Imaging within single NPCs reveals NXF1's role in mRNA export on the cytoplasmic side of the pore.
Active Transport, Cell Nucleus
/ physiology
Cell Line, Tumor
Cytoplasm
/ genetics
DEAD-box RNA Helicases
/ genetics
Humans
Nuclear Pore
/ genetics
Nucleocytoplasmic Transport Proteins
/ genetics
RNA, Messenger
/ genetics
RNA-Binding Proteins
/ genetics
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ genetics
Journal
The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356
Informations de publication
Date de publication:
02 09 2019
02 09 2019
Historique:
received:
25
01
2019
revised:
21
06
2019
accepted:
03
07
2019
pubmed:
4
8
2019
medline:
13
5
2020
entrez:
4
8
2019
Statut:
ppublish
Résumé
Translocation of mRNA through the nuclear pore complex (NPC) requires interactions with different NPC regions. To determine the interactions that are crucial for effective mRNA export in living cells, we examined mRNA export within individual pores by applying various types of mRNA export blocks that stalled mRNPs at different stages of transition. Focusing on the major mRNA export factor NXF1, we found that initial mRNP binding to the NPC did not require NXF1 in the NPC, whereas release into the cytoplasm did. NXF1 localization in the NPC did not require RNA or RNA binding. Superresolution microscopy showed that NXF1 consistently occupied positions on the cytoplasmic side of the NPC. Interactions with specific nucleoporins were pinpointed using FLIM-FRET for measuring protein-protein interactions inside single NPCs, showing that Dbp5 helicase activity of mRNA release is conserved in yeast and humans. Altogether, we find that specific interactions on the cytoplasmic side of the NPC are fundamental for the directional flow of mRNA export.
Identifiants
pubmed: 31375530
pii: jcb.201901127
doi: 10.1083/jcb.201901127
pmc: PMC6719458
doi:
Substances chimiques
NXF1 protein, human
0
Nucleocytoplasmic Transport Proteins
0
RNA, Messenger
0
RNA-Binding Proteins
0
Saccharomyces cerevisiae Proteins
0
DDX19B protein, human
EC 3.6.1.-
DEAD-box RNA Helicases
EC 3.6.4.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2962-2981Informations de copyright
© 2019 Ben-Yishay et al.
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