Research Progress of Structure and Function of Nuclear Transcription Factor Relish

doi:10.13438/j.cnki.jdzk.2024.01.013

Abstract

Abstract: The nuclear transcription factor Relish is a member of the NF-κbs superfamily functioning as an important immune signaling effector.Relish contains a conserved Rel homologue domain at the N-terminal and an ankyrin repeat domain at the C-terminal.Relish is actived in response to certain external stimulations transmitted by the Imd pathway,via phosphorylation,cleavage and other posttranslational modification of Relish.Activated Relish then translocates to nuclear and binds to DNA to regulate the expression of target genes,helping organisms to adapt to various physiological environments and stimuli,resisting the invasion and infection of foreign pathogens.The paper provides an brief review of the structure and function of Relish.The structural features of Relish include Rel homology domain,ankyrin repeats domain,nuclear localization sequence,caspase target site,serine-rich regions,and proline-glutamate-serine-rich domain.Functions of Relish mainly involve participating in innate immunity,regulating neural development and lifespan,regulating intestinal homeostasis and morphology,participating in stress regulation and other physiological activities.

Key words: Relish, NF-κB, innate immunity, Imd pathway

ZHANG Hong, LIU Qingzhen. Research Progress of Structure and Function of Nuclear Transcription Factor Relish[J]. Journal of Jishou University(Natural Sciences Edition), 2024, 45(1): 77-83.

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