A loss-of-function variant in SUV39H2 identified in autism-spectrum disorder causes altered H3K9 trimethylation and dysregulation of protocadherin β-cluster genes in the developing brain

• Published in: Molecular psychiatry Vol. 26; no. 12; pp. 7550 - 7559
• Main Authors: Balan, Shabeesh, Iwayama, Yoshimi, Ohnishi, Tetsuo, Fukuda, Mikiko, Shirai, Atsuko, Yamada, Ayumi, Weirich, Sara, Schuhmacher, Maren Kirstin, Dileep, Kalarickal Vijayan, Endo, Toshihiro, Hisano, Yasuko, Kotoshiba, Kaoru, Toyota, Tomoko, Otowa, Takeshi, Kuwabara, Hitoshi, Tochigi, Mamoru, Watanabe, Akiko, Ohba, Hisako, Maekawa, Motoko, Toyoshima, Manabu, Sasaki, Tsukasa, Nakamura, Kazuhiko, Tsujii, Masatsugu, Matsuzaki, Hideo, Zhang, Kam Y J, Jeltsch, Albert, Shinkai, Yoichi, Yoshikawa, Takeo
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 01.12.2021
• Subjects: Animals; Autism; Autistic Disorder; Brain - metabolism; Cerebellum; DNA methylation; Embryos; Enzymatic activity; Etiology; Genetic diversity; Histone H3; Histone methyltransferase; Histone-Lysine N-Methyltransferase - genetics; Histone-Lysine N-Methyltransferase - metabolism; Histones - genetics; Histones - metabolism; Hydrophobicity; Hyperactivity; Lysine; Mice; Neurodevelopment; Next-generation sequencing; Protocadherin; Protocadherins

Recent evidence has documented the potential roles of histone-modifying enzymes in autism-spectrum disorder (ASD). Aberrant histone H3 lysine 9 (H3K9) dimethylation resulting from genetic variants in histone methyltransferases is known for neurodevelopmental and behavioral anomalies. However, a syst...