SILAC-based phosphoproteomics reveals new PP2A-Cdc55-regulated processes in budding yeast.

ABSTRACT:

Background

Protein phosphatase 2A (PP2A) is a family of conserved serine/threonine phosphatases involved in several essential aspects of cell growth and proliferation. PP2ACdc55 phosphatase has been extensively related to cell cycle events in budding yeast; however, few PP2ACdc55 substrates have been identified. Here, we performed a quantitative mass spectrometry approach to reveal new substrates of PP2ACdc55 phosphatase and new PP2A-related processes in mitotic arrested cells.

Results

We identified 62 statistically significant PP2ACdc55 substrates involved mainly in actin-cytoskeleton organization. In addition, we validated new PP2ACdc55 substrates such as Slk19 and Lte1, involved in early and late anaphase pathways, and Zeo1, a component of the cell wall integrity pathway.

SUBMITTER: Baro B 

PROVIDER: S-EPMC5967524 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature