Influence of cargo size on Ran and energy requirements for nuclear protein import

Abstract

Previous work has shown that the transport of some small protein cargoes through the nuclear pore complex (NPC) can occur in vitro in the absence of nucleoside triphosphate hydrolysis. We now demonstrate that in the importin alpha/beta and transportin import pathways, efficient in vitro transport of large proteins, in contrast to smaller proteins, requires hydrolyzable GTP and the small GTPase Ran. Morphological and biochemical analysis indicates that the presence of Ran and GTP allows large cargo to efficiently cross central regions of the NPC. We further demonstrate that this function of RanGTP at least partly involves its direct binding to importin beta and transportin. We suggest that RanGTP functions in these pathways to promote the transport of large cargo by enhancing the ability of import complexes to traverse diffusionally restricted areas of the NPC.

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BibTeX RIS

BibTeX

@article{lyman2026influence,
  title = {{Influence of cargo size on Ran and energy requirements for nuclear protein import}},
  author = {Susan K. Lyman and Tinglu Guan and Janna Bednenko and Harald Wodrich and Larry Gerace},
  journal = {Journal of Cell Biology},
  year = {2026},
  month = oct,
  doi = {10.1083/jcb.200204163},
  url = {https://hal.science/hal-05784106v1},
  note = {CC BY-NC-SA},
}

RIS

TY  - JOUR
TI  - Influence of cargo size on Ran and energy requirements for nuclear protein import
AU  - Susan K. Lyman
AU  - Tinglu Guan
AU  - Janna Bednenko
AU  - Harald Wodrich
AU  - Larry Gerace
PY  - 2026
DA  - 2026/10/07
JO  - Journal of Cell Biology
DO  - 10.1083/jcb.200204163
UR  - https://hal.science/hal-05784106v1
AB  - Previous work has shown that the transport of some small protein cargoes through the nuclear pore complex (NPC) can occur in vitro in the absence of nucleoside triphosphate hydrolysis. We now demonstrate that in the importin alpha/beta and transportin import pathways, efficient in vitro transport of large proteins, in contrast to smaller proteins, requires hydrolyzable GTP and the small GTPase Ran. Morphological and biochemical analysis indicates that the presence of Ran and GTP allows large cargo to efficiently cross central regions of the NPC. We further demonstrate that this function of RanGTP at least partly involves its direct binding to importin beta and transportin. We suggest that RanGTP functions in these pathways to promote the transport of large cargo by enhancing the ability of import complexes to traverse diffusionally restricted areas of the NPC.
SN  - 0021-9525
SN  - 1540-8140
ER  -

Abstract

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