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. Author manuscript; available in PMC: 2014 Jun 1.
Published in final edited form as: Nat Struct Mol Biol. 2013 Nov 3;20(12):10.1038/nsmb.2706. doi: 10.1038/nsmb.2706

Figure 7. Cks1 differentially stimulates the phosphorylation of various sites in Stb1, Ndd1 and Swi5.

Figure 7

Purified cyclin-Cdk1 complexes with either Cks1wt or Cks1mut were used for phosphorylation of recombinant Stb1, Ndd1 and Swi5. The relative abundance of proteolytic phosphopeptides was analyzed using quantitative mass-spectrometry. The kinase reactions with Cks1wt or Cks1mut were supplemented with [16O]-ATP or [18O]-ATP, respectively, which allowed the detection of the phospho-peptides by the isotope shift (for further experimental details see the Online Methods section). (a, b, e, f, i, j) Examples of spectra showing the relative phosphorylation intensity of various phosphopeptides in reactions with Cks1wt or Cks1mut ([16O] and [18O], respectively); (c, g, k) Diagrams outlining the relative patterns of phosphopeptides obtained in the reactions with Cks1wt and Cks1mut; (d, h, l) Diagrams outlining Cks1-dependent docking networks in Stb1, Ndd1 and Stb1.