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

Cdc2-mediated modulation of pp60c-src activity

D R Stover1, J Liebetanz, N B Lydon

  • 1Research Department, Ciba-Geigy Ltd., Basel, Switzerland.

The Journal of Biological Chemistry
|October 28, 1994
PubMed
Summary

Cell division kinase Cdc2 partially reactivates Csk-inactivated pp60c-src, enhancing its subsequent dephosphorylation and full reactivation. This suggests Cdc2 regulates pp60c-src activity during mitosis.

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

Recent advances in protein kinase inhibition: current molecular scaffolds used for inhibitor synthesis.

Current opinion in drug discovery & development·2009
Same author

Effect of polymorphisms on the replicative capacity of protease inhibitor-resistant HIV-1 variants under drug pressure.

Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases·2004
Same author

Efficacy and safety of a specific inhibitor of the BCR-ABL tyrosine kinase in chronic myeloid leukemia.

The New England journal of medicine·2001
Same author

Abl protein-tyrosine kinase inhibitor STI571 inhibits in vitro signal transduction mediated by c-kit and platelet-derived growth factor receptors.

The Journal of pharmacology and experimental therapeutics·2000
Same author

Lessons learned from the development of an abl tyrosine kinase inhibitor for chronic myelogenous leukemia.

The Journal of clinical investigation·2000
Same author

The structure-based design of ATP-site directed protein kinase inhibitors.

Current medicinal chemistry·1999

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • p60c-src is a proto-oncogene tyrosine kinase.
  • Its activity is regulated by phosphorylation at Tyr-527.
  • Csk phosphorylates Tyr-527, inactivating p60c-src.

Purpose of the Study:

  • To investigate the regulatory role of other kinases and phosphatases on Csk-inactivated p60c-src.
  • To explore the interaction between Cdc2, CD45, and p60c-src phosphorylation.

Main Methods:

  • Purified p60c-src was dephosphorylated and rephosphorylated with Csk.
  • Csk-inactivated p60c-src was treated with Cdc2, CD45, or a phosphopeptide.
  • Changes in p60c-src activity and Tyr-527 phosphorylation were analyzed.

Main Results:

  • Cdc2 phosphorylation partially reactivated Csk-inactivated p60c-src without Tyr-527 dephosphorylation.
  • Cdc2 treatment facilitated subsequent reactivation by CD45 or a phosphopeptide.
  • Cdc2 phosphorylation increased accessibility of the Src homology 2 domain and Tyr-527 dephosphorylation.

Conclusions:

  • Cdc2 plays a role in the regulation of pp60c-src activity.
  • Cdc2-mediated phosphorylation primes pp60c-src for further regulation by phosphatases.
  • These findings suggest a role for Cdc2 in pp60c-src regulation during mitosis.

Related Experiment Videos