TTC3 ubiquitination terminates Akt-ivation.
In this issue of Developmental Cell, Suizu et al. (2009) describe a new mechanism for posttranslational regulation of the Akt serine/threonine protein kinase involving ubiquitination. They show that the E3 ubiquitin ligase TTC3 modifies phosphorylated and activated Akt and thereby promotes its degradation by the proteasome in the nucleus.
Toker
Alex
A
Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA. atoker@bidmc.harvard.edu
D002467:Cell Nucleus / Q000378:metabolism; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D051057:Proto-Oncogene Proteins c-akt / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination
C108062:TTC3 protein, human; D044767:Ubiquitin-Protein Ligases; D051057:Proto-Oncogene Proteins c-akt; D046988:Proteasome Endopeptidase Complex