TTC3 ubiquitination terminates Akt-ivation

Alex Toker

doi:10.1016/j.devcel.2009.12.003

TTC3 ubiquitination terminates Akt-ivation

Dev Cell. 2009 Dec;17(6):752-4. doi: 10.1016/j.devcel.2009.12.003.

Author

Alex Toker¹

Affiliation

¹ Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA. atoker@bidmc.harvard.edu

PMID: 20059946
DOI: 10.1016/j.devcel.2009.12.003

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.

Publication types

Comment

MeSH terms

Cell Nucleus / metabolism
Humans
Proteasome Endopeptidase Complex / metabolism
Proto-Oncogene Proteins c-akt / metabolism*
Ubiquitin-Protein Ligases / metabolism*
Ubiquitination

Substances

TTC3 protein, human
Ubiquitin-Protein Ligases
Proto-Oncogene Proteins c-akt
Proteasome Endopeptidase Complex