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

Microtubule binding to Smads may regulate TGF beta activity.

C Dong1, Z Li, R Alvarez

  • 1Department of Internal Medicine, College of Medicine and Public Health, Ohio State University, Columbus 43210, USA.

Molecular Cell
|March 11, 2000
PubMed
Summary

Microtubules (MTs) sequester Smad proteins in the cytoplasm. Disrupting MTs enhances TGF-beta signaling, revealing MTs as negative regulators of this crucial cellular pathway.

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

First Measurement of Time-Dependent CP Violation in the Flavor-Changing Neutral-Current Decay B^{0}→K_{S}^{0}μ^{+}μ^{-}.

Physical review letters·2026
Same author

Measurement of the Top-Quark Production Cross Section and Charge Asymmetry at LHCb.

Physical review letters·2026
Same author

Searches for B^{0}→K^{+}π^{-}τ^{+}τ^{-} and B_{s}^{0}→K^{+}K^{-}τ^{+}τ^{-} Decays.

Physical review letters·2026
Same author

First Evidence of the B_{s}^{0}→K^{-}π^{+}γ Decay.

Physical review letters·2026
Same author

Precision Measurement of CP Violation and Branching Fractions in B^{±}→K_{S}^{0}h^{±} (h=π, K) Decays and Search for the Rare Decay B_{c}^{±}→K_{S}^{0}K^{±}.

Physical review letters·2026
Same author

First Observation of the B[over ¯]_{s}^{0}→Λ_{c}^{+}Λ[over ¯]_{c}^{-} Decay and Evidence for the B[over ¯]^{0}→Λ_{c}^{+}Λ[over ¯]_{c}^{-} Decay.

Physical review letters·2026

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Smad proteins are key intracellular mediators in the Transforming Growth Factor-beta (TGF-beta) superfamily signaling pathway.
  • The precise mechanisms regulating Smad protein localization and activation remain incompletely understood.

Purpose of the Study:

  • To investigate the interaction between Smad proteins and microtubules (MTs).
  • To elucidate the role of MTs in the regulation of TGF-beta/Smad signaling.

Main Methods:

  • Co-immunoprecipitation and immunofluorescence to detect Smad-MT interactions in various cell lines.
  • Treatment with TGF-beta to observe Smad dynamics.
  • Disruption of the MT network using pharmacological agents (nocodazole, colchicine) and a tubulin mutant.

Related Experiment Videos

  • Assessment of Smad2/3 phosphorylation and transcriptional activity in response to TGF-beta stimulation and MT destabilization.

    • Main Results:

    • Endogenous Smad2, Smad3, and Smad4 proteins were found to bind to microtubules (MTs) in multiple cell lines, independent of TGF-beta stimulation.
    • TGF-beta stimulation induced the dissociation of Smad2 and Smad3 from MTs, followed by their phosphorylation and nuclear translocation, leading to transcriptional activation in CCL64 cells.
    • Disruption of the MT network significantly enhanced TGF-beta-induced Smad2 phosphorylation and transcriptional responses in CCL64 cells.

    Conclusions:

    • Microtubules act as a cytoplasmic sequestration network for Smad proteins.
    • MTs negatively regulate TGF-beta signaling by controlling Smad2 interaction with and phosphorylation by the TGF-beta receptor I.
    • This study reveals a novel regulatory mechanism for TGF-beta pathway function involving the microtubule cytoskeleton.