Abstract
Lipolysis is a conserved pathway used by organisms for the mobilization of fatty acid from triacylglycerols found in lipid storage droplets (LSDs). Numerous proteins, including the perilipins, CGI‐58, G0S2, and lipases interact and regulate fatty acid release in lipolysis. Because lipolysis is conserved throughout Animalia, and because several of these proteins interact with one another, it stands to reason that genes coding for these proteins are coevolving as species adapt to environmental changes. The present study traces the evolutionary history of lipolysis by examining the evolution of LSD proteins in different species of Animalia. Comparisons were made of fragments of protein sequences coding for LSD proteins previously demonstrated in the literature to interact with one another. Amino acid residues that are conserved between interacting partners and are indicative of potential protein‐protein interactions and will be used in subsequent analysis.
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