Journal article

Publication year: 2022

Pages: 909-920

Journal: Trends in Biochemical Sciences

Volume number: 47

Issue number: 11

ISSN: 0968-0004

eISSN: 1362-4326

DOI Link: https://doi.org/10.1016/j.tibs.2022.04.014

Publisher: Cell Press

Abstract: 
The histone variant H2A.Z has been extensively studied to understand its mani-fold DNA-based functions. In the past years, researchers identified its specific binding partners, the 'H2A.Z interactome', that convey H2A.Z-dependent chro-matin changes. Here, we summarize the latest findings regarding vertebrate H2A.Z-associated factors and focus on their roles in gene activation and repres-sion, cell cycle regulation, (neuro)development, and tumorigenesis. Additionally, we demonstrate how protein-protein interactions and post-translational histone modifications can fine-tune the complex interplay of H2A.Z-regulated gene expression. Last, we review the most recent results on interactors of the two iso-forms H2A.Z.1 and H2A.Z.2.1, which differ in only three amino acids, and focus on cancer-associated mutations of H2A and H2A.Z, which reveal fascinating insights into the functional importance of such minuscule changes.

Harvard Citation style: Kreienbaum, C., Paasche, L. and Hake, S. (2022) H2A.Z's ‘social’ network: functional partners of an enigmatic histone variant, Trends in Biochemical Sciences, 47(11), pp. 909-920. https://doi.org/10.1016/j.tibs.2022.04.014

APA Citation style: Kreienbaum, C., Paasche, L., & Hake, S. (2022). H2A.Z's ‘social’ network: functional partners of an enigmatic histone variant. Trends in Biochemical Sciences. 47(11), 909-920. https://doi.org/10.1016/j.tibs.2022.04.014