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TOR Signaling in Growth and Metabolism
Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control.
A colorectal cancer classification system that associates cellular phenotype and responses to therapy
Three subtypes have markedly better disease-free survival (DFS) after surgical resection, suggesting these patients might be spared from the adverse effects of chemotherapy when they have localized disease.
Important role of the LKB1-AMPK pathway in suppressing tumorigenesis in PTEN-deficient mice.
The results demonstrate the potential of AMPK activators, such as clinically approved metformin, as anticancer agents, which will suppress tumour development by triggering a physiological signalling pathway that potently inhibits cell growth.
Tor2 Directly Phosphorylates the AGC Kinase Ypk2 To Regulate Actin Polarization
It is proposed that Ypk protein kinases are direct and essential targets ofTORC2, coupling TORC2 to the cell integrity cascade.
Molecular Organization of Target of Rapamycin Complex 2*
- S. Wullschleger, R. Loewith, W. Oppliger, M. Hall
- Biology, ChemistryJournal of Biological Chemistry
- 2 September 2005
It is demonstrated that mammalian TOR is also oligomeric, likely a TORC2-TORC2 dimer, and the architecture of TorC2 is discussed in the context of TORC 2 assembly and regulation.
Identification of Protor as a novel Rictor-binding component of mTOR complex-2.
It is shown that detergents such as Triton X-100 or n-octylglucoside dissociate mTOR and mLST8 from a complex of Protor-1, Sin1 and Rictor, and that ProtOr-1 is not required for the assembly of other mTORC2 subunits into a complex.
Mutation of the PDK1 PH Domain Inhibits Protein Kinase B/Akt, Leading to Small Size and Insulin Resistance
- J. Bayascas, S. Wullschleger, D. Alessi
- Biology, ChemistryMolecular and Cellular Biology
- 17 March 2008
How reduced activation of PKB isoforms impinges on downstream signaling pathways, causing diminution of size as well as insulin resistance is revealed, establishing the importance of the PDK1-phosphoinositide interaction in enabling PKB to be efficiently activated with an animal model.
Protor-1 is required for efficient mTORC2-mediated activation of SGK1 in the kidney.
- Laura R. Pearce, E. Sommer, K. Sakamoto, S. Wullschleger, D. Alessi
- BiologyThe Biochemical journal
- 15 May 2011
Results suggest that Protor-1 may play a role in enabling mTORC2 to efficiently activate SGK1, at least in the kidney.
Regulation of the polarity kinases PAR-1/MARK by 14-3-3 interaction and phosphorylation
- O. Göransson, M. Deák, S. Wullschleger, N. Morrice, A. Prescott, D. Alessi
- Biology, ChemistryJournal of Cell Science
- 1 October 2006
It is demonstrated that 14-3-3 binding to MARK3 is dependent on phosphorylation, and necessitates the phosphate-binding pocket of 14-2-3, and that there are significant differences in the subcellular localisation of MARK isoforms, as well as in the impact that atypical PKC overexpression has on 14- 3-3binding and localisation.