Degron-independent recruitment of KAT2A expands the target space of CRBN molecular glues

S Samuel Ojeda (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.) M Meng Wang K Kheewoong Baek (Department of Cancer Biology, Dana–Farber Cancer Institute, Boston, MA 02215, USA.) W Wallace Bourgeois (Department of Pediatric Oncology, Dana-Farber Cancer Institute, Division of Hematology/Oncology, Boston Children’s Hospital, Harvard Medical School, Boston, MA, USA.) A Alba Sommerschield (Department of Pediatric Oncology, Dana-Farber Cancer Institute, Division of Hematology/Oncology, Boston Children’s Hospital, Harvard Medical School, Boston, MA, USA.) H Hong Yue (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.) R Rebecca J. Metivier (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.) P Panos Karagiannis (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.) T Talya S. Levitz (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.) Y Yuan Xiong (Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.) K Katherine A. Donovan S Scott A. Armstrong (Department of Pediatric Oncology, Dana-Farber Cancer Institute, Division of Hematology/Oncology, Boston Children’s Hospital, Harvard Medical School, Boston, MA, USA.) E Eric S. Fischer

Abstract

Lysine acetyltransferases (KATs) cooperate with oncogenes such as c-Myc, estrogen receptor, and lysine methyltransferase 2A (KMT2A) fusions to sustain malignant programs. Targeting of KAT proteins has shown clinical efficacy; however, achieving homolog selectivity for most KATs remains a major challenge. By extending cereblon (CRBN)–based molecular glues beyond the canonical degron space, we developed an exquisitely selective degrader of KAT2A. Cryo–electron microscopy revealed that CRBN recruits KAT2A independently of a degron; instead, the molecular glue engages a surface-exposed tyrosine, mimicking antibody-like molecular recognition. Selective KAT2A degradation leads to potent ablation of histone H3 lysine 9 acetylation (H3K9Ac), antiproliferative effects in acute myeloid leukemia cell lines, and in vivo efficacy in a patient-derived xenograft model, establishing KAT2A as a targetable vulnerability to treat a wide range of malignancies. More generally, degron-independent recruitment extends the CRBN-targetable proteome.

Article Details

Journal Science
Volume / Issue Vol. 393, Issue 6807
Published July 09, 2026
Pages 188-194
ISSN 0036-8075
Publisher American Association for the Advancement of Science

Journal Info

Science

American Association for the Advancement of Science

ISSN: 0036-8075 Social Sciences

Authors (13)

S

Samuel Ojeda

Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.

M

Meng Wang

K

Kheewoong Baek

Department of Cancer Biology, Dana–Farber Cancer Institute, Boston, MA 02215, USA.

W

Wallace Bourgeois

Department of Pediatric Oncology, Dana-Farber Cancer Institute, Division of Hematology/Oncology, Boston Children’s Hospital, Harvard Medical School, Boston, MA, USA.

A

Alba Sommerschield

Department of Pediatric Oncology, Dana-Farber Cancer Institute, Division of Hematology/Oncology, Boston Children’s Hospital, Harvard Medical School, Boston, MA, USA.

H

Hong Yue

Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.

R

Rebecca J. Metivier

Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.

P

Panos Karagiannis

Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.

T

Talya S. Levitz

Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.

Y

Yuan Xiong

Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.

K

Katherine A. Donovan

S

Scott A. Armstrong

Department of Pediatric Oncology, Dana-Farber Cancer Institute, Division of Hematology/Oncology, Boston Children’s Hospital, Harvard Medical School, Boston, MA, USA.

E

Eric S. Fischer