RRC ID 28091
Author Zhang MM, Wu PY, Kelly FD, Nurse P, Hang HC.
Title Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast.
Journal PLoS Biol
Abstract Protein S-palmitoylation, a lipid modification mediated by members of the palmitoyltransferase family, serves as an important membrane-targeting mechanism in eukaryotes. Although changes in palmitoyltransferase expression are associated with various physiological and disease states, how these changes affect global protein palmitoylation and cellular function remains unknown. Using a bioorthogonal chemical reporter and labeling strategy to identify and analyze multiple cognate substrates of a single Erf2 palmitoyltransferase, we demonstrate that control of Erf2 activity levels underlies the differential modification of key substrates such as the Rho3 GTPase in vegetative and meiotic cells. We show further that modulation of Erf2 activity levels drives changes in the palmitoylome as cells enter meiosis and affects meiotic entry. Disruption of Erf2 function delays meiotic entry, while increasing Erf2 palmitoyltransferase activity triggers aberrant meiosis in sensitized cells. Erf2-induced meiosis requires the function of the Rho3 GTPase, which is regulated by its palmitoylation state. We propose that control of palmitoyltransferase activity levels provides a fundamental mechanism for modulating palmitoylomes and cellular functions.
Volume 11(7)
Pages e1001597
Published 2013-7-1
DOI 10.1371/journal.pbio.1001597
PMID 23843742
PMC PMC3699447
MeSH Lipoylation / physiology* Meiosis / physiology Schizosaccharomyces / cytology* Schizosaccharomyces / metabolism*
IF 7.076
Times Cited 39
DNA material pDUAL-YFH41c (RDB06152)