The E3 ligase is a type of remarkable enzyme for understanding the ubiquitin and ubiquitin-like protein modification systems that contribute to functional changes of substrates and thus regulate a broad range of biological processes with endocrine regulation included. E3 ligases have emerged as pivotal targets for drug discovery using the function of targeted protein degradation.
Although E3 ubiquitin ligases are conserved among eukaryotes including plants and animals, they play an essential role in endocrine regulation. For example, loss of E3 ligase is likely to cause endocrine disorder or multiple stress in the organs and systems. E3 ubiquitin or ubiquitin-like ligases mainly include the following families: RING type, HECT type, RING-between-RING (RBR) family, PIAS1, RanBP2, Polycomb2, Dcn1, c-Cbl, Herc5, Ufl1, Atg5-Atg12/Atg16, etc. However, we know very little about their targets, co-factors, roles and crosstalk in cellular stress response, acute and chronic human or animal disease, animal development, immune response, hormone signaling pathways, etc.
In this Research Topic, we welcome a summary of the up-to-date findings about intrinsic ligase activity, focusing on the well-known E3 ligase-substrate interactions. Besides, we would like to define novel E3 ligase substrates that can mediate numerous hormone signalling pathways and endocrine regulation. We will highlight the search for relevant and novel targets, outlining the processes that were proven to be nice and straightforward for screening potential targets as well as their subsequent functional analysis. The aforementioned research work will lead to new and exciting future studies.
We welcome contributions in various forms (Original Research, Review, Mini-Review, Methods, Perspective articles, etc.) highlighting but not limited to the following subjects:
• Update the knowledge about the regulatory mechanism of E3 ubiquitin ligase in cellular stress response.
• Seek for the co-factors with the pathogenic mechanisms shared by E3 and endocrine diseases, from genetical, molecular, and environmental perspectives.
• Identify co-factors or substrates linking endocrine dysfunction and E3 ligase using novel methodologies (proteomic, metabolomic, computational, chemical-biology, etc.).
• Make innovative and challenging hypotheses aiming at reducing the burden of the disease, based on the existing scientific evidence.
• Elucidate the novel mechanism of endocrine homeostasis regulated by E3 ligase or its co-factors.
The E3 ligase is a type of remarkable enzyme for understanding the ubiquitin and ubiquitin-like protein modification systems that contribute to functional changes of substrates and thus regulate a broad range of biological processes with endocrine regulation included. E3 ligases have emerged as pivotal targets for drug discovery using the function of targeted protein degradation.
Although E3 ubiquitin ligases are conserved among eukaryotes including plants and animals, they play an essential role in endocrine regulation. For example, loss of E3 ligase is likely to cause endocrine disorder or multiple stress in the organs and systems. E3 ubiquitin or ubiquitin-like ligases mainly include the following families: RING type, HECT type, RING-between-RING (RBR) family, PIAS1, RanBP2, Polycomb2, Dcn1, c-Cbl, Herc5, Ufl1, Atg5-Atg12/Atg16, etc. However, we know very little about their targets, co-factors, roles and crosstalk in cellular stress response, acute and chronic human or animal disease, animal development, immune response, hormone signaling pathways, etc.
In this Research Topic, we welcome a summary of the up-to-date findings about intrinsic ligase activity, focusing on the well-known E3 ligase-substrate interactions. Besides, we would like to define novel E3 ligase substrates that can mediate numerous hormone signalling pathways and endocrine regulation. We will highlight the search for relevant and novel targets, outlining the processes that were proven to be nice and straightforward for screening potential targets as well as their subsequent functional analysis. The aforementioned research work will lead to new and exciting future studies.
We welcome contributions in various forms (Original Research, Review, Mini-Review, Methods, Perspective articles, etc.) highlighting but not limited to the following subjects:
• Update the knowledge about the regulatory mechanism of E3 ubiquitin ligase in cellular stress response.
• Seek for the co-factors with the pathogenic mechanisms shared by E3 and endocrine diseases, from genetical, molecular, and environmental perspectives.
• Identify co-factors or substrates linking endocrine dysfunction and E3 ligase using novel methodologies (proteomic, metabolomic, computational, chemical-biology, etc.).
• Make innovative and challenging hypotheses aiming at reducing the burden of the disease, based on the existing scientific evidence.
• Elucidate the novel mechanism of endocrine homeostasis regulated by E3 ligase or its co-factors.
