Heat Shock Protein 90 controls pelvic fin development in a desert pupfish

Authors: Ken McKenna, Maja Aleksic, Chalisa Pansin, Alexander Jones, Georgina Puentedura, Stanley Hillyard, Frank Van Breukelen

Year: 2016 (xlviii)

Abstract

Heat Shock Protein 90 (HSP90) is an important molecular chaperone that assists with protein folding and has been shown to mas k genetic variability in fish. HSP90 is often diverted to other roles within cells during heat shock and other stressful conditions. We hypothesized that HSP90 played an important role in the development of pelvic fins in pupfish. We focused on HSP90’s role in pelvic fin development because a lack of pelvic fins is often used as a diagnostic tool for identifying the critically endangered Devils Hole Pupfish (Cyprinodon diabolis). We reared two species of pupfish at 28 ’C and 33 ’C and measured a reduction in total number of pelvic fin rays and in pelvic fin presence at the higher temperature. We then inhibited HSP90 at different developmental periods in a Refuge population of fish derived from C. diabolis using 17-DMAG and a heat shock of 33 ’C. We demonstrated that total number of fin rays is reduced when HSP90 is inhibited using both chemical means and an ecologically relevant heat shock. Our results support past findings that suggest that pelvic fin development in pupfish is plastic. Developmental plasticity could thus explain at least one of the morphological features used to identify C. diabolis.