Cited by 378PI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase SignalingMetabolism, Diabetes, and Cancer

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Mitogenic Activation, Phosphorylation, and Nuclear Translocation of Protein Kinase Bβ

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Meier, Roger, Alessi, Dario R., Cron, Peter, Andjelković, Mirjana, Hemmings, Brian A.·1997·Journal of Biological Chemistry

DOI 10.1074/jbc.272.48.30491

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Abstract

Protein kinase B (PKB) is a member of the second messenger-dependent family of serine/threonine kinases that has been implicated in signaling pathways downstream of growth factor receptor tyrosine kinases and phosphatidylinositol 3-kinase. Here we report the characterization of the human beta-isoform of PKB (PKBbeta). PKBbeta is ubiquitously expressed in a number of human tissues, with mRNA and protein levels elevated in heart, liver, skeletal muscle, and kidney. After transfection into HEK-293 or COS-1 cells, PKBbeta is activated 2- to 12-fold by mitogens and survival factors. Activation was due to phosphorylation on Thr-309 and Ser-474, which correspond to Thr-308 and Ser-473 implicated in the regulation of PKBalpha. Both phosphorylation and activation were prevented by the phosphatidylinositol 3-kinase inhibitor wortmannin. Moreover, membrane-targeted PKBbeta was constitutively activated when overexpressed in HEK-293 cells. Although the specific activity of PKBbeta was lower than that of PKBalpha toward Crosstide as a substrate (23 nmol/min/mg compared with 178 nmol/min/mg for PKBalpha), both enzymes showed similar substrate specificities. Using confocal microscopy, we show that activation of PKBbeta results in its nuclear translocation within 20 to 30 min after stimulation. These observations provide evidence that PKBbeta undergoes nuclear translocation upon mitogenic activation and support a role for PKB in signaling from receptor tyrosine kinases to the nucleus through phosphatidylinositol 3-kinase.

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Authors: Meier, R., Alessi, D. R., Cron, P., Andjelković, M., & Hemmings, B. A.
Affiliations: Friedrich Miescher Institute (CH)
University of Dundee (GB)
Corresponding author: Hemmings, Brian A.
ORCID: Alessi, Dario R.
Andjelković, Mirjana
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1997-11
Volume: 272
Issue: 48
Pages: 30491-30497
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.272.48.30491
OpenAlex: W2112620000
Semantic Scholar: 04080b05d4799385077ac3417ff97498cc43a4a4
Cited by: 378
References: 37
Citations by year: 2026: 3 · 2025: 3 · 2024: 8 · 2023: 5 · 2022: 5 · 2021: 1 · 2020: 6 · 2019: 8 · 2017: 2 · 2016: 8 · 2015: 8 · 2014: 8 · 2013: 11 · 2012: 10
FWCI: 7.47
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, 8374 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
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: mitogen stimulation, phosphorylation, nuclear translocation, phosphatidylinositol 3-kinase, wortmannin, receptor tyrosine kinase signaling, substrate specificity, growth factor signaling
MeSH terms: Amino Acid Sequence, Animals, Biological Transport, Cell Compartmentation, Cell Nucleus, Enzyme Activation, Growth Substances, Humans, Insulin, Insulin-Like Growth Factor I, Mitogens, Molecular Sequence Data, Phosphorylation, Phosphoserine, Phosphothreonine, Proto-Oncogene Proteins, Substrate Specificity, Tissue Distribution, Protein Serine-Threonine Kinases, COS Cells, Phosphatidylinositol 3-Kinases, Proto-Oncogene Proteins c-akt, Rats

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Mitogenic Activation, Phosphorylation, and Nuclear Translocation of Protein Kinase Bβ

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