title: CDK6 binds and promotes the degradation of the EYA2 protein.
abstract: Cyclin-dependent kinase 6 (Cdk6) is a D-Cyclin-activated kinase that is directly involved in driving the cell cycle through inactivation of pRB in G₁ phase. Increasingly, evidence suggests that CDK6, while directly driving the cell cycle, may only be essential for proliferation of specialized cell types, agreeing with the notion that CDK6 also plays an important role in differentiation. Here, evidence is presented that CDK6 binds to and promotes degradation of the EYA2 protein. The EYA proteins are a family of proteins that activate genes essential for the development of multiple organs, regulate cell proliferation, and are misregulated in several types of cancer. This interaction suggests that CDK6 regulates EYA2 activity, a mechanism that could be important in development and in cancer.
authors.affiliation: Department of Biology; Connecticut College; New London, CT USA.
authors.forename: Dawn
authors.initials: D
authors.lastname: Kohrt
authors.affiliation: Department of Biology; Connecticut College; New London, CT USA; Department of Developmental, Molecular, and Chemical Biology; Tufts University School of Medicine, and Molecular Oncology Research Institute; Tufts Medical Center; Boston, MA USA.
authors.forename: Jennifer
authors.initials: J
authors.lastname: Crary
authors.affiliation: Department of Chemistry; Connecticut College; New London, CT USA.
authors.forename: Marc
authors.initials: M
authors.lastname: Zimmer
authors.affiliation: Department of Pharmacology; University of Colorado School of Medicine; Aurora, CO USA.
authors.forename: Aaron N
authors.initials: AN
authors.lastname: Patrick
authors.affiliation: Department of Pharmacology; University of Colorado School of Medicine; Aurora, CO USA.
authors.forename: Heide L
authors.initials: HL
authors.lastname: Ford
authors.affiliation: Department of Developmental, Molecular, and Chemical Biology; Tufts University School of Medicine, and Molecular Oncology Research Institute; Tufts Medical Center; Boston, MA USA.
authors.forename: Philip W
authors.initials: PW
authors.lastname: Hinds
authors.affiliation: Department of Biology; Connecticut College; New London, CT USA.
authors.forename: Martha J
authors.initials: MJ
authors.lastname: Grossel
mesh_terms: D002453:Cell Cycle / Q000235:genetics; D002454:Cell Differentiation / Q000235:genetics; D049109:Cell Proliferation; D051361:Cyclin-Dependent Kinase 6 / Q000235:genetics / Q000378:metabolism*; D016193:G1 Phase / Q000235:genetics*; D057809:HEK293 Cells; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism*; D009369:Neoplasms / Q000235:genetics; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D017027:Protein Tyrosine Phosphatases / Q000235:genetics / Q000378:metabolism*; D059748:Proteolysis
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D009687:Nuclear Proteins; C495911:CDK6 protein, human; D051361:Cyclin-Dependent Kinase 6; C106938:EYA2 protein, human; D017027:Protein Tyrosine Phosphatases
keywords: Cdk6; EYA2; cancer; cell cycle; degradation; progenitor cell; proliferation