HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

Detection of a novel quiescence-dependent protein kinase.

Abstract
We have identified a cell quiescence-specific 33-kDa cytoplasmic protein kinase (p33(QIK), Quiescence-Induced Kinase) based on induction of p33(QIK)-specific kinase activity of cells growth-arrested in the quiescent phase and deactivation upon entry into the cell cycle. Blockage of macromolecular synthesis prevents p33(QIK) from deactivation, indicating a requirement of newly synthesized regulators for deactivation of p33(QIK) during G(0)/G(1) transition. Stress shock induces additional increases of p33(QIK) activity in a quiescence-dependent manner that correlates with induction of apoptosis. Using a specific antibody to Krs1/Mst2 protein, we found that p33(QIK) is related to p63(Krs1) and is distinguishable from a 36-kDa protein kinase, which is induced through proteolytic modification of activated p63(Krs1) in proliferating cells undergoing apoptosis. p33(QIK) is constantly expressed in quiescent, proliferating, and apoptotic quiescent cells. Regulation of p33(QIK) activity involves protein phosphorylation/dephosphorylation in a proteolysis-independent manner. Regulation of p33(QIK) and related p63(Krs1) and p36 appears to involve distinct pathways in quiescent and proliferating cells, respectively. Our results illustrate the relevance of p33(QIK) activity for cell quiescence that may provide a new insight into signaling pathways regulated in cells during quiescence and quiescence-related apoptosis.
AuthorsH C Wang, K A Fecteau
JournalThe Journal of biological chemistry (J Biol Chem) Vol. 275 Issue 33 Pg. 25850-7 (Aug 18 2000) ISSN: 0021-9258 [Print] United States
PMID10840030 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Anti-Bacterial Agents
  • Antibiotics, Antineoplastic
  • Depsipeptides
  • Peptides, Cyclic
  • Recombinant Proteins
  • romidepsin
  • Protein Kinases
  • quiescence-induced kinase
  • Protein Serine-Threonine Kinases
  • STK3 protein, human
  • Serine-Threonine Kinase 3
  • Stk3 protein, mouse
  • Phosphoprotein Phosphatases
  • PTPRU protein, human
  • Protein Tyrosine Phosphatases
  • Ptpru protein, mouse
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2
  • CASP3 protein, human
  • Casp3 protein, mouse
  • Caspase 3
  • Caspases
Topics
  • 3T3 Cells
  • Animals
  • Anti-Bacterial Agents (pharmacology)
  • Antibiotics, Antineoplastic (pharmacology)
  • Apoptosis
  • Blotting, Western
  • Caspase 3
  • Caspases (metabolism)
  • Cell Cycle
  • Cell Division
  • Cytosol (enzymology)
  • Depsipeptides
  • Enzyme Activation (drug effects)
  • Enzyme Induction (drug effects)
  • Flow Cytometry
  • Humans
  • Mice
  • Peptides, Cyclic
  • Phosphoprotein Phosphatases (metabolism)
  • Phosphorylation
  • Protein Kinases (chemistry, metabolism)
  • Protein Serine-Threonine Kinases (metabolism)
  • Protein Tyrosine Phosphatases (metabolism)
  • Receptor-Like Protein Tyrosine Phosphatases, Class 2
  • Recombinant Proteins (metabolism)
  • Serine-Threonine Kinase 3
  • Signal Transduction
  • Stress, Physiological

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: