PKC-mediated phosphorylation governs the stability and function of CELF1 as a driver of EMT in breast epithelial cells.

ABSTRACT: Epithelial to mesenchymal transition (EMT) is believed to be a principal factor contributing to cancer metastasis. The post-transcriptional and post-translational mechanisms underlying EMT are comparatively underexplored. We previously demonstrated that the CELF1 RNA binding protein is necessary and sufficient to drive the EMT of breast epithelial cells, and that the relative protein expression of CELF1 in this context was dictated at the post-translational level. Here, we elucidate the mechanism of this regulation. Mass spectrometric analysis of CELF1 isolated from mesenchymal MCF-10A cells identified multiple sites of serine and threonine phosphorylation on the protein, correlating with the increased stability of this protein in this cellular state. Analysis of phosphomimetic and serine/

SUBMITTER: Massey S 

PROVIDER: S-EPMC11585768 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature