Format

Send to

Choose Destination
EMBO Rep. 2006 Jul;7(7):727-33. Epub 2006 Apr 28.

c-Abl acetylation by histone acetyltransferases regulates its nuclear-cytoplasmic localization.

Author information

1
Dulbecco Telethon Institute, Via Montpellier 1, 00133 Rome, Italy.

Abstract

c-Abl function is strictly dependent on its subcellular localization. Using an in vitro approach, we identify c-Abl as a new substrate for p300, CBP (CREB-binding protein) and PCAF (p300/CBP-associated factor) histone acetyltransferases. Remarkably, acetylation markedly alters its subcellular localization. Point mutagenesis indicated that Lys 730, located in the second nuclear localization signal, is the main target of p300 activity. It has previously been reported that c-Abl accumulates in the cytoplasm during myogenic differentiation. Here, we show that c-Abl protein is acetylated at early stages of myogenic differentiation. Indeed, acetylation on Lys 730 drives c-Abl accumulation in the cytoplasm and promotes differentiation. Thus, Lys 730 acetylation is a novel post-translational modification of c-Abl and a novel mechanism for modulating its subcellular localization that contributes to myogenic differentiation.

PMID:
16648821
PMCID:
PMC1500821
DOI:
10.1038/sj.embor.7400700
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center