Integration of nutritional and stress signaling pathways by Maf1.
Repression of RNA polymerase III transcription under many conditions requires Maf1, a yeast protein with close sequence homologs in all eukaryotes. Three recent studies have identified key aspects of Maf1 regulation, which suggest that Maf1 integrates the responses from convergent nutritional and stress signaling pathways. These new findings indicate that the opposing actions of protein kinase A and protein phosphatase 2A alter the phosphorylation state of Maf1 and thereby regulate its localization and repressing activity.
Willis
Ian M
IM
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. willis@aecom.yu.edu
Moir
Robyn D
RD
D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D019913:Nuclear Localization Signals; D018384:Oxidative Stress; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D054648:Protein Phosphatase 2; D012320:RNA Polymerase III / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic
C104954:MAF1 protein, S cerevisiae; D019913:Nuclear Localization Signals; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D017868:Cyclic AMP-Dependent Protein Kinases; D012320:RNA Polymerase III; D010749:Phosphoprotein Phosphatases; D054648:Protein Phosphatase 2