نتایج جستجو برای: nucleocytoplasmic shuttling

تعداد نتایج: 4663  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2004
Stephan Güttinger Petra Mühlhäusser Roland Koller-Eichhorn Julius Brennecke Ulrike Kutay

The RanGTP-binding nuclear transport receptors transportin1 (TRN1) and transportin2 (TRN2) are highly similar in sequence but are reported to function in nuclear import and export, respectively. Here we show that TRN2 possesses properties of a nuclear import receptor. TRN1/2 both interacted with a similar set of RNA-binding proteins in a RanGTP-sensitive manner. TRN2 bound RanGTP with high affi...

2014
Heehyoung Lee Anne Schroeder Brian Armstrong Claudia Kowolik Marcin Kortylewski Hua Yu

Nucleocytoplasmic shuttling of signaling molecules is crucial for regulating their activity. Regulation of signal transducer and activator of transcription 3 (STAT3) is critical for normal physiology while STAT3 dysregulation underlies many diseases such as cancer. However, the mechanism(s) underlying STAT3 nuclear egress remains unclear. Here, we show that exportin 7 is critical for STAT3 nucl...

Journal: :International Journal of Molecular Sciences 2018

Journal: :Molecular and cellular biology 2002
Angela Iervolino Giorgia Santilli Rossana Trotta Clara Guerzoni Vincenzo Cesi Anna Bergamaschi Carlo Gambacorti-Passerini Bruno Calabretta Danilo Perrotti

hnRNP A1 is a nucleocytoplasmic shuttling heterogeneous nuclear ribonucleoprotein that accompanies eukaryotic mRNAs from the active site of transcription to that of translation. Although the importance of hnRNP A1 as a regulator of nuclear pre-mRNA and mRNA processing and export is well established, it is unknown whether this is relevant for the control of proliferation, survival, and different...

Journal: :The Journal of Cell Biology 2003
Frederic Kendirgi Dianne M. Barry Eric R. Griffis Maureen A. Powers Susan R. Wente

Gle1 is required for mRNA export in yeast and human cells. Here, we report that two human Gle1 (hGle1) isoforms are expressed in HeLa cells (hGle1A and B). The two encoded proteins are identical except for their COOH-terminal regions. hGle1A ends with a unique four-amino acid segment, whereas hGle1B has a COOH-terminal 43-amino acid span. Only hGle1B, the more abundant isoform, localizes to the...

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