Proceedings of the National Academy of Sciences of the United States of America, 117(15), 8503-8514 (2020-04-03)
The specific interaction of importins with nuclear localization signals (NLSs) of cargo proteins not only mediates nuclear import but also, prevents their aberrant phase separation and stress granule recruitment in the cytoplasm. The importin Transportin-1 (TNPO1) plays a key role...
The non-classical nuclear import carrier Transportin 1 modulates circadian rhythms through its effect on PER1 nuclear localization
Korge S, et al.
PLoS Genetics, 14(1), e1007189-e1007189 (2018)
Genome-wide genetic aberrations of thymoma using cDNA microarray based comparative genomic hybridization
The Journal of biological chemistry, 290(29), 17967-17984 (2015-06-11)
Activation of IκB kinase (IKK) and NF-κB by genotoxic stresses modulates apoptotic responses and production of inflammatory mediators, thereby contributing to therapy resistance and premature aging. We previously reported that genotoxic agents induce nuclear localization of NF-κB essential modulator (NEMO)...
The Journal of cell biology, 138(6), 1181-1192 (1997-09-23)
Heterogeneous nuclear ribonucleoprotein (hnRNP) A1 is an abundant nuclear protein that plays an important role in pre-mRNA processing and mRNA export from the nucleus. A1 shuttles rapidly between the nucleus and the cytoplasm, and a 38-amino acid domain, M9, serves...
microRNA miR-128 represses LINE-1 retrotransposition by downregulating the nuclear import factor TNPO1
Idica A, et al.
The Journal of Biological Chemistry, 28(1), jbc-M117 (2017)
IPO3 mediated nonclassical nuclear import of NEMO drives DNA damage-dependent NF-kappaB activation
Hwang B, et al.
The Journal of Biological Chemistry, jbc-M115 (2015)
Nuclear import receptors, also called importins, mediate nuclear import of proteins and chaperone aggregation-prone cargoes (e.g., neurodegeneration-linked RNA-binding proteins [RBPs]) in the cytoplasm. Importins were identified as modulators of cellular toxicity elicited by arginine-rich dipeptide repeat proteins (DPRs), an aberrant...
Transcriptional regulation of importin-alpha1 by JunD modulates subcellular localization of RNA-binding protein HuR in intestinal epithelial cells
Xu Y, et al.
American Journal of Physiology. Cell Physiology, 311(6), C874-C883 (2016)
Structural basis for substrate recognition and dissociation by human transportin 1
The primarily nuclear RNA-binding protein FUS (fused in sarcoma) forms pathological cytoplasmic inclusions in a subset of early-onset amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) patients. In response to cellular stress, FUS is recruited to cytoplasmic stress granules, which...
FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS
Human DICER1 protein cleaves double-stranded RNA into small sizes, a crucial step in production of single-stranded RNAs which are mediating factors of cytoplasmic RNA interference. Here, we clearly demonstrate that human DICER1 protein localizes not only to the cytoplasm but...
American journal of physiology. Cell physiology, 311(6), C874-C883 (2016-10-14)
The RNA-binding protein HuR is crucial for normal intestinal mucosal regeneration by modulating the stability and translation of target mRNAs, but the exact mechanism underlying HuR trafficking between the cytoplasm and nucleus remains largely unknown. Here we report a novel...
Molecular biology of the cell, 20(18), 4043-4058 (2009-07-31)
Mitosis in higher eukaryotes is marked by the sequential assembly of two massive structures: the mitotic spindle and the nucleus. Nuclear assembly itself requires the precise formation of both nuclear membranes and nuclear pore complexes. Previously, importin alpha/beta and RanGTP...
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