Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores

Krishna C. Mudumbi (), Rafal Czapiewski, Andrew Ruba, Samuel L. Junod, Yichen Li, Wangxi Luo, Christina Ngo, Valentina Ospina, Eric C. Schirmer () and Weidong Yang ()
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Krishna C. Mudumbi: Temple University
Rafal Czapiewski: University of Edinburgh
Andrew Ruba: Temple University
Samuel L. Junod: Temple University
Yichen Li: Temple University
Wangxi Luo: Temple University
Christina Ngo: Temple University
Valentina Ospina: Temple University
Eric C. Schirmer: University of Edinburgh
Weidong Yang: Temple University

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract Roughly 10% of eukaryotic transmembrane proteins are found on the nuclear membrane, yet how such proteins target and translocate to the nucleus remains in dispute. Most models propose transport through the nuclear pore complexes, but a central outstanding question is whether transit occurs through their central or peripheral channels. Using live-cell high-speed super-resolution single-molecule microscopy we could distinguish protein translocation through the central and peripheral channels, finding that most inner nuclear membrane proteins use only the peripheral channels, but some apparently extend intrinsically disordered domains containing nuclear localization signals into the central channel for directed nuclear transport. These nucleoplasmic signals are critical for central channel transport as their mutation blocks use of the central channels; however, the mutated proteins can still complete their translocation using only the peripheral channels, albeit at a reduced rate. Such proteins can still translocate using only the peripheral channels when central channel is blocked, but blocking the peripheral channels blocks translocation through both channels. This suggests that peripheral channel transport is the default mechanism that was adapted in evolution to include aspects of receptor-mediated central channel transport for directed trafficking of certain membrane proteins.

Date: 2020
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DOI: 10.1038/s41467-020-16033-x

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