The RAS family of small GTPases contains 26 isoforms and paralogs with around 20–30% amino acid identity. Although they share a G domain with five essential motives, each RAS family member harbors specific and additional features that make them unique in regulation, localization, effector selection, signaling networking, and function. Based on the sequence identity, structure, and functional features, RAS proteins are categorized into eight groups of paralogs: RAS, RAL, RRAS, RIT, RAP, RHEB, RASD, ERAS and DIRAS. Besides the oncogenic function of the RAS proteins, they also play fundamental roles in normal human development, where germline mutations lead to developmental disorders, referred to as RASopathies.
The sequence similarity between RAS proteins, especially in switch regions was tempting to misconduct the overlapping functions for related RAS Paralogs. However new evidence indicates unique functions of each RAS protein in normal and pathological conditions. Therefore, this research topic aims to bring together research at the forefront of the field, to cover the recent advances in our understanding of how distinctions between these paralogs selectively and functionally control individual RAS proteins in health and disease. This information will open-up the new avenues in developing paralog- and patient-specific pharmacological inhibitors that target directly up- or downstream modulators of individual RASs.
We welcome submissions of Original Research, Reviews, Mini-reviews, Brief reports, and other article types that cover, but are not limited to, the following suggested sub-topics in health and disease (e.g., cancers and RASopathies)
• The tissue- and cell-type-specific functions of RAS isoforms and paralogs
• Discovering the novel aspects of the regulation, complex formation, multiple effector pathways, crosstalk interactions and feedback mechanisms of the individual RAS members
• The subcellular localization of RAS proteins and signaling networks, and its importance in the RAS protein functions
• The dynamics regulation and spatial organization of RAS signaling networks
• The structural and molecular fingerprints of RAS paralogs and their mutant variants
The RAS family of small GTPases contains 26 isoforms and paralogs with around 20–30% amino acid identity. Although they share a G domain with five essential motives, each RAS family member harbors specific and additional features that make them unique in regulation, localization, effector selection, signaling networking, and function. Based on the sequence identity, structure, and functional features, RAS proteins are categorized into eight groups of paralogs: RAS, RAL, RRAS, RIT, RAP, RHEB, RASD, ERAS and DIRAS. Besides the oncogenic function of the RAS proteins, they also play fundamental roles in normal human development, where germline mutations lead to developmental disorders, referred to as RASopathies.
The sequence similarity between RAS proteins, especially in switch regions was tempting to misconduct the overlapping functions for related RAS Paralogs. However new evidence indicates unique functions of each RAS protein in normal and pathological conditions. Therefore, this research topic aims to bring together research at the forefront of the field, to cover the recent advances in our understanding of how distinctions between these paralogs selectively and functionally control individual RAS proteins in health and disease. This information will open-up the new avenues in developing paralog- and patient-specific pharmacological inhibitors that target directly up- or downstream modulators of individual RASs.
We welcome submissions of Original Research, Reviews, Mini-reviews, Brief reports, and other article types that cover, but are not limited to, the following suggested sub-topics in health and disease (e.g., cancers and RASopathies)
• The tissue- and cell-type-specific functions of RAS isoforms and paralogs
• Discovering the novel aspects of the regulation, complex formation, multiple effector pathways, crosstalk interactions and feedback mechanisms of the individual RAS members
• The subcellular localization of RAS proteins and signaling networks, and its importance in the RAS protein functions
• The dynamics regulation and spatial organization of RAS signaling networks
• The structural and molecular fingerprints of RAS paralogs and their mutant variants
