title: TTC3 ubiquitination terminates Akt-ivation.
abstract: 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.
authors.affiliation: Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA. atoker@bidmc.harvard.edu
authors.forename: Alex
authors.initials: A
authors.lastname: Toker
mesh_terms: 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
chemical_list: C108062:TTC3 protein, human; D044767:Ubiquitin-Protein Ligases; D051057:Proto-Oncogene Proteins c-akt; D046988:Proteasome Endopeptidase Complex