The importance of the GTP-binding protein tissue transglutaminase in the regulation of cell cycle progression. Academic Article uri icon

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the full length tTgase cDNA (wild type) and a mutant form of the cDNA whereby the active site cysteine (Cys 277) has been replaced by serine.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.

published proceedings

  • FEBS Lett

author list (cited authors)

  • Mian, S., el Alaoui, S., Lawry, J., Gentile, V., Davies, P. J., & Griffin, M.

citation count

  • 73

complete list of authors

  • Mian, S||el Alaoui, S||Lawry, J||Gentile, V||Davies, PJ||Griffin, M

publication date

  • August 1995

publisher