About this Research Topic
UDP-glycosyltransferase (UGT) enzymes catalyze the conjugation of an activated sugar form, uridine diphosphate (UDP)-glycoside, with a variety of small lipophilic compounds. This glycoside conjugation is one of the important mechanisms to detoxify xenobiotics in animals - it increases water solubility making the compounds more easily excretable, thereby protecting the cellular system from damage by toxic compounds. It is also involved in pigment sequestration providing color to the cuticle, wings or cocoons in insects. Some UGTs are highly expressed in insect antennae, suggesting a novel function in olfaction. Invertebrate UGTs, therefore, play an important physiological role in several processes, including detoxification, biosynthesis, storage and transport of bioactive compounds.
Compared to the drug-metabolizing mammalian UGTs, less attention has been paid to the invertebrate UGTs, but a recent surge of genome sequences has identified many UGT genes from diverse invertebrates that show multifaceted expression profiles in relation to tissues, hosts, xenobiotics, or other environmental factors. However, the names given to these UGT genes are somewhat random due to the lack of a universal nomenclature system. Once agreed, the use of a standard nomenclature will facilitate understanding and interspecies comparisons of this highly-diverse multigene family. There is an urgent need to summarize the current status of invertebrate UGT research and to give an insight on future avenues, including their molecular evolution, diverse physiological functions, and relevance to management strategies in agriculture, health and environment.
This Research Topic will focus on the invertebrate UDP-glycosyltransferases (UGTs) and we welcome the submission of Original Research, Review, Mini-Review, Methods and Perspective articles covering, but not limited to, the following sub-topics:
• Nomenclature system of invertebrate UGTs
• Molecular evolution of the UGT multigene family
• UGT-mediated detoxification of plant secondary compounds
• Pesticide resistance associated with UGT enzymes
• Virus UGTs in relation to arthropod physiology
• Olfaction-related functions of UGTs
• Molecular biology of UGT gene regulations
• Ecological and physiological implications of glycoside conjugation in invertebrates
Compared to the drug-metabolizing mammalian UGTs, less attention has been paid to the invertebrate UGTs, but a recent surge of genome sequences has identified many UGT genes from diverse invertebrates that show multifaceted expression profiles in relation to tissues, hosts, xenobiotics, or other environmental factors. However, the names given to these UGT genes are somewhat random due to the lack of a universal nomenclature system. Once agreed, the use of a standard nomenclature will facilitate understanding and interspecies comparisons of this highly-diverse multigene family. There is an urgent need to summarize the current status of invertebrate UGT research and to give an insight on future avenues, including their molecular evolution, diverse physiological functions, and relevance to management strategies in agriculture, health and environment.
This Research Topic will focus on the invertebrate UDP-glycosyltransferases (UGTs) and we welcome the submission of Original Research, Review, Mini-Review, Methods and Perspective articles covering, but not limited to, the following sub-topics:
• Nomenclature system of invertebrate UGTs
• Molecular evolution of the UGT multigene family
• UGT-mediated detoxification of plant secondary compounds
• Pesticide resistance associated with UGT enzymes
• Virus UGTs in relation to arthropod physiology
• Olfaction-related functions of UGTs
• Molecular biology of UGT gene regulations
• Ecological and physiological implications of glycoside conjugation in invertebrates
Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
