Gankyrin Is an Ankyrin-repeat Oncoprotein That Interacts with CDK4 Kinase and the S6 ATPase of the 26 S Proteasome*
Date
2002
Authors
Dawson, Simon
Apcher, Sebastien
Mee, Maureen
Higashitsuji, Hiroaki
Baker, Rohan
Uhle, Stefan
Dubiel, Wolfgang
Fujita, Jun
Mayer, R. John
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American Society for Biochemistry and Molecular Biology Inc
Abstract
A yeast two-hybrid screen with the human S6 (TBP7, RPT3) ATPase of the 26 S proteasome has identified gankyrin, a liver oncoprotein, as an interacting protein. Gankyrin interacts with both free and regulatory complex-associated S6 ATPase and is not stably associated with the 26 S particle. Deletional mutagenesis shows that the C-terminal 78 amino acids of the S6 ATPase are necessary and sufficient to mediate the interaction with gankyrin. Deletion of an orthologous gene in Saccharomyces cerevisiae suggests that it is dispensable for cell growth and viability. Overexpression and precipitation of tagged gankyrin from cultured cells detects a complex containing co-transfected tagged S6 ATPase (or endogenous S6) and endogenous cyclin D-dependent kinase CDK4. The proteasomal ATPases are part of the AAA (ATPases associated with diverse cellular activities) family, members of which are molecular chaperones; gankyrin complexes may therefore influence CDK4 function during oncogenesis.
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Keywords: Adenosinetriphosphate; Cell culture; Genes; Mutagenesis; Precipitation (chemical); Proteins; Yeast; Cell growths; Biochemistry; adenosine triphosphatase; amino acid; ankyrin; chaperone; cyclin dependent kinase 4; gankyrin; oncoprotein; proteasome; S6 kina
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Journal of Biological Chemistry
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Journal article
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2037-12-31
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