TIP41 interacts with TAP42 and negatively regulates the TOR signaling pathway

Jacinto, E., Guo, B., Arndt, K. T., Schmelzle, T., Hall, M. N. (November 2001) TIP41 interacts with TAP42 and negatively regulates the TOR signaling pathway. Molecular Cell, 8 (5). pp. 1017-1026. ISSN 1097-2765

URL: http://www.ncbi.nlm.nih.gov/pubmed/11741537
DOI: 10.1016/S1097-2765(01)00386-0

Abstract

In Saccharomyces cerevisiae, the rapamycin-sensitive TOR kinases negatively regulate the type 2A-related phosphatase SIT4 by promoting the association of this phosphatase with the inhibitor TAP42. Here, we describe TIP41, a conserved TAP42-interacting protein involved in the regulation of SIT4. Deletion of the TIP41 gene confers rapamycin resistance, suppresses a tap42 mutation, and prevents dissociation of SIT4 from TAP42. Furthermore, a TIP41 deletion prevents SIT4-dependent events such as dephosphorylation of the kinase NPR1 and nuclear translocation of the transcription factor GLN3. Thus, TIP41 negatively regulates the TOR pathway by binding and inhibiting TAP42. The binding of TIP41 to TAP42 is stimulated upon rapamycin treatment via SIT4-dependent dephosphorylation of TIP41, suggesting that TIP41 is part of a feedback loop that rapidly amplifies SIT4 phosphatase activity under TOR-inactivating conditions.

Item Type: Paper
Uncontrolled Keywords: PROTEIN PHOSPHATASE 2A SACCHAROMYCES-CEREVISIAE TRYPTOPHAN PERMEASE CATALYTIC SUBUNIT CELL-GROWTH RAPAMYCIN YEAST ALPHA-4 DEGRADATION EXPRESSION
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
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: November 2001
Date Deposited: 22 Jan 2014 16:17
Last Modified: 22 Jan 2014 16:17
Related URLs:
URI: https://repository.cshl.edu/id/eprint/29255

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