Molecular mechanisms underlying the physiological and pathological functions of histone modification

• Posttranslational modifications on histones (hPTM) are now understood to exert major regulatory impacts on diverse biological processes. A variety of hPTMs such as methylation, acetylation, phosphorylation, and ubiquitination, has been identified to be epigenetic marks driving gene regulatory networks controlling cell fate decisions. hPTMs are dynamically regulated by ‘writer’ and ‘eraser’ enzymes, and are recognized by dozens of ‘reader’ modules, and these proteins variously coordinate to specify many distinct biological outcomes. Owing to developments in mass spectrometry technologies, new histone modifications such as crotonylation, β-hydroxybutyrylation, lactylation, and serotonylation, have been reported to activate gene transcription, and these modifications have been functionally implicated in physiological responses to metabolic stress and pathological functions in tumorigenesis. One of our research interest is to explore the molecular mechanisms underlying the regulation and recognition of hPTMs and investigate their physiological and pathological functions.