Structural biology and regulation of protein import into the nucleus

M Christie, CW Chang, G Róna, KM Smith… - Journal of molecular …, 2016 - Elsevier
Proteins are translated in the cytoplasm, but many need to access the nucleus to perform
their functions. Understanding how these nuclear proteins are transported through the …

Nuclear localization signals for four distinct karyopherin-β nuclear import systems

M Soniat, YM Chook - Biochemical Journal, 2015 - portlandpress.com
The Karyopherin-β family of proteins mediates nuclear transport of macromolecules. Nuclear
versus cytoplasmic localization of proteins is often suggested by the presence of NLSs …

Recognition of the TDP-43 nuclear localization signal by importin α1/β

SG Doll, H Meshkin, AJ Bryer, F Li, YH Ko… - Cell reports, 2022 - cell.com
Cytoplasmic mislocalization of the TAR-DNA binding protein of 43 kDa (TDP-43) leads to
large, insoluble aggregates that are a hallmark of amyotrophic lateral sclerosis and …

[HTML][HTML] Transportin-1 and Transportin-2: protein nuclear import and beyond

L Twyffels, C Gueydan, V Kruys - FEBS letters, 2014 - Elsevier
Nearly 20 years after its identification as a new β-karyopherin mediating the nuclear import
of the RNA-binding protein hnRNP A1, Transportin-1 is still commonly overlooked in …

Nonclassical nuclear localization signals mediate nuclear import of CIRBP

B Bourgeois, S Hutten, B Gottschalk… - Proceedings of the …, 2020 - National Acad Sciences
The specific interaction of importins with nuclear localization signals (NLSs) of cargo
proteins not only mediates nuclear import but also, prevents their aberrant phase separation …

Structural determinants of nuclear export signal orientation in binding to exportin CRM1

HYJ Fung, SC Fu, CA Brautigam, YM Chook - elife, 2015 - elifesciences.org
The Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of
hundreds of proteins through recognition of their nuclear export signals (NESs), which are …

Protoplast Isolation and Shoot Regeneration from Protoplast-Derived Callus of Petunia hybrida Cv. Mirage Rose

HH Kang, AH Naing, CK Kim - Biology, 2020 - mdpi.com
Despite the increasing use of protoplasts in plant biotechnology research, shoot
regeneration from protoplasts remains challenging. In this study, we investigated the factors …

A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1

P Barraud, S Banerjee, WI Mohamed… - Proceedings of the …, 2014 - National Acad Sciences
The human RNA-editing enzyme adenosine deaminase acting on RNA (ADAR1) carries a
unique nuclear localization signal (NLS) that overlaps one of its double-stranded RNA …

Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation

J Lu, P Ge, MR Sawaya, MP Hughes, DR Boyer… - Journal of Biological …, 2024 - ASBMB
Heterogeneous nuclear ribonucleoprotein A2 (hnRNPA2) is a human ribonucleoprotein that
transports RNA to designated locations for translation via its ability to phase separate. Its …

Karyopherin-β2 recognition of a PY-NLS variant that lacks the proline-tyrosine motif

M Soniat, YM Chook - Structure, 2016 - cell.com
Summary Karyopherin-β2 or Transportin-1 binds proline-tyrosine nuclear localization
signals (PY-NLSs) in its cargos. PY-NLSs are described by structural disorder, overall …