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The importance of the GTP-binding protein tissue transglutaminase in the regulation of cell cycle progression
- Source :
- FEBS Letters. (1-2):27-31
- Publisher :
- Published by Elsevier B.V.
-
Abstract
- Tissue transglutaminase (tTgase) is a GTP-binding Ca(2+)-dependent enzyme which catalyses the post-translational modification of proteins via epsilon(gamma-glutamyl) lysine bridges. Recent evidence suggests that the GTP-binding activity of tTgase may be important in intracellular signaling thus explaining some of the diverse suggested roles for the enzyme. In the following work a malignant hamster fibrosarcoma (Met B) has been stably transfected with both the full length tTgase cDNA (wild type) and a mutant form of the cDNA whereby the active site cysteine (Cys 277) has been replaced by serine. Expression of this mutant cDNA leads to a protein with GTP binding activity which is deficient of protein crosslinking activity. When synchronised into S-phase and allowed to progress through the cell cycle tTgase transfected clones (both mutant and wild type), when compared to transfected controls, show a delayed progression from S-phase to G2/M when analysed by flow cytometry which appears to be elicited by the G-protein activity of the tTgase.
- Subjects :
- GTP'
G protein
Tissue transglutaminase
Fibrosarcoma
Mutant
Blotting, Western
Biophysics
GTP-binding protein
Cell cycle
Transfection
Biochemistry
GTP-binding protein regulators
Structural Biology
GTP-Binding Proteins
Complementary DNA
Cricetinae
Genetics
Serine
Tumor Cells, Cultured
Animals
Homeostasis
Humans
Point Mutation
Cysteine
Binding site
Molecular Biology
Binding Sites
Transglutaminases
biology
Wild type
Cell Biology
DNA
Molecular biology
Transglutaminase
Recombinant Proteins
biology.protein
Mutagenesis, Site-Directed
Protein Processing, Post-Translational
Cell Division
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1-2
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....600a140bf28ae731ff8889fb6eda8199
- Full Text :
- https://doi.org/10.1016/0014-5793(95)00782-5