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

Premature p34cdc2 activation required for apoptosis

L Shi1, W K Nishioka, J Th'ng

  • 1Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Canada.

Science (New York, N.Y.)
|February 25, 1994
PubMed
Summary

Premature activation of the cell cycle kinase p34cdc2 triggers apoptosis, leading to DNA fragmentation and nuclear collapse. Inhibiting this kinase prevents cell death, suggesting a general mechanism for nuclear disruption during apoptosis.

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

Casein kinase 2 phosphorylates and induces the SALL2 tumor suppressor degradation in colon cancer cells.

Cell death & disease·2024
Same author

In vitro molecular magnetic resonance imaging detection and measurement of apoptosis using superparamagnetic iron oxide + antibody as ligands for nucleosomes.

Physics in medicine and biology·2012
Same author

An improved double-beam infrared microspectrometer.

Applied optics·2010
Same author

Orienting rigid and flexible biological assemblies in ferrofluids for small-angle neutron scattering studies.

Biophysical journal·2009
Same author

Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival.

Cellular and molecular life sciences : CMLS·2009
Same author

Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution.

Journal of molecular biology·2006

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The serine-threonine kinase p34cdc2 plays a critical role in cell cycle regulation.
  • Aberrant activation of p34cdc2 can induce cell death pathways.
  • Apoptosis, or programmed cell death, involves specific molecular events leading to cell dismantling.

Purpose of the Study:

  • To investigate the role of p34cdc2 activation in apoptosis.
  • To determine if premature p34cdc2 activation is a requirement for apoptosis.
  • To elucidate the mechanism by which p34cdc2 contributes to nuclear disruption during cell death.

Main Methods:

  • Utilizing a lymphocyte granule protease model to induce apoptosis.
  • Monitoring p34cdc2 activation, including tyrosine dephosphorylation.

Related Experiment Videos

  • Employing excess peptide substrate to block kinase activity.
  • Using a temperature-sensitive mutant to inactivate p34cdc2.

    • Main Results:

    • Premature activation of p34cdc2 was essential for apoptosis induced by the protease.
    • Rapid p34cdc2 activation and tyrosine dephosphorylation occurred at apoptosis initiation.
    • Blocking p34cdc2 activity prevented DNA fragmentation and nuclear collapse.
    • Inactivating p34cdc2 in a mutant also inhibited these apoptotic features.

    Conclusions:

    • Premature p34cdc2 activation is a key event in initiating apoptosis.
    • This kinase activation is involved in the nuclear dismantling characteristic of apoptosis.
    • p34cdc2 may represent a general mechanism for inducing nuclear disruption in apoptotic cells.