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

Weirich, Christine S.; Erzberger, J.P.; Flick, J S; Berger, James M.; Thorner, Jeremy; Weis, Karsten

doi:10.1038/ncb1424

Cited by 261 publications

(316 citation statements)

References 42 publications

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“…It interacts with the transcription machinery and with nascent RNPs 74,75 to mediate mRNA export from the nucleus 110,111 , and it has also been implicated in the termination of translation 112,113 . Although it is not known whether Dbp5 remains bound to mRNAs from transcription to export, as eIF4AIII does, elegant studies have demonstrated that Dbp5 activity must be highly localized during mRNA export 114,115 .…”

Section: Nuclear Specklesmentioning

confidence: 99%

“…Dbp5 also interacts with nuclear pore protein Gle1 (REFS 117,120), and the C-terminal region of Gle1 stim ulates RNA-dependent ATPase activity of Dbp5 in vitro 114,121 . Gle1 mutants that fail to activate Dbp5 also affect mRNA export 114 .…”

Section: Nuclear Specklesmentioning

confidence: 99%

“…Gle1 mutants that fail to activate Dbp5 also affect mRNA export 114 . These findings suggest that Gle1 is a specific cofactor of Dbp5 (REF.…”

Section: Nuclear Specklesmentioning

confidence: 99%

“…These findings suggest that Gle1 is a specific cofactor of Dbp5 (REF. 114). Several observations suggest that Gle1 activates Dbp5 in a manner that requires the small metabolite inositol hexakisphosphate (InsP 6 ) 114,115 .…”

Section: Nuclear Specklesmentioning

confidence: 99%

“…114). Several observations suggest that Gle1 activates Dbp5 in a manner that requires the small metabolite inositol hexakisphosphate (InsP 6 ) 114,115 . Mutations in the InsP 6 pathway genetically interact with gle1 mutants 122 and, in vitro, InsP 6 further increases the Gle1-dependent stimulation of Figure 4 | Regulation of eIF4A during translation initiation.…”

Section: Nuclear Specklesmentioning

confidence: 99%

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From unwinding to clamping — the DEAD box RNA helicase family

Linder

Jankowsky

2011

Nat Rev Mol Cell Biol

917

1,035

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Nearly all aspects of RNA metabolism, from transcription and translation to mRNA decay, involve RNA helicases, which are enzymes that use ATP to bind or remodel RNA and RNA-protein complexes (ribonucleoprotein (RNP) complexes) 1 . RNA helicases are found in all three domains of life, and many viruses also encode one or more of these proteins 2,3 . Together with the structurally related DNA helicases that function in replication, recombination and repair, the RNA helicases are classified into superfamilies and families, based on sequence and structural features 3,4 . DEAD box proteins form the largest helicase family, with 37 members in humans and 26 in Saccharomyces cerevisiae 3 , and are characterized by the presence of an Asp-Glu-Ala-Asp (DEAD) motif.DEAD box helicases have central and, in many cases, essential physiological roles in cellular RNA metabolism 5 (FIG. 1). The proteins generally function as part of larger multicomponent assemblies, such as the spliceosom e or the eukaryotic translation initiation machinery 6 . Mutations and deregulation of several DEAD box proteins have been linked to disease states, including cancer 7 . Although all DEAD box proteins contain a structurally highly conserved core with conserved ATP-binding and RNA-binding sites, different proteins have been associated with diverse and seemingly unrelated functions, including the disassembly of RNPs, chaperoning during RNA folding and even stabil ization of protein complexes on RNA 5,6 . How these highly conserved proteins fulfil such an array of different functions has been a long-standing question.Research has now started to illuminate the molecular basis for this functional diversity. In this Review, we summarize how structural data, together with biochemical and biophysical studies, have revealed unexpected modes by which these proteins function. We also discuss how novel molecular and cell biological approaches have better defined the cellular roles of DEAD box helicases. We outline our current view on common structural and mechan istic themes that have emerged, and on physical models of how these 'unusual' RNA helicases work.Structures of DEAD box RNA helicases A number of structural studies have universally shown that members of the DEAD box family contain a highly conserved helicase core that harbours the binding sites for ATP and RNA 3,4,8 . The core is surrounded by variable auxiliary domains, which are thought to be critical for the diverse functions of these enzymes.Structure of the helicase core. DEAD box proteins belong to helicase superfamily 2 (SF2) 2 . Similarly to all SF2 helicases, DEAD box proteins are built around a highly conserved helicase core of two virtually identical domains that resemble the bacterial recombination protein recombinase A (RecA) 3,4,8 (FIG. 2a,b). Within this helicase core, at least 12 characteristic sequence motifs are located at conserved positions (FIG. 2a,b). Some of these motifs are conserved across the entire SF2 family, whereas others are found only in the DEAD box family 3 ....

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Section: Nuclear Specklesmentioning

confidence: 99%

Section: Nuclear Specklesmentioning

confidence: 99%

“…Gle1 mutants that fail to activate Dbp5 also affect mRNA export 114 . These findings suggest that Gle1 is a specific cofactor of Dbp5 (REF.…”

Section: Nuclear Specklesmentioning

confidence: 99%

Section: Nuclear Specklesmentioning

confidence: 99%

Section: Nuclear Specklesmentioning

confidence: 99%

See 3 more Smart Citations

From unwinding to clamping — the DEAD box RNA helicase family

Linder

Jankowsky

2011

Nat Rev Mol Cell Biol

917

1,035

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The Plant Nuclear Pore Complex — The Nucleocytoplasmic Barrier and Beyond

Zhou

Boruc

Meier

2013

Annual Plant Reviews

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The Plant Nuclear Pore Complex – The Nucleocytoplasmic Barrier and Beyond

Zhou

Boruc

Meier

2018

Annual Plant Reviews Online

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The nuclear pore complex (NPC) provides a highly organized pathway for selective transport between the nucleoplasm and the cytoplasm. Recent work undertaken to characterize the mechanisms and regulation of transport through the plant NPC has resulted in the identification of key components showing similarities – and also significant differences – between plants and other organisms. Mutant studies reveal roles for nucleoporins in plant–microbe interactions, hormone response, abiotic‐stress tolerance, plant development, and flowering‐time regulation. Recently, significant progress has been made in identifying about 30 proteins that constitute the plant NPC as well as several NPC‐associated proteins and in characterizing the structure of the plant NPC. A newly discovered connection between nuclear pore‐associated proteins and inner nuclear envelope proteins expands our knowledge of plant nuclear envelope architecture. Dynamic patterns of subcellular localization suggest mitotic functions of plant nucleoporins away from the nuclear pore.

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

Cited by 261 publications

References 42 publications

From unwinding to clamping — the DEAD box RNA helicase family

From unwinding to clamping — the DEAD box RNA helicase family

The Plant Nuclear Pore Complex — The Nucleocytoplasmic Barrier and Beyond

The Plant Nuclear Pore Complex – The Nucleocytoplasmic Barrier and Beyond

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