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

RanBP3 influences interactions between CRM1 and its nuclear protein export substrates.

L Englmeier1, M Fornerod, F R Bischoff

  • 1European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.

EMBO Reports
|September 26, 2001
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

A theory on SARS-COV-2 susceptibility: reduced TLR7-activity as a mechanistic link between men, obese and elderly.

Journal of biological regulators and homeostatic agents·2020
Same author

MN1 overexpression is driven by loss of DNMT3B methylation activity in inv(16) pediatric AML.

Oncogene·2017
Same author

C-terminal BRE overexpression in 11q23-rearranged and t(8;16) acute myeloid leukemia is caused by intragenic transcription initiation.

Leukemia·2017
Same author

miR-139-5p controls translation in myeloid leukemia through EIF4G2.

Oncogene·2015
Same author

miR-9 is a tumor suppressor in pediatric AML with t(8;21).

Leukemia·2013
Same author

A new function of ROD1 in nonsense-mediated mRNA decay.

FEBS letters·2012

RanBP3 acts as a novel cofactor, enhancing CRM1-mediated nuclear export of proteins in eukaryotes. It stabilizes CRM1-export substrate interactions, facilitating cellular transport.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Transport

Background:

  • CRM1 (Chromosome Region Maintenance 1) is a key nuclear transport receptor.
  • CRM1 mediates the export of numerous proteins from the nucleus to the cytoplasm.
  • The precise mechanisms regulating CRM1-mediated export are not fully understood.

Purpose of the Study:

  • To investigate the role of RanBP3 (Ran-binding protein 3) in CRM1-mediated protein export.
  • To elucidate the mechanism by which RanBP3 interacts with CRM1 and influences substrate export.

Main Methods:

  • Biochemical assays to study protein interactions.
  • In vitro experiments using permeabilized cells to assess nuclear export.
  • Analysis of the effects of RanBP3 on CRM1-substrate binding affinities.

Related Experiment Videos

Main Results:

  • RanBP3 directly interacts with CRM1 and forms a trimeric complex with CRM1 and RanGTP.
  • RanBP3 does not bind CRM1 as an export substrate but stabilizes the CRM1-export substrate complex.
  • Nuclear RanBP3 stimulates CRM1-dependent protein export in vitro.
  • RanBP3 binding to CRM1 alters the receptor's affinity for different substrates.

Conclusions:

  • RanBP3 functions as a novel cofactor in the CRM1-mediated nuclear export pathway.
  • RanBP3 plays a critical role in the recognition and efficient export of specific CRM1 cargo proteins.
  • This discovery provides new insights into the regulation of nuclear transport.