Molecular cloning and expression of glycogen synthase kinase‐3/factor A.
Open accessAbstract
Glycogen synthase kinase-3 (GSK-3) is a protein-serine kinase implicated in the hormonal control of several regulatory proteins including glycogen synthase and the transcription factor c-jun. Two classes of rat brain cDNA for this enzyme have been isolated termed GSK-3 alpha and GSK-3 beta. The alpha-type encodes a 51 kd polypeptide, the sequence of which includes all of the tryptic peptides determined by protein sequence analysis of purified skeletal muscle GSK-3. The novel beta-type cDNA has the potential to encode a 47 kd protein with 85% amino acid identity to GSK-3 alpha. The two types of cDNA are the products of distinct genes as determined by genomic organization and nucleic acid sequence analysis. Both alpha and beta clones exhibit kinase activity when expressed in COS-1 cells and type-specific antibodies to GSK-3 alpha and beta detect proteins of 51 and 47 kd, respectively, in a variety of rat tissue extracts, with highest levels of both in brain. Partial purification of GSK-3 activity from bovine brain results in the isolation of active alpha and beta proteins. The physiological importance of these two proteins in cellular signal transduction is discussed.
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By immunoblotting, the c-myc antibody recognized a band of approximately 48 kDa only in transfected CHO cells, consistent with recombinant GSK3β with a c-myc tail.
“By immunoblotting the c-myc MAb recognized a band with an apparent molecular mass of ap- proximately 48 kDa only in transfected CHO cells (Fig. 3A), consistent with the apparent molecular mass of recombinant GSK3fl [ 19] with an added c-myc tail.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [19]
GSK3β can orchestrate pathological tau phosphorylation at over two-dozen disease-associated sites.
“The GSK3β can orchestrate pathological tau-phosphorylation at over two-dozen disease-associated sites [181–184].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [181]
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- Authors
- Woodgett, J. R.
- Affiliations
- Ludwig Cancer Research (GB)
- Corresponding author
- Woodgett, J. R.
- ORCID
- Woodgett, J. R.
- Venue
- The EMBO Journal
- Published
- 1990-08-01
- Volume
- 9
- Issue
- 8
- Pages
- 2431-2438
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC552268
- OpenAlex
- W1983055247
- Cited by
- 1,362
- References
- 42
- Citations by year
- 2026: 17 · 2025: 32 · 2024: 31 · 2023: 41 · 2022: 46 · 2021: 64 · 2020: 60 · 2019: 40 · 2018: 46 · 2017: 47 · 2016: 54 · 2015: 48 · 2014: 64 · 2013: 67 · 2012: 65
- FWCI
- 5.42
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and 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 › Signaling Pathways in Disease
- Keywords
- glycogen synthase kinase-3, GSK3β, cDNA cloning, kinase activity, brain, skeletal muscle, signal transduction, glycogen synthase, c-Jun, gene structure
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Brain, Cattle, Cell Line, Cloning, Molecular, Gene Amplification, Genes, Molecular Sequence Data, Muscles, Protein Kinases, Rabbits, Reticulocytes, Sequence Homology, Nucleic Acid, Transfection, Oligonucleotide Probes, Gene Library, Gene Expression, Calcium-Calmodulin-Dependent Protein Kinases, Glycogen Synthase Kinases, Rats
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