Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-37897
Mol Cell 2001 Jul 01;81:71-84. doi: 10.1016/s1097-2765(01)00277-5.
Show Gene links Show Anatomy links

A TPR motif cofactor contributes to p300 activity in the p53 response.

Demonacos C , Krstic-Demonacos M , La Thangue NB .


Abstract
The transcription of p53 target genes involves p300/CBP coactivators, which are multiprotein complexes that interact with the p53 activation domain. We report a cofactor in the p300 coactivator complex, Strap, which has an unusual structure, being composed almost entirely of a tandem series of six tetratricopeptide repeat (TPR) motifs. The TPR motif functions as a protein interaction domain, and it is consistent with this property that Strap harbors distinct and dedicated domains that allow it to bind and augment the interaction between different components of the p300 complex. Strap facilitates p53 activity in response to stress, in part through the stress-responsive accumulation of Strap protein and interfering with the MDM2-dependent downregulation of p53.

PubMed ID: 11511361
Article link: Mol Cell
Grant support: [+]

Genes referenced: LOC100893406 LOC105438357 LOC577224 prkci tpr