Inducible degradation-coupled phosphoproteomics identifies PP2A^Rts1 as a novel eisosome regulator.

ABSTRACT:

Introduction

Reversible protein phosphorylation is an abundant post-translational modification dynamically regulated by opposing kinases and phosphatases. Protein phosphorylation has been extensively studied in cell division, where waves of cyclin-dependent kinase activity, peaking in mitosis, drive the sequential stages of the cell cycle. Here we developed and employed a strategy to specifically probe kinase or phosphatase substrates at desired times or experimental conditions in the model organism Saccharomyces cerevisiae.

Methods

We combined auxin-inducible degradation (AID) with mass spectrometry-based phosphoproteomics, which allowed us to arrest physiologically normal cultures in mitosis prior to rapid phosphatase degradation and phosphoproteome analysis.

Res

SUBMITTER: DeMarco AG 

PROVIDER: S-EPMC11371571 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature