Abstract:
:The serine threonine kinase Akt is a core survival factor that underlies a variety of human diseases. Although regulatory phosphorylation and dephosphorylation have been well documented, the other posttranslational mechanisms that modulate Akt activity remain unclear. We show here that tetratricopeptide repeat domain 3 (TTC3) is an E3 ligase that interacts with Akt. TTC3 contains a canonical RING finger motif, a pair of tetratricopeptide motifs, a putative Akt phosphorylation site, and nuclear localization signals, and is encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. Moreover, DS cells exhibit elevated TTC3 expression, reduced phosphorylated Akt, and accumulation in the G(2)M phase, which can be reversed by TTC3 siRNA or Myr-Akt. Thus, interaction between TTC3 and Akt may contribute to the clinical symptoms of DS.
journal_name
Dev Celljournal_title
Developmental cellauthors
Suizu F,Hiramuki Y,Okumura F,Matsuda M,Okumura AJ,Hirata N,Narita M,Kohno T,Yokota J,Bohgaki M,Obuse C,Hatakeyama S,Obata T,Noguchi Mdoi
10.1016/j.devcel.2009.09.007subject
Has Abstractpub_date
2009-12-01 00:00:00pages
800-10issue
6eissn
1534-5807issn
1878-1551pii
S1534-5807(09)00389-Xjournal_volume
17pub_type
杂志文章abstract::The glucose transporter type 4 (glut4) is critical for metabolic homeostasis. Insulin regulates glut4 by modulating its expression on the cell surface. This regulation is mainly achieved by targeting the endocytic recycling of glut4. We identify general receptor for 3-phosphoinositides 1 (Grp1) as a guanine nucleotide...
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