西亚试剂：WSTF regulates the H2A.X DNA damage response via a novel ty

发布时间：2025-06-15

WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity

Andrew Xiao1, Haitao Li2, David Shechter1, Sung Hee Ahn1, Laura A. Fabrizio3, Hediye Erdjument-Bromage3, Satoko Ishibe-Murakami2, Bin Wang4, Paul Tempst3, Kay Hofmann5, Dinshaw J. Patel2, Stephen J. Elledge4 & C. David Allis1

1 Laboratory of Chromatin Biology, The Rockefeller University, New York, New York 10065, USA
2 Structural Biology Program,
3 Molecular Biology Program, Memorial-Sloan-Kettering Cancer Center, New York, New York 10065, USA
4 Howard Hughes Medical Institute, Department of Genetics, Harvard Partners Center for Genetics and Genomics, Harvard Medical School, Boston, Massachusetts 02115, USA
5 Miltenyi Biotec GmbH, 50829 Koeln, Germany

DNA double-stranded breaks present a serious challenge for eukaryotic cells. The inability to repair breaks leads to genomic instability, carcinogenesis and cell death. During the double-strand break response, mammalian chromatin undergoes reorganization demarcated by H2A.X Ser 139 phosphorylation (-H2A.X). However, the regulation of -H2A.X phosphorylation and its precise role in chromatin remodelling during the repair process remain unclear. Here we report a new regulatory mechanism mediated by WSTF (Williams–Beuren syndrome transcription factor, also known as BAZ1B)—a component of the WICH complex (WSTF–ISWI ATP-dependent chromatin-remodelling complex). We show that WSTF has intrinsic tyrosine kinase activity by means of a domain that shares no sequence homology to any known kinase fold. We show that WSTF phosphorylates Tyr 142 of H2A.X, and that WSTF activity has an important role in regulating several events that are critical for the DNA damage response. Our work demonstrates a new mechanism that regulates the DNA damage response and expands our knowledge of domains that contain intrinsic tyrosine kinase activity.

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