Regulation and Function of Hsp27 in Zebrafish

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Small heat shock proteins (sHsps) are a large, but poorly understood, family of proteins. In vertebrates and many invertebrates, sHsps are constitutively found in muscle cells where they may play roles in homeostasis and injury repair. Preliminary results obtained in the Shelden laboratory have revealed striking, stress-dependent recruitment of the ubiquitous small heat shock protein, Hsp27, to muscle myofibrils. This research focuses on defining the mechanism and functional significance of this recruitment and specifically addresses the following questions: 1) How is Hsp27 regulated when it associates with myofibrils, and what is the effect of regulation on its function?, 2) What are the kinetics of association between Hsp27 and myofibrils during injury? and, 3) What is the target for Hsp27 within myofibrils? The project will employ immunolocalization as well as ulltrastructural and biochemical approaches to examine stress-induced redistribution of Hsp27 and phosphoserine mutants of Hsp27 in zebrafish embryos. Completion of this work will substantially advance the understanding of Hsp27 regulation and function in muscle cells. These studies are also expected to advance general understanding of sHsp functions and response of muscle cells to stress and injury, especially in vivo. Such knowledge may ultimately be used to enhance muscle growth, or ameliorate injury and age-dependent muscle dysfunction in commercial or clinical settings, and permit a better understanding of adaptations to environmental stress in poikilotherm (cold blooded) animals. In addition, the project will support outreach and educational activities to students in area elementary schools and junior and senior high school students at a local summer science camp program.