Exact(1)
We documented elsewhere using Phos-tag gel mobility shift that Ypk1 phosphorylation at T662, one of its well-characterized TORC2 sites, is eliminated when cells are subjected to hyperosmotic shock for 10 min (Lee et al., 2012), and the same effect is observed using a specific antibody (Niles et al., 2012) that monitors phosphorylation of Ypk1 at the same site.
Similar(59)
To investigate this, we monitored phosphorylation of the Nodal intracellular signal transducer Smad2 in oep mutants with a normal or down regulated expression of rasl11b.
JNK activation was determined by monitoring phosphorylation of JNK (Thr183 and Tyr185) and c-Jun (Ser63), which is a substrate of JNK.
Confluent BAEC were stimulated with 5 mM 2-DG for 5 to 120 min, and AMPK activation was measured by monitoring phosphorylation of AMPKα-Thr172.
Using both untransfected and transfected cells, we monitored phosphorylation of STAT1 and STAT2 under the same experimental conditions as in Figure 3B.
To determine if low pH enhances F− -mediated stress, we treated LS8 cells with F− at pH 6.6 or pH 7.4 and monitored phosphorylation of JNK and c-jun.
JNK activation was determined by monitoring phosphorylation of JNK1 and total expression of this protein.
That inhibition was not observed strongly suggests that Met oxidation is not affecting our ability to monitor phosphorylation of Ser.
These observations were confirmed at protein level by monitoring phosphorylation of Stat3 and extracellular signal-related kinase (Erk) 1/2.
We also monitored phosphorylation of the transcriptional repressor Mig1p, which is targeted by Snf1p under low glucose conditions.
We also monitored phosphorylation of various Akt substrates, including PRAS40, FOXO1 and GSK3 using phosphospecific antibodies against Akt phosphorylation sites of these proteins.
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