Akt/PKB

Gene/Protein · 44 studies in the Atlas · also known as Akt, AKT, AKT1, PKB, protein kinase B, Akt Ser473

Key kinase downstream of PI3K in growth signalling; activated by PDK1 at T308 and further phosphorylated by mTORC2 at S473, which shapes which substrates it hits.

The main 'grow' relay from growth factors. A key signaling kinase that sits downstream of PI3K. It is switched on by PI3K signaling through PDK1, with mTORC2 adding a second mark that tunes what it does. It's one of the cell's central 'growth is good, keep going' signals.

T308 by PDK1 and S473 by mTORC2. Recruitment and activation are separate events – a distinction the older Atlas diagram blurred.

TL;DR. Akt/PKB appears in 44 curated studies in Oliver's mTOR Atlas: 1 in people (1 human study); 15 in animal models; 26 at the molecular level (cells, biochemistry, structure); 2 reviews. It has 5 interactions in the curated pathway model.

In the pathway model

5 interactions in the curated mTOR pathway model (3 acting from Akt/PKB, 2 acting on it). Each row is a claim with the evidence behind it; the evidence code is the kind of study, not its quality.

Interaction	Mechanism	Evidence	Studies
Akt/PKB inhibits PRAS40 mechanism: phosphorylation · this link in full · on the map table	Akt tags PRAS40, which then gets pulled away from mTORC1 – a second way insulin releases a brake.Akt phosphorylates PRAS40, which then gets sequestered away from mTORC1 - a second, parallel way insulin lifts a brake. Holds under: Three 2007 studies in cultured mammalian cells. Not tested in whole animals or in people, and how much this branch adds beside Akt's route through TSC2 is not measured. plausible in people, not shown directly · settled in the literature	M	SAN2007, VAN2007, OSH2007
Akt/PKB inhibits TSC1/TSC2 mechanism: phosphorylation · this link in full · on the map table	Akt tags TSC2 to disable it. Growth signals work by releasing a brake, not by pressing a gas pedal.Akt phosphorylates TSC2, disabling the complex. Growth-factor signalling works by removing a brake, not by pressing an accelerator. Holds under: In mouse liver, Akt phosphorylation of TSC2 is the main route by which insulin switches on mTORC1, but feeding activates hepatic mTORC1 without it; that response needs dietary protein instead (KAL2026). The biochemical mechanism itself was shown in cultured human cells (INO2002). plausible in people, not shown directly · settled in the literature	A	INO2002, KAL2026, LAP2026, MAN2002, POT2002
Akt/PKB inhibits FOXO1/3 mechanism: phosphorylation · this link in full · on the map table	Akt tags FOXO proteins and keeps them out of the nucleus; this specific link belongs to mTORC2, not mTORC1.Akt phosphorylates FOXO transcription factors and excludes them from the nucleus. Rictor or mLST8 deletion abolishes signalling to Akt–FOXO while sparing S6K1. Holds under: Mouse knockouts and cell lines; FOXO isoform contributions differ by tissue. This Akt output depends on mTORC2. Deleting rictor or mLST8 in mice removed Akt signalling to FOXO while S6K1 was spared (GUE2006), and SIN1, an essential mTORC2 subunit, controls Akt Ser473 phosphorylation and which substrates Akt reaches (JAC2006). The mTORC2-to-Akt step itself is the separate edge MTORC2-AKT. plausible in people, not shown directly · settled in the literature	M	GUE2006, JAC2006, BRU1999
mTORC2 activates Akt/PKB mechanism: phosphorylation · this link in full · on the map table	mTORC2 adds the final activating tag to Akt – the same step that long-term use of the drug rapamycin eventually disrupts. In mice, that disruption is a major reason long-term rapamycin raises blood sugar.mTORC2 puts the second, activating phosphate on Akt (Ser473). This is the step rapamycin eventually breaks, and a major reason, in mice, that chronic rapamycin impairs glucose tolerance (LAM2012). Holds under: Mammalian cell studies, cancer cells and one mouse and rat liver study (ARI2015). Ser473 phosphorylation is shown in cells. The glucose consequence of losing it comes from mouse work (LAM2012) and has not been measured in people. S473 contribution to Akt output is substrate-dependent: some Akt substrates are strongly mTORC2-dependent, others barely. plausible in people, not shown directly · settled in the literature	A	JAC2006, FRI2006, YAN2006, LIU2015, ROD2011, ARI2015, GAN2011, FAC2008, HAG2012
PI3K activates Akt/PKB mechanism: recruitment · this link in full · on the map table	That lipid pulls Akt to the cell membrane, where it gets switched on.PIP3 pulls Akt to the membrane, where it gets phosphorylated and activated. Holds under: Mammalian cell study (LIU2015) plus a review (CAN2002). Cell biochemistry; not tested in whole animals or in people by the cited sources. PIP3 recruits Akt; recruitment alone does not activate it. Full activation additionally needs PDK1 (T308) and mTORC2 (S473), so the strength of this link depends on the activity of both of those. plausible in people, not shown directly · settled in the literature	M	CAN2002, LIU2015

Evidence at a glance

Evidence	What it means	Studies
H	Human study	1
A	Animal model	15
M	Molecular — cells, biochemistry, structure	26
R	Review — secondary literature, not a new result	2

Studies

Year	Evidence	Study
2026	H	Pregnane X receptor-mediated liver growth: a controlled clinical trial in healthy volunteers and identification of the role of AKT-MTOR pathway in mouse. LASSILA2026 One week of rifampicin increased the liver volume-to-body-weight ratio by 2.7% in 16 healthy volunteers, and PXR activation enlarged the liver in male mice, accompanied by increased AKT-MTOR pathway activity, without YAP activation.
2026	A	mTOR inhibition augments antitumor immune effector response by reprogramming the TP53-mutant, immune-cold HNSCC tumor microenvironment NAT2026 In syngeneic TP53-mutant HNSCC mouse models, the mTOR inhibitor everolimus reprogrammed the immune-cold tumor microenvironment: it increased CD8+ T cell and dendritic cell infiltration, reduced Tregs and HIF-1α/VEGFA-driven MDSC recruitment, boosted TNF-α/CXCL10 chemokine signaling, and reduced PD-1/PD-L1 expression — restoring T-cell cytotoxic competence and suppressing tumor growth.
2026	A	Salvianolic Acid B Enhances Motor Function Recovery after Spinal Cord Injury in Association with AKT/mTOR/HIF-1α Pathway Activation and Angiogenesis. YAO2026 Salvianolic acid B improved motor recovery, neuronal survival and angiogenesis after rat spinal cord injury in association with AKT/mTOR/HIF-1α activation; the effects were reversed by the AKT inhibitor capivasertib.
2026	A	Dietary protein governs the role of insulin signaling in the postprandial regulation of hepatic mTORC1. KAL2026 In liver-specific mouse genetic models, AKT-mediated TSC2 phosphorylation is the main route by which insulin induces hepatic mTORC1, but is dispensable for feeding-induced activation; postprandial mTORC1 activation instead requires dietary protein, and hepatic mTORC1 signalling is not elevated in diet-induced obesity despite impaired insulin/glucose homeostasis.
2026	A	Novel mTORC1 Booster LAPTM4A Potentiates Pathological Cardiac Hypertrophy HU2026 Identifies LAPTM4A, a lysosomal transmembrane protein, as a novel booster of mTORC1 signaling in cardiomyocytes: LAPTM4A binds NEDD4L, driving K63-linked ubiquitination of AKT and downstream mTORC1-p70S6K/4EBP1-mediated protein synthesis, without affecting lysosomal autophagy. Cardiomyocyte-specific LAPTM4A deletion attenuated TAC-induced hypertrophy/fibrosis in mice; an FDA-approved-drug screen identified magnolol as a LAPTM4A suppressor with cardioprotective effect in vivo.
2026	A	LncRNA DLX6-AS1 promotes necroptosis through PI3K/AKT/mTOR signaling pathway in myocardial ischemia/reperfusion injury mice SU2026 LncRNA DLX6-AS1 activates PI3K/AKT/mTOR signaling to promote necroptosis in myocardial ischemia-reperfusion injury; inhibiting DLX6-AS1 suppresses necroptosis and protects cardiomyocytes.
2026	A	An ANGPTL8-AKT2-mTOR Axis Drives Adipose Senescence and Aging-Related Functional Decline HE2026 Identifies ANGPTL8 as an endocrine driver of adipose-tissue aging: circulating ANGPTL8 tracked with biological age and mortality risk in a large human cohort, and genetic deletion of Angptl8 in mice extended lifespan and reduced senescence markers. Mechanistically, ANGPTL8 binds AKT2 and drives the AKT-mTOR-S6K axis to promote adipocyte senescence; blocking that axis abolished the pro-senescent effect.
2026	A	Corilagin attenuates osteoarthritis progression by coordinating NF-κB inhibition with PI3K/AKT/mTOR-associated autophagy restoration. ZHOU2026B Corilagin restores chondrocyte autophagic flux and ECM synthesis by inhibiting PI3K/AKT/mTOR and NF-κB signalling, reducing cartilage erosion and OARSI scores in the mouse DMM osteoarthritis model.
2026	A	Impaired mTOR/SREBP1-Mediated Lipogenesis as a Mechanism of Hepatic Glycogen Accumulation in a Carnivorous Fish Model, Largemouth Bass (Micropterus salmoides) TAO2026 mTOR/SREBP1 signaling governs hepatic glucose partitioning; the insulin-responsive mTOR/SREBP1 axis promotes lipogenesis versus glycogen accumulation. In this model -- a carnivorous fish -- impairment of the axis is associated with hepatic glycogen overload mimicking glucose intolerance.
2026	A	Pungenin Promotes Hair Growth in Mouse Models of Androgenic Alopecia Through Transcriptional Regulation of the PI3K/AKT/mTOR Axis. ZHAI2026 Topical pungenin accelerated hair regrowth in DHT-induced androgenetic alopecia mice, reducing type II 5α-reductase expression and modulating PI3K/AKT/FoxO/mTOR transcriptional signalling in hair follicle cells.
2026	A	Anti-breast cancer effects of the Xingxiao Pill are associated with inhibition of the ErbB3/PI3K/AKT/mTOR pathway, modulation of amino acid metabolism, and promotion of apoptosis. ZHANG2026C Xingxiao Pill inhibited 4T1 breast cancer growth in vitro and in vivo by suppressing ErbB3/PI3K/AKT/mTOR signalling and reshaping amino acid metabolism; cinnamic acid and palmitic acid were identified as constituents that bind mTOR.
2026	A	Feeding-Induced Muscle mTORC1 Signaling Regulates Postprandial Protein Synthesis and Endurance but Not Muscle Size LAP2026 Using a mouse model expressing an AKT-nonphosphorylatable TSC2 mutant specifically in skeletal muscle, the Manning lab genetically separated feeding-induced from contraction-induced mTORC1 activation. AKT-mediated TSC2 phosphorylation is required for feeding (but not contraction) to activate muscle mTORC1 and drive postprandial protein synthesis — yet mice lacking this feeding-induced signal have normal muscle mass and myofiber size, and instead show improved maximal endurance capacity with a modest rise in mitochondrial content. The finding dissociates mTORC1's role in postprandial anabolism from its role in maintaining steady-state muscle mass, and is a directly relevant data point for whether the pattern/source of mTORC1 activation (feeding vs. mechanical) — not just its average level — shapes downstream outcomes.
2018	A	In Vivo Decoding Mechanisms of the Temporal Patterns of Blood Insulin by the Insulin-AKT Pathway in the Liver KUB2018 The in-vivo follow-up to KUB2012. In rat liver, all temporal patterns of blood insulin were encoded at the insulin receptor, and downstream molecules decoded them selectively through AKT: S6K read the additional (pulse-like) secretion, G6Pase the basal secretion via FoxO1, GSK3-beta all of it. Modelling tied the selectivity to network structure, sensitivity and time constants. Shows that pattern decoding is not only a cell-culture effect.
2012	A	Hepatic mTORC2 activates glycolysis and lipogenesis through Akt, glucokinase, and SREBP1c HAG2012 The authors deleted rictor, an essential mTORC2 component, only in mouse liver. In fed knockout mice the liver lost Akt Ser473 phosphorylation and had lower glucokinase and SREBP1c activity, so it kept making glucose (gluconeogenesis) while glycolysis and fat synthesis fell, as if it could not sense that the animal had eaten. The mice became hyperglycaemic and hyperinsulinaemic with low blood lipids. In mTORC2-deficient hepatocytes, constitutively active Akt2 restored both glucose flux and lipogenesis, while extra glucokinase restored glucose flux but not lipogenesis, placing Akt as the main route from hepatic mTORC2 to these outputs. Boundary: Mouse liver with lifelong genetic loss of mTORC2, plus cultured mouse hepatocytes. Not a drug study and not tested in people. Drafted from the abstract only.
2008	A	Skeletal muscle-specific ablation of raptor, but not of rictor, causes metabolic changes and results in muscle dystrophy BEN2008 In mice, muscle-specific raptor loss (not rictor) causes dystrophy, showing mTORC1 is essential for muscle homeostasis.
2001	A	Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR NES2001 Tested whether tumour cells that have lost PTEN depend more on mTOR. The rapamycin analogue CCI-779 (temsirolimus) blocked growth of PTEN-null cells and tumours preferentially, and reversed the extra tumour growth caused by constitutively active Akt, placing mTOR downstream of Akt in tumour formation. PTEN loss went with higher S6 kinase activity and S6 phosphorylation. Sensitivity was not explained by how well the drug blocked S6 phosphorylation, since S6 was inhibited in sensitive and resistant lines alike. Boundary: worked from the abstract only (scanned PMC record); mouse and human cell lines and mouse tumour models, not patients.
2026	M	Firefox, a protein encoded by circular PVT1, is essential for MYC-driven oncogenesis. TIW2026 A micropeptide (Firefox/FFX) encoded by the circular RNA circPVT1 stimulates AKT-mTORC1 signaling and cap-dependent translation to sustain MYC protein abundance and transcriptional output. FFX depletion reduces MYC levels and impairs tumor growth in MYC-amplified xenograft models, identifying an mTORC1-linked vulnerability in MYC-driven cancers.
2026	M	IGF2BP3-Mediated m6A Modification of OLR1 mRNA Promotes Immune Evasion in CRC via the PI3K/AKT/mTOR Pathway CHEN2026B IGF2BP3 stabilizes OLR1 via m6A RNA modification, activating PI3K/AKT/mTOR signaling which suppresses CD8+ T cell anti-tumor activity and drives immune evasion in colorectal cancer.
2026	M	Brucella suis vaccine strain 2 promotes intracellular proliferation by inducing M2 macrophage polarization and autophagy through PI3K/Akt/mTOR signalling. LI2026B Brucella suis vaccine strain 2 drives mixed M1/M2 macrophage polarisation and autophagic activation in BV2 cells; the M2 state and autophagy synergistically promote intracellular bacterial replication through PI3K/Akt/mTOR signalling.
2026	M	mTORC1 inhibition upregulates CD20 and enhances anti-CD20 antibody efficacy in B-cell precursor acute lymphoblastic leukemia DAB2026 mTORC1 inhibitors upregulate CD20 via the AKT-FOXO1 axis and promote B-lineage maturation in B-cell precursor ALL, enhancing the antitumor efficacy of anti-CD20 monoclonal antibodies -- including in high-risk IKZF1-deleted disease -- providing a rationale for combining mTORC1 inhibition with CD20-directed immunotherapy.
2026	M	Inferring feedback regulation from static snapshots of a single signal GIN2026 Introduces AoF (Assay of Feedback), a perturbation-free single-cell imaging method that reconstructs how a signal CHANGES OVER TIME from fixed-cell snapshots, using DNA content and Geminin to order cells along the cell cycle. Applied to Akt phosphorylation, it uncovers a negative feedback loop that is active only in a narrow window at the G1/S transition; biochemistry points to mTORC1/S6K1-dependent inhibitory phosphorylation of IRS1 as the likely source, though the authors state this edge is not uniquely established. Directly relevant to the question of whether mTOR pathway activity is better described as a time-varying pattern than a fixed level.
2023	M	Continuous sensing of nutrients and growth factors by the mTORC1-TFEB axis SPA2023 Live imaging of single MCF10A cells shows mTORC1-TFEB signalling adjusts continuously to amino acids and insulin, given alone, one after another or together; at physiological amino acid levels TFEB, AMPK and AKT activity fluctuate in step, and these graded changes track protein synthesis rate through a distributed set of mTORC1 effectors.
2019	R	The PI3K-AKT network at the interface of oncogenic signalling and cancer metabolism HOX2019 Review of the PI3K-AKT-mTOR network at the interface of oncogenic signalling and metabolism.
2015	M	Lysosomal mTORC2/PHLPP1/Akt regulate chaperone-mediated autophagy ARI2015 Extends the mTOR-autophagy relationship to a third form of autophagy that the Atlas otherwise does not cover, and reverses two of its usual terms. Here it is mTORC2, not mTORC1, that sits on the lysosomal membrane, and it inhibits chaperone-mediated autophagy through Akt, while the phosphatase PHLPP1 counteracts it; the balance controls assembly and disassembly of the translocation complex that pulls single proteins into the lysosome. Boundary: mechanism in cells and rodent liver; the claim that restoring this axis helps in ageing or disease is proposed, not tested here.
2012	M	Temporal coding of insulin action through multiplexing of the AKT pathway KUB2012 The same pathway can carry different messages in the shape of its signal over time. A short insulin pulse produced transient AKT phosphorylation and a sustained dose produced sustained AKT phosphorylation. S6K read only the transient part, G6Pase only the sustained part and GSK3-beta both. Which output responds depends on the pattern, not just the amount - the clearest cell-level case in the atlas that timing carries information in this pathway.
2012	M	A dynamic network model of mTOR signaling reveals TSC-independent mTORC2 regulation DAL2012 A time-resolved, data-fitted model of the whole core insulin-mTOR network, including the mTORC1 negative feedback loop onto PI3K. Perturbing it in silico and in cells showed that TSC1-TSC2 is not a regulator of mTORC2, directly or through the feedback loop, and that mTORC2 activation runs through a PI3K variant insensitive to that loop. One of the few places where the feedback loops in the atlas are treated as a dynamical system rather than a diagram.
2011	M	mTOR kinase inhibition causes feedback-dependent biphasic regulation of AKT signaling ROD2011 mTOR kinase inhibition triggers feedback-dependent biphasic AKT reactivation, informing resistance.
2011	M	Activation of mTORC2 by association with the ribosome ZIN2011 mTORC2 is activated by direct association with the ribosome downstream of PI3K.
2011	M	Evidence for direct activation of mTORC2 kinase activity by phosphatidylinositol 3,4,5-trisphosphate GAN2011 PIP3 directly stimulates mTORC2 kinase activity, linking PI3K to mTORC2.
2009	M	DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival PET2009 Identified DEPTOR as a built-in brake on BOTH mTOR complexes. The twist: in some multiple myelomas DEPTOR is overexpressed, which by relieving a feedback loop actually keeps pro-survival Akt signaling ON - a neat example of how an 'inhibitor' can be co-opted by cancer.
2009	M	Active-site inhibitors of mTOR target rapamycin-resistant outputs of mTORC1 and mTORC2 FEL2009 The parallel discovery to Thoreen 2009 (same year), from the Shokat lab. Their TORKinibs (PP242, PP30) block mTOR's active site, hitting both complexes and shutting down cap-dependent translation that rapamycin misses. Together these two papers established a whole new drug class beyond rapamycin.
2008	M	The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C FAC2008 Cells lacking the mTORC2 components mTOR, SIN1 or rictor lost phosphorylation of Akt and of conventional protein kinase C at the turn motif, a site near the end of the kinase domain. This phosphorylation did not depend on growth factors, and the authors reported the same function in yeast. Turn-motif phosphorylation helped newly made Akt and PKC fold correctly and stay stable; without it, Akt was held by the chaperone Hsp90 and protected from ubiquitin-mediated breakdown. mTORC2 controlled the Akt turn-motif and hydrophobic-motif (Ser473) sites independently in vivo and phosphorylated both directly in vitro. Boundary: Cell culture, yeast and in vitro kinase assays, with mouse tissue for the in vivo site analysis. Shows a protein-maturation role of mTORC2, not an organismal phenotype. Drafted from the abstract only.
2007	M	PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase SAN2007 Identified PRAS40 as the missing insulin-controlled brake INSIDE mTORC1. When insulin is absent PRAS40 clamps the complex shut; insulin makes Akt phosphorylate PRAS40, releasing the brake so Rheb can fully switch mTORC1 on. Explained how hormone signals set the exact strength of mTORC1 activity.
2006	M	Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB SAR2006 The molecular explanation for rapamycin's dark side. Short-term rapamycin only hits mTORC1, but prolonged treatment can also inhibit the assembly of NEW mTORC2 in susceptible cell types, reducing mTORC2 abundance and cutting Akt signaling over time. The wording matters: this is prevention of new assembly, not the dismantling of complexes already built, and the response depends on cell context and length of exposure. This is the mechanistic root of the insulin-resistance side effect later shown in mice (see Lamming 2012) - crucial for anyone dosing rapamycin for longevity.
2006	M	Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1 GUE2006 The foundational genetic 'dissection' of the two complexes in living mice. Deleting Raptor was lethal early (mTORC1 essential); deleting Rictor or mLST8 selectively knocked out mTORC2 signaling to Akt and PKCalpha but spared S6K1. This cleanly assigned jobs to each complex and showed mLST8 is an mTORC2-specific requirement in mice.
2006	M	mTOR inhibition induces upstream receptor tyrosine kinase signaling and activates Akt ORE2006 mTORC1 inhibition relieves feedback and activates upstream RTK-PI3K-Akt signalling. The Akt activation was demonstrated both in cancer cell lines and in patient tumours treated with RAD001 (everolimus), so this record carries a human pharmacodynamic component, not only in-vitro data.
2005	M	Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex SAR2005 The rictor-mTOR complex (mTORC2) directly phosphorylates Akt/PKB on Ser473, regulating cell survival.
2004	M	Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton SAR2004 Discovery of Rictor and the SECOND mTOR complex, mTORC2. Crucially showed this complex is NOT blocked by rapamycin and does not use Raptor - it controls the cytoskeleton via PKC. This is the paper that split mTOR biology into 'two faces' at the molecular level.
2002	R	The phosphoinositide 3-kinase pathway CAN2002 Review establishing PI3K as a central signaling hub controlling cell survival, metabolism, and growth downstream of growth-factor receptors and upstream of Akt and mTOR.
2002	M	TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling INO2002 Akt directly phosphorylates and inactivates TSC2, disrupting the TSC1-TSC2 complex and releasing its inhibition of mTOR - the link between growth-factor/insulin signaling and mTORC1 activation.
2002	M	Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway MAN2002 The authors combined biochemistry with a search for Akt consensus motifs and picked out tuberin, the TSC2 tumour suppressor protein, as a likely Akt substrate. They showed that activating PI3K leads to phosphorylation of tuberin at sites matching the Akt motif, and that Akt can phosphorylate tuberin both in vitro and in cells. Two of these sites, S939 and T1462, were regulated by PI3K, and T1462 stayed phosphorylated in tumour cell lines lacking PTEN. A tuberin mutant without the main PI3K-dependent sites blocked activation of S6K1. Together with papers from other labs in the same months, this was one of the early papers to link growth-factor signalling through Akt to the TSC complex and mTORC1 output. Boundary: cultured mammalian cells and in vitro kinase assays, with overexpressed tuberin mutants; no whole-animal or human tissue data.
2002	M	Akt regulates growth by directly phosphorylating Tsc2 POT2002 Working in fruit flies, the authors showed that Akt directly phosphorylates the Drosophila Tsc2 protein in vitro at two conserved residues, Ser924 and Thr1518. Tsc2 with these sites mutated no longer responded to Akt signalling, and its complex with Tsc1 became more stable. Turning up Akt signalling in fly tissue increased cell size, broke up the Tsc1-Tsc2 complex and changed where the two proteins sat in the cell. Expressing a Tsc2 mutant that Akt cannot phosphorylate blocked the growth signals from Akt, which led the authors to propose Tsc2 as the key Akt target for growth in the insulin pathway. Boundary: Drosophila tissues and in vitro biochemistry with overexpressed mutant proteins; the claim that Tsc2 carries all Akt growth signals was tested in flies, not in mammals.
2001	M	Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways ROM2001 Shows IGF-1 drives muscle fiber hypertrophy through Akt, via both the mTOR and GSK3 branches, in cultured myotubes, establishing mTOR as a central node for muscle growth signaling.
1999	M	Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor BRU1999 Akt phosphorylates the Forkhead transcription factor FKHRL1 (a FOXO family member), driving its cytoplasmic retention via 14-3-3 binding and blocking Fas-ligand-driven apoptosis — the discovery that placed FOXO transcription factors downstream of Akt/PI3K survival signalling.

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Barton, O. (2026). Akt/PKB [Entity page]. In Oliver's mTOR Atlas [Data set]. https://mtor-atlas.org/gene/akt-pkb/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_gene_akt_pkb,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}: Akt/PKB},
  howpublished = {Entity page in a data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/gene/akt-pkb/},
  doi          = {10.5281/zenodo.22059963}
}

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