Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Rules for nuclear localization sequence recognition by karyopherin beta 2.

Brittany J Lee1, Ahmet E Cansizoglu, Katherine E Süel

  • 1Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park, Dallas, TX 75390, USA.

Cell
|August 12, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

POSTN<sup>+</sup> CAFs facilitate gastric cancer peritoneal metastasis by promoting ICAM-1-dependent tumor cell adhesion and CD8<sup>+</sup> T-cell exhaustion.

Frontiers in immunology·2026
Same author

The effect of blood flow restriction combined with different resistance training on the improvement of athletic performance in male tactical personnel.

Frontiers in physiology·2026
Same author

Importin-9 recognizes the winged-helix fold of ETS transcription factors to mediate nuclear import.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

CliPepPI: Scalable prediction of domain-peptide specificity using contrastive learning.

bioRxiv : the preprint server for biology·2026
Same author

Multiple roads between the nucleus and the cytoplasm: classes of linear NLSs and NESs and their receptors.

Current opinion in structural biology·2026
Same author

Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026
Same journal

A viral ORFeome library for systems-level genetic dissection of host-pathogen interactions.

Cell·2026
Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026
Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026
Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026
Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026
Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026
See all related articles

Researchers identified rules for Karyopherin beta 2 (Kapbeta2) to recognize nuclear localization signals (NLSs). This discovery helps predict new Kapbeta2 substrates involved in nucleocytoplasmic transport.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Karyopherin beta (Kapbeta) proteins facilitate nucleocytoplasmic transport by binding nuclear localization signals (NLSs) and nuclear export signals (NESs).
  • Ran GTPase regulates this transport process through its nucleotide cycle.
  • Predicting novel Kapbeta substrates has been challenging due to the complexity of recognized signals.

Purpose of the Study:

  • To elucidate the mechanism of substrate displacement by Ran GTPase.
  • To define rules for Nuclear Localization Signal (NLS) recognition by Kapbeta2 (Transportin).
  • To identify new candidate Kapbeta2 substrates.

Main Methods:

  • Determined the structure of Kapbeta2 bound to the NLS of hnRNP A1.
  • Analyzed Kapbeta2-substrate interactions to derive NLS recognition rules.

Related Experiment Videos

  • Validated predictive rules by identifying and experimentally confirming new Kapbeta2 substrates.
  • Main Results:

    • The structure reveals how Ran GTPase displaces substrates from Kapbeta2.
    • Three key rules for Kapbeta2 NLS recognition were defined: structural disorder, basic character, and a specific C-terminal consensus sequence.
    • 81 new candidate Kapbeta2 substrates were identified, with five confirmed experimentally.

    Conclusions:

    • The study defines and validates a novel NLS recognition mechanism for Kapbeta2.
    • These findings provide a predictive framework for identifying new substrates of nucleocytoplasmic transport machinery.
    • The identified rules enable the discovery of NLSs not predictable by primary sequence analysis alone.