MinireviewCBP/p300 acetyltransferase activity in hematologic malignancies

- CBP/p300 has protein lysine acetyltransferase activity that is regulated by cell cycle progression and phosphorylation.
- CBP/p300 acetylate transcription factors that are critical for hematopoietic stem cell function.
- Aberrant acetylation of non-histone substrates by CBP/p300 can facilitate their oncogenic potential.
- Targeted therapy against CBP/p300 KAT activity may be an effective therapeutic strategy for hematopoietic malignancies.

CREB binding protein (CBP) and p300 are critical regulators of hematopoiesis through both their transcriptional coactivator and acetyltransferase activities. Loss or mutation of CBP/p300 results in hematologic deficiencies in proliferation and differentiation as well as disruption of hematopoietic stem cell renewal and the microenvironment. Aberrant lysine acetylation mediated by CBP/p300 has recently been implicated in the genesis of multiple hematologic cancers. Understanding the effects of disrupting the acetyltransferase activity of CBP/p300 could pave the way for new therapeutic approaches to treat patients with these diseases.