Scyl1 facilitates nuclear tRNA export in mammalian cells by acting at the nuclear pore complex.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Bioinformatic Analyses of the Ataxin-2 Family Since Algae Emphasize Its Small Isoforms, Large Chimerisms, and the Importance of Human Exon 1B as Target of Therapies to Prevent Neurodegeneration.International journal of molecular sciences · 2026Article
- SCYL1 deficiency in CALFAN syndrome is associated with ER stress and cell death.Disease models & mechanisms · 2025Article
- Disorders of vesicular trafficking presenting with recurrent acute liver failure: NBAS, RINT1, and SCYL1 deficiency.Journal of inherited metabolic disease · 2025Review
- Recurrent Acute Liver Failure in a Bahraini Child With a Novel Mutation of Spinocerebellar Ataxia-21.Cureus · 2023Article
- Overexpression of SCYL1 Is Associated with Progression of Breast Cancer.Current oncology (Toronto, Ont.) · 2022Article
- Lipid Dyshomeostasis and Inherited Cerebellar Ataxia.Molecular neurobiology · 2022Review
- Karyopherin abnormalities in neurodegenerative proteinopathies.Brain : a journal of neurology · 2021Review
- Diversity roles of CHD1L in normal cell function and tumorigenesis.Biomarker research · 2021Review
- SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis.Molecular biology of the cell · 2020Article
- Slo2 potassium channel function depends on RNA editing-regulated expression of a SCYL1 protein.eLife · 2020Article
- Recurrent acute liver failure associated with novelWorld journal of clinical cases · 2019Article
- Overlapping Role of SCYL1 and SCYL3 in Maintaining Motor Neuron Viability.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Article
- Classification of Genes: Standardized Clinical Validity Assessment of Gene-Disease Associations Aids Diagnostic Exome Analysis and Reclassifications.Human mutation · 2017Article
- SCYL pseudokinases in neuronal function and survival.Neural regeneration research · 2016Review
- Disruptive SCYL1 Mutations Underlie a Syndrome Characterized by Recurrent Episodes of Liver Failure, Peripheral Neuropathy, Cerebellar Atrophy, and Ataxia.American journal of human genetics · 2015Article
- Overexpression of N-terminal kinase like gene promotes tumorigenicity of hepatocellular carcinoma by regulating cell cycle progression and cell motility.Oncotarget · 2015Article
- Protein kinase A is part of a mechanism that regulates nuclear reimport of the nuclear tRNA export receptors Los1p and Msn5p.Eukaryotic cell · 2014Article
- Crystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasm.Nucleic acids research · 2013Article
- An early onset progressive motor neuron disorder in Scyl1-deficient mice is associated with mislocalization of TDP-43.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Scyl1 is an evolutionarily conserved N-terminal protein kinase-like domain protein that plays a role in COP1-mediated retrograde protein trafficking in mammalian cells. Furthermore, loss of Scyl1 function has been shown to result in neurodegenerative disorders in mice. Here, we report that Scyl1 is also a cytoplasmic component of the mammalian nuclear tRNA export machinery. Like exportin-t, overexpression of Scyl1 restored export of a nuclear export-defective serine amber suppressor tRNA mutant in COS-7 cells. Scyl1 binds tRNA saturably, and associates with the nuclear pore complex by interacting, in part, with Nup98. Scyl1 copurifies with the nuclear tRNA export receptors exportin-t and exportin-5, the RanGTPase, and the eukaryotic elongation factor eEF-1A, which transports aminoacyl-tRNAs to the ribosomes. Scyl1 interacts directly with exportin-t and RanGTP but not with eEF-1A or RanGDP in vitro. Moreover, exportin-t containing tRNA, Scyl1, and RanGTP form a quaternary complex in vitro. Biochemical characterization also suggests that the nuclear aminoacylation-dependent pathway is primarily responsible for tRNA export in mammalian cells. These findings together suggest that Scyl1 participates in the nuclear aminoacylation-dependent tRNA export pathway and may unload aminoacyl-tRNAs from the nuclear tRNA export receptor at the cytoplasmic side of the nuclear pore complex and channels them to eEF-1A.
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