Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases

Di Como, C. J., Arndt, K. T. (August 1996) Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes and Development, 10 (15). pp. 1904-16. ISSN 0890-9369 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/8756348
DOI: 10.1101/gad.10.15.1904

Abstract

We identified an essential Saccharomyces cerevisiae protein, Tap42, that associates with Sit4, a type 2A-related protein phosphatase, and with the type 2A phosphatase catalytic subunits. The association of Tap42 with the phosphatases does not require the previously identified phosphatase subunits. Genetic analysis suggests that Tap42 functions positively with both phosphatases. Mutations in TAP42 can confer almost complete rapamycin resistance. In addition, Tap42/Sit4 and Tap42/PP2A complex formation is regulated by nutrient growth signals and the rapamycin-sensitive Tor signaling pathway. These findings, combined with the defect in translation of the tap42-11 mutant at the nonpermissive temperature, suggest that Tap42, Sit4, and PP2A are components of the Tor signaling pathway.

Item Type: Paper
Uncontrolled Keywords: 1-Phosphatidylinositol 3-Kinase Amino Acid Sequence Cell Cycle Proteins/metabolism Culture Media Drug Resistance, Microbial/genetics Fungal Proteins/drug effects/genetics/ metabolism Gene Expression Regulation, Fungal Genes, Fungal Genes, Suppressor Molecular Sequence Data Mutation Phosphoprotein Phosphatase/drug effects/genetics/ metabolism Phosphoproteins/chemistry Phosphotransferases (Alcohol Group Acceptor)/drug effects/ genetics/metabolism Polyenes/pharmacology Precipitation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Saccharomyces cerevisiae/chemistry/drug effects/genetics Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Signal Transduction Sirolimus
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein phosphatase
organism description > yeast
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: 1 August 1996
Date Deposited: 22 May 2014 18:38
Last Modified: 22 May 2014 18:38
Related URLs:
URI: https://repository.cshl.edu/id/eprint/30157

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