AKT1 blocking peptide (CDBP5044)

16 amino acids near the amino terminus of human Akt.
Species Reactivity
Human, rat, mouse
200 μg/mL
UniProt ID
Antigen Description
The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Mutations in this gene have been associated with the Proteus syndrome. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2011]
14-3-3 protein binding; ATP binding; ATP binding; enzyme binding; identical protein binding; kinase activity; nitric-oxide synthase regulator activity; phosphatidylinositol-3,4,5-trisphosphate binding; phosphatidylinositol-3,4-bisphosphate binding; protein binding; protein kinase C binding; protein kinase activity; protein serine/threonine kinase activity; protein serine/threonine kinase activity; protein serine/threonine/tyrosine kinase activity
AKT1; v-akt murine thymoma viral oncogene homolog 1; AKT; PKB; RAC; CWS6; PRKBA; PKB-ALPHA; RAC-ALPHA; RAC-alpha serine/threonine-protein kinase; AKT1m; PKB alpha; RAC-PK-alpha; proto-oncogene c-Akt; protein kinase B alpha; rac protein kinase alpha


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Phosphorylation-dependent substrate selectivity of protein kinase B (AKT1)


Authors: Balasuriya, Nileeka; Davey, Norman E.; Johnson, Jared L.; Liu, Huadong; Biggar, Kyle K.; Cantley, Lewis C.; Li, Shawn Shun-Cheng; O'Donoghue, Patrick

Protein kinase B (AKT1) is a central node in a signaling pathway that regulates cell survival. The diverse pathways regulated by AKT1 are communicated in the cell via the phosphorylation of perhaps more than 100 cellular substrates. AKT1 is itself activated by phosphorylation at Thr-308 and Ser-473. Despite the fact that these phosphorylation sites are biomarkers for cancers and tumor biology, their individual roles in shaping AKT1 substrate selectivity are unknown. We recently developed a method to produce AKT1 with programmed phosphorylation at either or both of its key regulatory sites. Here, we used both defined and randomized peptide libraries to map the substrate selectivity of site-specific, singly and doubly phosphorylated AKT1 variants. To globally quantitate AKT1 substrate preferences, we synthesized three AKT1 substrate peptide libraries: one based on 84 ?known? substrates and two independent and larger oriented peptide array libraries (OPALs) of ?10(11)peptides each. We found that each phospho-form of AKT1 has common and distinct substrate requirements. Compared with pAKT1(T308), the addition of Ser-473 phosphorylation increased AKT1 activities on some, but not all of its substrates. This is the first report that Ser-473 phosphorylation can positively or negatively regulate kinase activity in a substrate-dependent fashion. Bioinformatics analysis indicated that the OPAL-activity data effectively discriminate known AKT1 substrates from closely related kinase substrates. Our results also enabled predictions of novel AKT1 substrates that suggest new and expanded roles for AKT1 signaling in regulating cellular processes.

LncRNA NEAT1 promotes gastric cancer progression via miR-1294/AKT1 axis


Authors: Wu, Dianchao; Li, Hui; Wang, Junfeng; Li, Hua; Xiao, Qihai; Zhao, Xiaofeng; Huo, Zhibin

Long non-coding RNAs (lncRNAs) were reported to promote the development of gastric cancer (GC). Nuclear-enriched abundant transcript 1 (NEAT1) played a great role in diverse cancers, but the mechanism of NEAT1 in GC remains indistinct. NEAT1 and AKT1 were distinctly up-regulated and miR-1294 was down-regulated in GC tissues and cells. Cell proliferation and metastasis were refrained but apoptosis was promoted in GC cells after knockdown of NEAT1. NEAT1 negatively regulated miR-1294 expression, and the miR-1294 inhibitor reverted the si-NEAT1-induced effect on GC cells. NEAT1 modulated AKT1 expression through miR-1294, and the si-NEAT1-induced effect was relieved by AKT1. NEAT1 affected phosphatidylinositol 3-kinase (PI3K)/AKT/mammalian target of rapamycin (mTOR) signaling pathway via regulating miR-1294 and AKT1. NEAT1 could modulate cell proliferation, apoptosis, and metastasis in GC cells by regulating the PI3K/AKT/mTOR signaling pathway via the miR-1294/ AKT1 axis, showing the great potential for NEAT1 as a valid biomarker in the progression and treatment of GC.

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