TORC2 plasma membrane localization is essential for cell viability and restricted to a distinct domain

Berchtold, Doris and Walther, Tobias C. (2009) TORC2 plasma membrane localization is essential for cell viability and restricted to a distinct domain. Molecular Biology of the Cell, 20 5: 1565-1575. doi:10.1091/mbc.E08-10-1001

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Author Berchtold, Doris
Walther, Tobias C.
Title TORC2 plasma membrane localization is essential for cell viability and restricted to a distinct domain
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2009-03-01
Sub-type Article (original research)
DOI 10.1091/mbc.E08-10-1001
Open Access Status File (Publisher version)
Volume 20
Issue 5
Start page 1565
End page 1575
Total pages 11
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Language eng
Formatted abstract
The conserved target of rapamycin (TOR) kinases regulate many aspects of cellular physiology. They exist in two distinct complexes, termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2), that posses both overlapping and distinct components. TORC1 and TORC2 respond differently to the drug rapamycin and have different cellular functions: whereas the rapamycin-sensitive TORC1 controls many aspects of cell growth and has been characterized in great detail, the TOR complex 2 is less understood and regulates actin polymerization, cell polarity, and ceramide metabolism. How signaling specificity and discrimination between different input signals for the two kinase complexes is achieved is not understood. Here, we show that TORC1 and TORC2 have different localizations in Saccharomyces cerevisiae. TORC1 is localized exclusively to the vacuolar membrane, whereas TORC2 is localized dynamically in a previously unrecognized plasma membrane domain, which we term membrane compartment containing TORC2 (MCT). We find that plasma membrane localization of TORC2 is essential for viability and mediated by lipid binding of the C-terminal domain of the Avo1 subunit. From these data, we suggest that the TOR complexes are spatially separated to determine downstream signaling specificity and their responsiveness to different inputs.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Mon, 10 Sep 2012, 09:32:42 EST by Susan Allen on behalf of Institute for Molecular Bioscience