The target of rapamycin (TOR) is a protein kinase that, by forming complexes with partner proteins, governs diverse cellular signalling networks to regulate a wide range of processes. TOR thus plays central roles in maintaining normal cellular functions and, when dysregulated, in diverse diseases. TOR forms two distinct types of multiprotein complexes (TOR complexes 1 and 2, TORC1 and TORC2). TORC1 and TORC2 differ in their composition, their control and their substrates, so that they play quite distinct roles in cellular physiology. Much effort has been focused on deciphering the detailed regulatory links within the TOR pathways and the structure and control of TOR complexes. In this review, we summarize recent advances in understanding mammalian (m) TORC2, its structure, its regulation, and its substrates, which link TORC2 signalling to the control of cell functions. It is now clear that TORC2 regulates several aspects of cell metabolism, including lipogenesis and glucose transport. It also regulates gene transcription, the cytoskeleton, and the activity of a subset of other protein kinases.
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Cover Image
Cover Image
A high-resolution crystal structure of the molybdenum insertase Cnx1E from Arabidopsis thaliana reveals two mutually exclusive molybdate binding sites, that have mechanistic implications for the Mo-insertion process into the pterin moiety of the molybdenum cofactor. In this issue of the Biochemical Journal, Kruse et al. found that molybdate is sequentially bound to the entry and the catalytically-productive site, going hand in hand with a distinct backbone conformation shift. In this image, adenylated molybdopterin and the two molybdate ions are shown in front of the Cnx1E active site. (Image provided by J. Krausze, W. A. Sassen and T. Kruse); for details see pages 1739–1753.
Who does TORC2 talk to?
Jianling Xie, Xuemin Wang, Christopher G. Proud; Who does TORC2 talk to?. Biochem J 31 May 2018; 475 (10): 1721–1738. doi: https://doi.org/10.1042/BCJ20180130
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