How to operate a nuclear pore complex by Kap-centric control

Lim, Roderick Y. H.; Huang, Biao; Kapinos, Larisa E.

doi:10.1080/19491034.2015.1090061

Cited by 46 publications

(61 citation statements)

References 74 publications

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“…5 A ). We had previously shown that a pool of endogenous Kapβ1 (endoKapβ1) persisted at the NE for a prolonged duration after permeabilization ( Lim et al, 2015 ). Upon confirming that endogenous Kapα (endoKapα) colocalizes with endoKapβ1 at the NE, we used Ran mix, which reinstates the soluble transport machinery to power NCT in permeabilized cells ( Görlich et al, 1995 ).…”

Section: Resultsmentioning

confidence: 99%

“…Indeed, evidence of these two pools can be found in the bimodal kinetics of exogenous Kapβ1 in digitonin-permeabilized cells ( Lowe et al, 2015 ) and mRNA export in living cells ( Grünwald and Singer, 2010 ). We therefore proposed a mechanism known as Kap-centric control whereby Kapβ1 occupancy in the FG Nups plays a role in regulating NPC barrier selectivity and transport speed ( Lim et al, 2015 ).…”

Section: Introductionmentioning

confidence: 99%

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Karyopherins regulate nuclear pore complex barrier and transport function

Kapinos

Huang

Rencurel

et al. 2017

Journal of Cell Biology

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113

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Karyopherins regulate nuclear pore complex barrier and transport function

Kapinos

Huang

Rencurel

et al. 2017

Journal of Cell Biology

Self Cite

113

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“…During transport, NTRs modulate the biophysical state of the disordered FG-Nups inside the NPC by engaging in rapid binding and unbinding events [22,[137][138][139][140]. Recent data suggest that NTRs can also modulate the biophysical state and toxicity of several IDPs related to neurodegenerative diseases [134,[141][142][143][144][145][146].…”

Section: Maintenance Quiescent Muscle Cells Maintain Theirmentioning

confidence: 99%

Poor old pores—The challenge of making and maintaining nuclear pore complexes in aging

2020

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The nuclear pore complex (NPC) is the sole gateway to the nuclear interior, and its function is essential to all eukaryotic life. Controlling the functionality of NPCs is a tremendous challenge for cells. Firstly, NPCs are large structures, and their complex assembly does occasionally go awry. Secondly, once assembled, some components of the NPC persist for an extremely long time and, as a result, are susceptible to accumulate damage. Lastly, a significant proportion of the NPC is composed of intrinsically disordered proteins that are prone to aggregation. In this review, we summarize how the quality of NPCs is guarded in young cells and discuss the current knowledge on the fate of NPCs during normal aging in different tissues and organisms. We discuss the extent to which current data supports a hypothesis that NPCs are poorly maintained during aging of nondividing cells, while in dividing cells the main challenge is related to the assembly of new NPCs. Our survey of current knowledge points toward NPC quality control as an important node in aging of both dividing and nondividing cells. Here, the loss of protein homeostasis during aging is central and the NPC appears to both be impacted by, and to drive, this process.

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“…Many different models have been proposed to explain the selective transport of NTRs through NPCs, including the virtual-gate model ( Rout et al, 2000 ; Rout et al, 2003 ), the reversible-collapse (or polymer-brush) model ( Lim et al, 2007 ), the reduction-of-dimensionality ( Peters, 2005 ) and ‘molecular velcro’ ( Schleicher et al, 2014 ) model, the hydrogel model ( Ribbeck and Görlich, 2001 ; Frey and Görlich, 2007 ), the Kap-centric model ( Lim et al, 2015 ; Kapinos et al, 2017 ), and the forest model ( Yamada et al, 2010 ). However, no consensus has been reached on one prevailing model.…”

Section: Introductionmentioning

confidence: 99%

Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics

Ananth

Mishra

Frey

et al. 2018

eLife

113

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Nuclear pore complexes (NPCs) lined with intrinsically disordered FG-domains act as selective gatekeepers for molecular transport between the nucleus and the cytoplasm in eukaryotic cells. The underlying physical mechanism of the intriguing selectivity is still under debate. Here, we probe the transport of ions and transport receptors through biomimetic NPCs consisting of Nsp1 domains attached to the inner surface of solid-state nanopores. We examine both wildtype FG-domains and hydrophilic SG-mutants. FG-nanopores showed a clear selectivity as transport receptors can translocate across the pore whereas other proteins cannot. SG mutant pores lack such selectivity. To unravel this striking difference, we present coarse-grained molecular dynamics simulations that reveal that FG-pores exhibit a high-density, nonuniform protein distribution, in contrast to a uniform and significantly less-dense protein distribution in the SG-mutant. We conclude that the sequence-dependent density distribution of disordered proteins inside the NPC plays a key role for its conductivity and selective permeability.

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How to operate a nuclear pore complex by Kap-centric control

Cited by 46 publications

References 74 publications

Karyopherins regulate nuclear pore complex barrier and transport function

Karyopherins regulate nuclear pore complex barrier and transport function

Poor old pores—The challenge of making and maintaining nuclear pore complexes in aging

Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics

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