Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export.

Nature cell biology - 1 Jul 2006

Weirich Christine S, Erzberger Jan P, Flick Jeffrey S, Berger James M, Thorner Jeremy, Weis Karsten

Abstract excerpt

The DExD/H-box ATPase Dbp5 is essential for nuclear mRNA export, although its precise role in this process remains poorly understood. Here, we identify the nuclear pore protein Gle1 as a cellular activator of Dbp5. Dbp5 alone is unable to stably bind RNA or effectively hydrolyse ATP under physiological conditions, but addition of Gle1 dramatically stimulates these activities. A gle1 point mutant deficient for...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Active Transport, Cell Nucleus
Share to DEAD-box RNA Helicases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Nuclear Pore

Share to Nuclear Pore Complex Proteins

Share to Nucleocytoplasmic Transport Proteins

Share to Phytic Acid

Share to RNA Helicases

Source

Identifiers

PMID: 16783364
DOI: 10.1038/ncb1424

Genes

GLE1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export.PMID 16783364Read ↗

The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1.Semantic proximity Read ↗

The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1.Semantic proximity Read ↗

Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.Semantic proximity Read ↗

Gle1 is a multifunctional DEAD-box protein regulator that modulates Ded1 in translation initiation.Semantic proximity Read ↗

Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells.Semantic proximity Read ↗

The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim.Semantic proximity Read ↗

The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p.Semantic proximity Read ↗

Nuclear Export of Pre-Ribosomal Subunits Requires Dbp5, but Not as an RNA-Helicase as for mRNA Export.Semantic proximity Read ↗

An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components.Semantic proximity Read ↗

A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export.Semantic proximity Read ↗

Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway.Semantic proximity Read ↗

The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.