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Paperback

Evolutionary conserved features of FG repeats that allow the formation of hydrogel-based perme-ability barriers with NPC-like properties

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Non-globular FG domains constitute the permeability barrier of nuclear pore complexes (NPCs), which control all macromolecular exchange between nucleus and cytoplasm. Whilst objects smaller than 30kDa can passively diffuse across this barrier, larger molecules need to be chaperoned by nuclear transport receptors (NTRs). However, the modus operandi and, inextricably linked, the exact physical nature of the NPC permeability barrier are still controversially discussed. Whereas so far, most studies exclusively focused on yeast or vertebrate FG domains, the ability of FG domains from different species to form selective barriers was explored here. Interestingly, all studied species contain ‘cohesive’ FG domains that interact with each other to form a characteristic (hydrogel) phase mimicking the permeability properties of NPCs.

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MORE INFO
Format
Paperback
Publisher
Cuvillier
Date
23 August 2013
Pages
172
ISBN
9783954044917

Non-globular FG domains constitute the permeability barrier of nuclear pore complexes (NPCs), which control all macromolecular exchange between nucleus and cytoplasm. Whilst objects smaller than 30kDa can passively diffuse across this barrier, larger molecules need to be chaperoned by nuclear transport receptors (NTRs). However, the modus operandi and, inextricably linked, the exact physical nature of the NPC permeability barrier are still controversially discussed. Whereas so far, most studies exclusively focused on yeast or vertebrate FG domains, the ability of FG domains from different species to form selective barriers was explored here. Interestingly, all studied species contain ‘cohesive’ FG domains that interact with each other to form a characteristic (hydrogel) phase mimicking the permeability properties of NPCs.

Read More
Format
Paperback
Publisher
Cuvillier
Date
23 August 2013
Pages
172
ISBN
9783954044917