Abstract
The nuclear pore complex (NPC) is the sole mediator of nucle-ocytoplasmic transport. Despite great advances in understanding its conserved core architecture, the peripheral regions can exhibit considerable variation within and between species. One such structure is the cage-like nuclear basket. Despite its crucial roles in mRNA surveillance and chromatin organization, an architectural understanding has remained elusive. Using in-cell cryo-electron tomography and subtomogram analysis, we explored the NPC’s structural variations and the nuclear basket across fungi (yeast; S. cerevisiae), mammals (mouse; M. musculus), and protozoa (T. gondii). Using integrative structural modeling, we computed a model of the basket in yeast and mammals that revealed how a hub of Nups in the nuclear ring binds to basket-forming Mlp/Tpr proteins: the coiled-coil domains of Mlp/Tpr form the struts of the basket, while their unstructured termini constitute the basket distal densities, which potentially serve as a docking site for mRNA preprocessing before nucleocytoplasmic transport
Competing Interest Statement
The authors have declared no competing interest.
Footnotes
Digvijay Singh: dgvjayS
Neelesh Soni: neeleshsoni03
Joshua Hutchings: Josh-Hutchings94
Ignacia Echeverria: ig_ech
Trevor van Eeuwen: _themovingvan_
Michael P. Rout : Rout-Lab_RU
Andrej Sali : salilab_ucsf
Elizabeth Villa : TheVillaLab