PMC:4349302 / 33397-34127 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4349302","sourcedb":"PMC","sourceid":"4349302","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4349302","text":"Flux rates correlate positively with respective protein abundances. Accordingly, highest fluxes are encountered for phosphorylation and dephosphorylation of PI4KIII β, followed by lower rates for PKD and CERT. Basal phosphorylation and dephosphorylation rates of PKD are two orders of magnitude higher than ceramide transfer dependent activation. The model also predicts that the majority of CERT molecules is unphosphorylated. However, the rates of phosphorylation and dephosphosphorylation are rather similar, indicating that dephosphorylation at the ER is very efficient. An uncertainty of several orders of magnitude is predicted for TGN bound CERT (CERTaTGN), suggesting that our data agrees with different TGN resting times.","tracks":[]}