English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Preprint

A quantitative map of nuclear pore assembly reveals two distinct mechanisms

MPS-Authors
/persons/resource/persons226314

Politi,  Antonio Z.
Research Group of Cytoskeletal Dynamics in Oocytes, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Facility for Light Microscopy, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
Supplementary Material (public)
There is no public supplementary material available
Citation

Otsuka, S., Tempkin, J. O. B., Zhang, W., Politi, A. Z., Rybina, A., Hossain, M. J., et al. (2022). A quantitative map of nuclear pore assembly reveals two distinct mechanisms. bioRxiv. doi:10.1101/2021.05.17.444137.


Cite as: https://hdl.handle.net/21.11116/0000-000C-8C37-9
Abstract
Understanding how the nuclear pore complex (NPC) assembles is of fundamental importance to grasp the mechanisms behind its essential function and understand its role during evolution of eukaryotes1–4. While at least two NPC assembly pathways exist, one during exit from mitosis and one during nuclear growth in interphase, we currently lack a quantitative map of the molecular assembly events. Here, we use fluorescence correlation spectroscopy (FCS) calibrated live imaging of endogenously fluorescently-tagged nucleoporins to map the changes in composition and stoichiometry of seven major modules of the human NPC during its assembly in single dividing cells. This systematic quantitative map reveals that the two assembly pathways employ strikingly different molecular mechanisms, inverting the order of addition of two large structural components, the central ring complex and nuclear filaments. The dynamic stoichiometry data underpinned integrative spatiotemporal modeling of the NPC assembly pathway, predicting the structures of postmitotic NPC assembly intermediates.