The authors of “Hcm1 integrates signals from Cdk1 and calcineurin to control cell proliferation” (Mol. Biol. Cell [2015] 26, 3570–3577; originally published in MBoC In Press as 10.1091/mbc.E15-07-0469) wish to make a correction to both Figure Figure 1A and Figure 2A. In both figures the phosphosites that are labeled “S69” should actually read “S66.” The corrected figures are below.
FIGURE 1:
Hcm1 phosphorylation affects cellular fitness. (A) Positions of Cdk1 phosphosites that activate (green) and destabilize Hcm1 (red). Mutations that block degradation lead to an increase in protein level (15A, 3N, 3N/16E); phosphomimetic mutations (16E, 3N/16E) lead to constitutive activity (CA). (B) Strains expressing PGK1-URA3 (blue lines) and PGK1-GFP-URA3 (red lines) were cocultured and the percentage of each strain in the population determined at the indicated time points. Average values ±1 SD of five to eight replicates.
FIGURE 2:
Hcm1 is dephosphorylated by calcineurin in vivo. (A) Diagram of Hcm1 mutants assayed in B–D, along with the number of Cdk1 (S/T-P) sites retained in each protein. (B) Yeast two-hybrid assay showing interaction between Hcm1 and Cna1. Deletion of the docking site (hcm1ΔPSIEIQ) disrupts the interaction. (C) Western blots comparing separation of Hcm1 proteins that contain different numbers of Cdk1 sites on a Phos-tag gel (top) and standard SDS–PAGE (bottom). (D) Phos-tag Western blot of strains expressing Hcm1-15A (15A, no Cdk1 sites), wild-type Hcm1 (WT), Hcm1ΔPSIEIQ (ΔP), or wild-type Hcm1 in a cnb1Δ strain assayed after the addition of CaCl2 for 10 min and compared with untreated control cells. (E) Hcm1 phosphorylation assayed as in D, except that cells were treated with FK506 or ET buffer for 1 h and then CaCl2 was added for 15 min.
The HTML and PDF versions were corrected on the Molecular Biology of the Cell website on November 13, 2015. These corrections may not appear on copies of the article that reside on other websites.