Abstract
In this review, we provide recent data on the role of mTOR kinase in the brain under physiological conditions and after damage, with a particular focus on cerebral ischemia. We cover the upstream and downstream pathways that regulate the activation state of mTOR complexes. Furthermore, we summarize recent advances in our understanding of mTORC1 and mTORC2 status in ischemia–hypoxia at tissue and cellular levels and analyze the existing evidence related to two types of neural cells, namely glia and neurons. Finally, we discuss the potential use of mTORC1 and mTORC2 as therapeutic targets after stroke.
Highlights
Departamento de Biología (Fisiología Animal), Facultad de Ciencias, Universidad Autónoma de Madrid, Centro de Biología Molecular “Severo Ochoa” (CBMSO), Universidad Autónoma de Madrid/CSIC, 28049 Madrid, Spain
One of the most remarkable characteristics of mTORCs, especially mTORC1, is that of the most remarkable characteristics ofas mTORCs, especially mTORC1, is that theseOne complexes are cellular energy sensors, and such they act as signal convergence these complexes are cellular energy sensors, and as such they act as signal convergence centers from extra- and intra-cellular “energetic factors”
This overactivation of autophagy is probably triggered by a dramatic decrease in mTORC1 activity through the upregulation of AMPK and downregulation of the phosphoinositide 3-kinase (PI3K)/Akt pathway induced by the ischemic conditions
Summary
Mammalian/mechanistic target of rapamycin (mTOR) is a 289 kDa serine–threonine kinase and a key element of two mTOR complexes called mTORC1 and mTORC2 (mTORCs) [1–4]. Akt substrate kDa) are specific subunits of mTORC1, exclusive to mTORC2 [7] (Figure 1) All of these proteins have different functions in the while Rictor (rapamycin-insensitive companion of mTOR), mSin, and Protor1/2 are excomplexes. Do they have structural functions (stabilizing the complexes and clusive to mTORC2 [7] (Figure 1). All of these proteins have different functions in the recruiting mTOR substrates) but they contribute to regulating mTOR activity. Recent studies demonstrate an post-translational modifications of some of the companion proteins, mainly by important impact in the fine-tuned activity of mTOR kinase, according to post-translational phosphorylation. 4 of its localization in lysosome membranes (see Section 1.2.3.) [31]
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