Role of Translocation in the Activation and Function of Protein Kinase B

Andjelkovic, Mirjana; Alessi, Dario R.; Meier, Roger; Fernandez, Anne; Lamb, Ned J.C.; Frech, Matthias; Cron, Peter; Cohen, Philip; Lucocq, John M.; Hemmings, Brian A.

doi:10.1074/jbc.272.50.31515

Cited by 1,051PI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase SignalingMetabolism, Diabetes, and Cancer

Role of Translocation in the Activation and Function of Protein Kinase B

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Andjelkovic, Mirjana, Alessi, Dario R., Meier, Roger, Fernandez, Anne, Lamb, Ned J.C., Frech, Matthias, Cron, Peter, Cohen, Philip +2 more·1997·Journal of Biological Chemistry

DOI 10.1074/jbc.272.50.31515

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Abstract

We have investigated the role of subcellular localization in the regulation of protein kinase B (PKB) activation. The myristoylation/palmitylation motif from the Lck tyrosine kinase was attached to the N terminus of protein kinase B to alter its subcellular location. Myristoylated/palmitylated (m/p)-PKBalpha was associated with the plasma membrane of transfected cells, whereas the wild-type kinase was mostly cytosolic. The activity of m/p-PKBalpha was 60-fold higher compared with the unstimulated wild-type enzyme, and could not be stimulated further by growth factors or phosphatase inhibitors. In vivo 32P labeling and mutagenesis demonstrated that m/p-PKBalpha activity was due to phosphorylation on Thr308 and Ser473, that are normally induced on PKB following stimulation of the cells with insulin or insulin-like growth factor-1 (IGF-1). A dominant negative form of phosphoinositide 3-kinase (PI3-K) did not affect m/p-PKBalpha activity. The pleckstrin homology (PH) domain of m/p-PKBalpha was not required for its activation or phosphorylation on Thr308 and Ser473, suggesting that this domain may serve as a membrane-targeting module. Consistent with this view, PKBalpha was translocated to the plasma membrane within minutes after stimulation with IGF-1. This translocation required the PH domain and was sensitive to wortmannin. Our results indicate that PI3-K activity is required for translocation of PKB to the plasma membrane, where its activation occurs through phosphorylation of the same sites that are induced by insulin or IGF-1. Following activation the kinase detached from the membrane and translocated to the nucleus.

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Activation of PKB promotes translocation of PKB to the nucleus and phosphorylates Mdm2 in the nuclear compartment.
“Our data suggest that activation of PKB promotes translocation of PKB to the nucleus (5,6) and phosphorylates Mdm2 in the nuclear compartment.”
From Stabilization of Mdm2 via Decreased Ubiquitination Is Mediated by Protein Kinase B/Akt-dependent Phosphorylation (2004) · cites this paper as [5]

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Authors: Andjelkovic, M., Alessi, D. R., Meier, R., Fernandez, A., Lamb, N. J. C., Frech, M., Cron, P., Cohen, P., Lucocq, J. M., & Hemmings, B. A.
Affiliations: University of Dundee (GB)
Friedrich Miescher Institute (CH)
Centre National de la Recherche Scientifique (FR)
Corresponding author: Hemmings, Brian A.
ORCID: Alessi, Dario R.
Fernandez, Anne
Lamb, Ned J.C.
Frech, Matthias
Cohen, Philip
Lucocq, John M.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1997-12
Volume: 272
Issue: 50
Pages: 31515-31524
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.272.50.31515
OpenAlex: W2064242629
Cited by: 1,051
References: 53
Citations by year: 2026: 5 · 2025: 15 · 2024: 12 · 2023: 8 · 2022: 15 · 2021: 16 · 2020: 15 · 2019: 28 · 2018: 16 · 2017: 18 · 2016: 20 · 2015: 32 · 2014: 29 · 2013: 41 · 2012: 33
FWCI: 16.79
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8342 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion, other-oa)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: Akt, subcellular translocation, membrane translocation, myristoylation, palmitoylation, Lck tyrosine kinase, pleckstrin homology domain, PI3-kinase, Ser473 phosphorylation, insulin signaling, IGF-1 signaling, wortmannin, nuclear translocation, plasma membrane
MeSH terms: Biological Transport, Cell Membrane, Cells, Cultured, Chromones, Enzyme Activation, Enzyme Inhibitors, Humans, Insulin-Like Growth Factor I, Morpholines, Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Serine, Threonine, Protein Serine-Threonine Kinases, Amino Acid Substitution, Protein Sorting Signals, Proto-Oncogene Proteins c-akt

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Role of Translocation in the Activation and Function of Protein Kinase B

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