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DBP5 Dbp5p

Dbp5, Dbp5p, rat8
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which exhibits RNA-dependent ATPase and ATP-dependent RNA-unwinding activities. This protein is recruited to the cytoplasmic fibrils of the nuclear pore complex, where it participates in the export of mRNA from the nucleus. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Gle1, ATPase, CAN, STEP, AGE
Papers on Dbp5
Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex.
Wente et al., Nashville, United States. In Genetics, 2014
In Saccharomyces cerevisiae, the NPC proteins Nup159 and Nup42 are asymmetrically localized to the cytoplasmic face and have distinct functional domains: a phenylalanine-glycine (FG) repeat domain that docks mRNP transport receptors and domains that bind the DEAD-box ATPase Dbp5 and its activating cofactor Gle1, respectively.
Degradation of oligouridylated histone mRNAs: see UUUUU and goodbye.
Review
Heissmeyer et al., München, Germany. In Wiley Interdiscip Rev Rna, 2014
Recent research on factors such as SLIP1, DBP5, eIF3, CTIF, CBP80/20, and ERI1 has provided new insights into the 3' end formation, the nuclear export, and the translation of histone mRNAs.
AMP sensing by DEAD-box RNA helicases.
Jankowsky et al., Cleveland, United States. In J Mol Biol, 2013
However, the yeast DEAD-box helicases Sub2p and Dbp5p are not inhibited by AMP.
Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins.
Conti et al., Chapel Hill, United States. In Nucleic Acids Res, 2013
We discovered a SLIP1-binding motif (SBM) in two additional proteins: the translation initiation factor eIF3g and the mRNA-export factor DBP5.
Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its function in mRNA nuclear export.
Stewart et al., Cambridge, United Kingdom. In Structure, 2012
Structural coherence is lost in the RNA-binding compromised Nab2-C437S mutant, which also suppresses the rat8-2 allele of RNA helicase Dbp5.
Insights into mRNP biogenesis provided by new genetic interactions among export and transcription factors.
Cole et al., Burjassot, Spain. In Bmc Genet, 2011
Although the shuttling DEAD-box protein Dbp5p is concentrated on the cytoplasmic fibrils of the NPC, previous studies demonstrated that it interacts physically and genetically with factors involved in transcription initiation.
Dbp5, Gle1-IP6 and Nup159: a working model for mRNP export.
GeneRIF
Wente et al., Nashville, United States. In Nucleus, 2011
Dbp5, Gle1-IP6 and Nup159: a working model for mRNP export.
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.
Wente et al., Nashville, United States. In Genes Dev, 2011
At cytoplasmic NPC filaments, the ATPase activity of DEAD-box protein Dbp5 is activated by inositol hexakisphosphate (IP(6))-bound Gle1 to mediate remodeling of mRNA-protein (mRNP) complexes.
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.
Cole et al., United States. In Genes Dev, 2011
The DEAD-box protein Dbp5 mediates export by triggering removal of mRNP proteins in a spatially controlled manner.
Structural basis for the function of the Saccharomyces cerevisiae Gfd1 protein in mRNA nuclear export.
Stewart et al., Cambridge, United Kingdom. In J Biol Chem, 2010
Dbp5 removes Nab2 from mRNPs at the cytoplasmic face of the pore and, importantly, a Nab2 RNA-binding mutant suppresses the thermosensitive rat8-2 (dbp5) mutant.
Control of mRNA export and translation termination by inositol hexakisphosphate requires specific interaction with Gle1.
GeneRIF
Wente et al., Nashville, United States. In J Biol Chem, 2010
Gle1 specifically binds IP(6); this interaction is required for the full potentiation of Dbp5 ATPase activity during both mRNA export and translation termination
Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA.
Felber et al., Frederick, United States. In Nucleic Acids Res, 2009
The DEAD family RNA helicase Dbp5 is essential for nuclear export of mRNA and is thought to dissociate Mex67 from mRNP upon translocation, thereby generating directional passage.
Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.
GeneRIF
Weis et al., Berkeley, United States. In Proc Natl Acad Sci U S A, 2009
Study identified several charged surface residues that, when mutated, weaken the binding of Gle1 and inhibit the ability of Gle1 to stimulate Dbp5's ATPase activity.
Systolic and fourth- and fifth-phase diastolic blood pressure from ages 8 to 18 years: Project HeartBeat!
Eissa et al., Atlanta, United States. In Am J Prev Med, 2009
BACKGROUND: Systolic and fourth-phase and fifth-phase diastolic blood pressure (SBP, DBP4, DBP5) have appeared to differ in their patterns of age-related change, and SBP and DBP5 differ in their respective associations with anthropometric variables.
The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch.
GeneRIF
Schüler et al., Stockholm, Sweden. In J Biol Chem, 2009
Results describe the crystal structures of human DDX19, a DEXD/H-box protein, in its open and closed cleft conformations.
The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner.
GeneRIF
Conti et al., Martinsried, Germany. In Nat Struct Mol Biol, 2009
Using in vitro assays, the authors demonstrate that NUP214 decreases both the RNA binding and ATPase activities of DBP5.
Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export.
Impact
GeneRIF
Weis et al., Berkeley, United States. In Nat Cell Biol, 2006
Our results define specific functions for Gle1 and InsP6 in mRNA export and suggest that local activation of Dbp5 at the nuclear pore is critical for mRNA export.
Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export.
Impact
GeneRIF
Wente et al., Nashville, United States. In Nat Cell Biol, 2006
Dbp5 activation at NPCs requires Gle1 and InsP6. This would facilitate spatial control of the remodelling of mRNP protein composition during directional transport and provide energy to power transport cycles.
Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function.
Impact
Jeang et al., Bethesda, United States. In Cell, 2004
Plausibly, DDX3 is the human RNA helicase which functions in the CRM1 RNA export pathway analogously to the postulated role for Dbp5p in yeast mRNA export.
Blood pressure by age in childhood and adolescence: a review of 129 surveys worldwide.
Review
Labarthe et al., Houston, United States. In Int J Epidemiol, 1989
The results indicate, foremost, the almost universal overall upward progression of blood pressure levels between ages 6 and 18 years, separately for systolic, fourth-phase and fifth-phase diastolic pressures (SBP, DBP4, DBP5).
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