Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 24, Issue -, Pages 80-90Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2014.10.015
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Funding
- Hong Kong Research Grants Council (RGC) Early Career Scheme (ECS) [HKU 709813P]
- General Research Fund [GRF17303114]
- Hung Hing Ying Physical Science Research Fund [20373739]
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Histone posttranslational modifications (PTMs) play key roles in the regulation of many fundamental cellular processes, such as gene transcription, DNA damage repair and chromosome segregation. Significant progress has been made on the detection of a large variety of PTMs on histones. However, the identification of these PTMs' regulating enzymes (i.e. 'writers' and 'erasers') and functional binding partners (i.e. 'readers') have been a relatively slow-paced process. As a result, cellular functions and regulatory mechanisms of many histone PTMs, particularly the newly identified ones, remain poorly understood. This review focuses on the recent progress in developing chemical proteomics approaches to profile readers, erasers and writers of histone PTMs. One of such efforts involves the development of the Cross-Linking-Assisted and SILAC-based Protein Identification (CLASPI) approach to examine PTM-mediated protein-protein interactions.
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