Research Perspectives:
Mutant Cbl proteins as oncogenic drivers in myeloproliferative disorders
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Abstract
1 Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE
2 Department of Genetics, Cell Biology and Anatomy, College of Medicine, University of Nebraska Medical Center, Omaha, NE
3 Department of Biochemistry & Molecular Biology, College of Medicine, University of Nebraska Medical Center, Omaha, NE
4 Department of Pharmaceutical Sciences, College of Pharmacy, University of Nebraska Medical Center, Omaha, NE
5 Dana Farber Cancer Institute, Harvard Medical School, Boston, MA
Keywords: Cbl, E3 ubiquitin ligase, leukemia, protein tyrosine kinase, signal transduction
Received: March 7, 2011; Accepted: March 20, 2011; Published: March 20, 2011;
Correspondence:
Mayumi Naramura, e-mail:
Hamid Band, e-mail:
Abstract
Casitas B-lineage lymphoma (Cbl) family proteins are evolutionarily-conserved attenuators of protein tyrosine kinase (PTK) signaling. Biochemical analyses over the past two decades have firmly established that the negative regulatory functions of Cbl proteins are mediated through their ability to facilitate ubiquitination and thus promote degradation of PTKs. As aberrant activation of PTKs is frequently associated with oncogenesis, it has long been postulated that loss of normal Cbl functions may lead to unregulated activation of PTKs and cellular transformation. In the last few years, mutations in the CBL gene have been identified in a subset of human patients with myeloid malignancies. Here we discuss insights gained from the analyses of Cbl mutants both in human patients and in animal models and propose potential mechanisms of oncogenesis through this pathway.
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