Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions.
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.
Duke Scholars
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- Saccharomyces cerevisiae Proteins
- Saccharomyces cerevisiae
- Receptors, Cytoplasmic and Nuclear
- Protein Domains
- Nuclear Pore Complex Proteins
- Nuclear Pore
- Multiprotein Complexes
- Membrane Transport Proteins
- Intrinsically Disordered Proteins
- Allosteric Regulation
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Saccharomyces cerevisiae Proteins
- Saccharomyces cerevisiae
- Receptors, Cytoplasmic and Nuclear
- Protein Domains
- Nuclear Pore Complex Proteins
- Nuclear Pore
- Multiprotein Complexes
- Membrane Transport Proteins
- Intrinsically Disordered Proteins
- Allosteric Regulation