Dr. Chunbin Zou’s Research

Dr. Zou’s laboratory focuses on a novel epigenetic code histone O-palmitoylation and its pathophysiological significances. Dr. Zou serendipitously discovered a novel histone modification called histone O-palmitoylation that acts as a new epigenetic mark to regulate gene transcription. Under pathophysiological stimulation, a cytosolic residing active lung surfactant synthetic enzyme Acyl CoA: Lysophosphatidylcholine acyltansferase1 (Lpcat1) migrates into the nucleus. The nuclear Lpcat1 bindsto and O-palmitoylates histone NH2-terminal tail by attaching a situated long fatty acid (C-16, palmitoyl group) to the serine/threonine residues. He demonstrated that Lpcat1 mediated-histone O-palmitoylation alters chromatin architecture, interplays with histone acetylation and phosphorylation, and acts as an epigenetic code to regulate proinflammatory gene transcription. This discovery was published in J. Biol. Chem. and the publication was highlighted by Faculty of 1000 organization. Continuing on this line of research will add ample knowledge of a novel layer of epigenetic regulation both in basic and medical scientific fields.

The related research interest in Dr. Zou’s laboratory is deregulation of key proteins in the lung. In the life processes, proteins are dynamic in responding to the environmental changes or pathological stimuli. If a given protein is needed, de novo synthesis from mRNA will be augmented. If redundant, proteins will be promptly dumped out by degradation via ubiquitin proteasomal/lysosomal degradation machinery. Regulation of protein stability via degradation plays an important role in a vast range of life processes. Protein turnover is not a randomly happened event but highly multi-layer regulated and is a substrate-specific signal transduction cascade. His studies demonstrated that acetylation/deacetylation modulates ubiquitination and regulates E3 ubiquitin ligase binding to the protein substrate thereafter governs protein degradation. He has uncovered several unstudied enzymes called E3 ubiquitin ligases that control the protein degradation of several important epigenetic histone modification enzymes in pneumonia lung tissues. He is actively to seek the possible small molecules that may modulate the protein degradation and enzyme activity thus control the pathological progress of acute lung injury.

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