2000
DOI: 10.1017/s1355838200000832
|View full text |Cite
|
Sign up to set email alerts
|

The mRNA export in Caenorhabditis elegans is mediated by Ce-NXF-1, an ortholog of human TAP/NXF and Saccharomyces cerevisiae Mex67p

Abstract: , and Nup214, indicating that the rim association occurs through components of the nuclear pore complex. In summary, Ce-NXF-1 belongs together with hTAP and Mex67p to a family of proteins that participate in mRNA export and can provide a direct molecular link between mRNAs and components of the nuclear pore complex. Therefore, despite differences in mRNA metabolism between these species, they utilize a conserved mRNA transport mechanism.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

4
92
0

Year Published

2001
2001
2018
2018

Publication Types

Select...
6
2
2

Relationship

0
10

Authors

Journals

citations
Cited by 95 publications
(96 citation statements)
references
References 37 publications
4
92
0
Order By: Relevance
“…Nuclear export of RNA Nuclear export of most mRNAs relies on NXF-1/TAP and HEL-1/UAP56 (Tan et al 2000;MacMorris et al 2003), whereas XPO-1 is responsible for export of other RNA polymerase II-transcribed genes, such as small nuclear RNAs, premicro RNAs (pre-miRNAs), and certain mRNAs. The best-characterized miRNA in C. elegans is let-7, which controls developmental timing.…”
Section: Nuclear Localization and Nuclear Export Signalsmentioning
confidence: 99%
“…Nuclear export of RNA Nuclear export of most mRNAs relies on NXF-1/TAP and HEL-1/UAP56 (Tan et al 2000;MacMorris et al 2003), whereas XPO-1 is responsible for export of other RNA polymerase II-transcribed genes, such as small nuclear RNAs, premicro RNAs (pre-miRNAs), and certain mRNAs. The best-characterized miRNA in C. elegans is let-7, which controls developmental timing.…”
Section: Nuclear Localization and Nuclear Export Signalsmentioning
confidence: 99%
“…[17][18][19][20][21][22] Other studies suggest that the role of NUP98 in RNA transport may be mediated by TAP (TIP associated protein), a novel cellular factor first identified for its interaction with TIP (tyrosine kinase-interacting protein) (Figure 1a). [30][31][32] TAP is required for export of cellular mRNA substrates. The glutamine-rich C-terminal domain of TAP interacts with the FG repeats of NUP98.…”
Section: Figurementioning
confidence: 99%
“…TAP, which itself facilitates the nuclear export of cellular mRNA (45,46), heterodimerizes with p15 that further stimulates mRNP export (47,48). TAP proteins represent a class of nuclear transport receptors that, via an essential C-terminal domain, directly interact with nucleoporin components of the NPC (49 -51).…”
mentioning
confidence: 99%