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. 2021 Feb 10;220(4):e201912060. doi: 10.1083/jcb.201912060

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© 2021 Chang et al.

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Figure 4. — TORC1 phosphorylates Scd6. (A) In vitro kinase assay screen for 15 mRNA-binding proteins that interact with TORC1. (B) In vitro kinase assay using a temperature-sensitive mutant of Kog1, kog1-105. Kog1 was immunoprecipitated from lysates of cells and incubated with E. coli–purified Scd6. The relative ratio of phosphorylated Scd6 to total Scd6 was calculated, and the mean ± SD of triplicate experiments is shown below each lane. (C) In vitro kinase assay under rapamycin treatment. Tor1 was immunoprecipitated from cell lysates that were extracted from mock or rapamycin-treated cells. (D) In vitro kinase assay with the C-terminal fragment of Scd6 (amino acids 201–349). 3A indicates a mutant of Scd6(201–349) in which S256, S280, and S287 residues were replaced with Ala.