Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions.
Sci Adv
; 5(11): eaax1836, 2019 11.
Article
in En
| MEDLINE
| ID: mdl-31807700
ABSTRACT
Intrinsically disordered regions (IDRs) of proteins are implicated in key macromolecular interactions. However, the molecular forces underlying IDR function within multicomponent assemblies remain elusive. By combining thermodynamic and structural data, we have discovered an allostery-based mechanism regulating the soluble core region of the nuclear pore complex (NPC) composed of nucleoporins Nup53, Nic96, and Nup157. We have identified distinct IDRs in Nup53 that are functionally coupled when binding to partner nucleoporins and karyopherins (Kaps) involved in NPC assembly and nucleocytoplasmic transport. We show that the Nup53·Kap121 complex forms an ensemble of structures that destabilize Nup53 hub interactions. Our study provides a molecular framework for understanding how disordered and folded domains communicate within macromolecular complexes.
Full text:
1
Database:
MEDLINE
Main subject:
Membrane Transport Proteins
/
Saccharomyces cerevisiae
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Receptors, Cytoplasmic and Nuclear
/
Nuclear Pore
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Nuclear Pore Complex Proteins
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Saccharomyces cerevisiae Proteins
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Multiprotein Complexes
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Intrinsically Disordered Proteins
Language:
En
Year:
2019
Type:
Article