4.6 Review Book Chapter

Degradation of Activated Protein Kinases by Ubiquitination

Journal

ANNUAL REVIEW OF BIOCHEMISTRY
Volume 78, Issue -, Pages 435-475

Publisher

ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.013008.092711

Keywords

activation; downregulation; phosphorylation; ubiquitin

Funding

  1. National Cancer Institute [5R01CA109035]
  2. Pediatric Brain Tumor Foundation
  3. Brain Tumor Society Research
  4. Phi Beta Psi Sorority Research Grant
  5. The University of Texas M. D. Anderson Cancer Center
  6. National Cancer Institute grant [CA80100, CA82683, CA116402]
  7. NATIONAL CANCER INSTITUTE [R01CA082683, R01CA116402, R01CA080100, R01CA109035] Funding Source: NIH RePORTER

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Protein kinases are important regulators of intracellular signal transduction pathways and play critical roles in diverse cellular functions. Once a protein kinase is activated, its activity is subsequently downregulated through a variety of mechanisms. Accumulating evidence indicates that the activation of protein kinases commonly, initiates their downregulation via the ubiquitin/proteasome pathway. Failure to regulate protein kinase activity, or expression levels can cause human diseases.

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