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Open AccessJournal ArticleDOI

TAP, the Human Homolog of Mex67p, Mediates CTE-Dependent RNA Export from the Nucleus

TLDR
TAP, like its yeast homolog Mex67p, is a bona fide mRNA nuclear export mediator and is the second cellular RNA binding protein shown to be directly involved in the export of its target RNA.
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This article is published in Molecular Cell.The article was published on 1998-04-01 and is currently open access. It has received 572 citations till now. The article focuses on the topics: NXF1 & Nuclear export signal.

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Citations
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Mechanisms of Alternative Pre-Messenger RNA Splicing

TL;DR: This review describes what is currently known of the molecular mechanisms that control changes in splice site choice and starts with the best-characterized systems from the Drosophila sex determination pathway, and then describes the regulators of other systems about whose mechanisms there is some data.
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Transport between the cell nucleus and the cytoplasm.

TL;DR: A focus of this review is nuclear export of messenger RNA, which apparently largely relies on export mediators distinct from importin beta-related factors.
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Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs

TL;DR: Nuclear export of pre-miRNAs is studied and it is shown that the process is saturable and thus carrier-mediated, and that exportin 5 interacts with double-stranded RNA in a sequence-independent manner.
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Messenger-RNA-binding proteins and the messages they carry.

TL;DR: From sites of transcription in the nucleus to the outreaches of the cytoplasm, messenger RNAs are associated with RNA-binding proteins that communicate crucial information to the translation machinery for the surveillance of nonsense mutations and for mRNA localization and translation.
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RNA-binding proteins and post-transcriptional gene regulation

TL;DR: The RBPs that interact with pre‐mRNAs and mRNAs are focused on and their roles in the regulation of post‐transcriptional gene expression are discussed.
References
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Journal ArticleDOI

CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals

TL;DR: It is concluded that CRM1 is an export receptor for leucine-rich nuclear export signals and a model for the role of RanGTP inCRM1 function and in nuclear export in general is discussed.
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Analytical properties of the nanoelectrospray ion source.

TL;DR: Improved desolvation in nanoES led to instrument-limited resolution of the signals of a glycoprotein and the ability to signal average extensively allowed the C-terminal sequencing of a 40 kDa protein.
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Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry

TL;DR: A simple and robust technique for the sequencing of proteins isolated by polyacrylamide gel electro-phoresis, using nano-electrospray3,4 tandem mass spectrometry5,6 and multiple-sequence stretches of up to 16 amino acids are obtained.
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Error-tolerant identification of peptides in sequence databases by peptide sequence tags.

TL;DR: A new approach to the identification of mass spectrometrically fragmented peptides is demonstrated and an algorithm developed here that uses the sequence tag to find the peptide in a sequence database is up to 1 million-fold more discriminating than the partial sequence information alone.
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CRM1 is responsible for intracellular transport mediated by the nuclear export signal

TL;DR: It is shown that p110 is CRM1, which is an evolutionarily conserved protein originally found as an essential nuclear protein in fission yeast and known as a likely target of LMB, which indicates that CRM 1 is an essential mediator of the NES-dependent nuclear export of proteins in eukaryotic cells.
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