4lpa
Crystal structure of a Cdc6 phosphopeptide in complex with Cks1Crystal structure of a Cdc6 phosphopeptide in complex with Cks1
Structural highlights
FunctionCKS1_YEAST Binds to the catalytic subunit of the cyclin dependent kinase (CDC28) and is essential for its biological function. Publication Abstract from PubMedCks is an evolutionarily conserved protein that regulates cyclin-dependent kinase (CDK) activity. Clarifying the underlying mechanisms and cellular contexts of Cks function is critical because Cks is essential for proper cell growth, and its overexpression has been linked to cancer. We observe that budding-yeast Cks associates with select phosphorylated sequences in cell cycle-regulatory proteins. We characterize the molecular interactions responsible for this specificity and demonstrate that Cks enhances CDK activity in response to specific priming phosphosites. Identification of the binding consensus sequence allows us to identify putative Cks-directed CDK substrates and binding partners. We characterize new Cks-binding sites in the mitotic regulator Wee1 and discover a new role for Cks in regulating CDK activity at mitotic entry. Together, our results portray Cks as a multifunctional phosphoadaptor that serves as a specificity factor for CDK activity. Cks confers specificity to phosphorylation-dependent CDK signaling pathways.,McGrath DA, Balog ER, Koivomagi M, Lucena R, Mai MV, Hirschi A, Kellogg DR, Loog M, Rubin SM Nat Struct Mol Biol. 2013 Dec;20(12):1407-14. doi: 10.1038/nsmb.2707. Epub 2013, Nov 3. PMID:24186063[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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