Screening of a large Rubinstein–Taybi cohort identified many novel variants and emphasizes the importance of the CREBBP histone acetyltransferase domain

2020 ◽  
Vol 182 (11) ◽  
pp. 2508-2520
Author(s):  
Esther Cross ◽  
Philippa J. Duncan‐Flavell ◽  
Rachel J. Howarth ◽  
James I. Hobbs ◽  
Nicholas Simon Thomas ◽  
...  
Keyword(s):  
Histone Acetyltransferase ◽  
Novel Variants ◽  
Acetyltransferase Domain

scholarly journals The Human Monocytic Leukemia Zinc Finger Histone Acetyltransferase Domain Contains DNA-binding Activity Implicated in Chromatin Targeting

2007 ◽  
Vol 282 (50) ◽  
pp. 36603-36613 ◽  
Author(s):  
Marc A. Holbert ◽  
Timothy Sikorski ◽  
Juliana Carten ◽  
Danielle Snowflack ◽  
Santosh Hodawadekar ◽  
...  
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Histone Acetyltransferase ◽  
Binding Activity ◽  
Monocytic Leukemia ◽  
Dna Binding Activity ◽  
Human Monocytic Leukemia ◽  
Acetyltransferase Domain

Bromodomain and Histone Acetyltransferase Domain Specificities Control Mixed Lineage Leukemia Phenotype

2006 ◽  
Vol 66 (20) ◽  
pp. 10032-10039 ◽  
Author(s):  
Donna A. Santillan ◽  
Catherine M. Theisler ◽  
Amanda S. Ryan ◽  
Relja Popovic ◽  
Tara Stuart ◽  
...  
Keyword(s):  
Histone Acetyltransferase ◽  
Mixed Lineage Leukemia ◽  
Acetyltransferase Domain

Targeting of a histone acetyltransferase domain to a promoter enhances protein expression levels in mammalian cells

2005 ◽  
Vol 115 (1) ◽  
pp. 35-46 ◽  
Author(s):  
T.H.J. Kwaks ◽  
R.G.A.B. Sewalt ◽  
R. van Blokland ◽  
T.J. Siersma ◽  
M. Kasiem ◽  
...  
Keyword(s):  
Protein Expression ◽  
Mammalian Cells ◽  
Histone Acetyltransferase ◽  
Expression Levels ◽  
Acetyltransferase Domain

scholarly journals Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A

2007 ◽  
Vol 68 (1) ◽  
pp. 403-407 ◽  
Author(s):  
Anja Schuetz ◽  
Galina Bernstein ◽  
Aiping Dong ◽  
Tatiana Antoshenko ◽  
Hong Wu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Histone Acetyltransferase ◽  
Coenzyme A ◽  
Binary Complex ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Acetyltransferase Domain

scholarly journals Interaction and Functional Cooperation between the LIM Protein FHL2, CBP/p300, and β-Catenin

2004 ◽  
Vol 24 (24) ◽  
pp. 10689-10702 ◽  
Author(s):  
Charlotte Labalette ◽  
Claire-Angélique Renard ◽  
Christine Neuveut ◽  
Marie-Annick Buendia ◽  
Yu Wei
Keyword(s):  
Gene Expression ◽  
Androgen Receptor ◽  
Transcriptional Activation ◽  
Ternary Complex ◽  
Histone Acetyltransferase ◽  
Lim Protein ◽  
Transactivation Activity ◽  
Exogenous Expression ◽  
Acetyltransferase Domain

ABSTRACT Transcriptional activation of gene expression by Wnt signaling is driven by the association of β-catenin with TCF/LEF factors and the recruitment of transcriptional coactivators. It has been shown that the LIM protein FHL2 and the acetyltransferase CBP/p300 individually stimulate β-catenin transactivating activity and that β-catenin is acetylated by p300. Here, we report that FHL2 and CBP/p300 synergistically enhanced β-catenin/TCF-mediated transcription from Wnt-responsive promoters and that the acetyltransferase activity of CBP/p300 was involved in the cooperation. CBP/p300 interacted directly with FHL2, predominantly through the CH3 domain but not the histone acetyltransferase domain, and different regions of CBP/p300 were involved in FHL2 and β-catenin binding. We provided evidence for the formation of a ternary complex by FHL2, CBP/p300, and β-catenin and for colocalization of the three proteins in the nucleus. In murine FHL2−/− embryo fibroblasts, the transactivation activity of β-catenin/TCF was markedly reduced, and this defect could be restored by exogenous expression of FHL2. However, CBP/p300 were still able to coactivate the β-catenin/TCF complex in FHL2−/− cells, suggesting that FHL2 is dispensable for the coactivator function of CBP/p300 on β-catenin. Furthermore, we found that FHL2 significantly increased acetylation of β-catenin by p300 in vivo. Finally, we showed that FHL2, CBP/p300, and β-catenin could synergistically activate androgen receptor-mediated transcription, indicating that the synergistic coactivator function is not restricted to TCF/LEF.

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