grant
A Functional Analysis of Arginine Methylation
Organization UNIVERSITY OF TX MD ANDERSON CAN CTRLocation HOUSTON, UNITED STATESPosted 1 Sept 2024Deadline 31 Jul 2029
NIHUS FederalResearch GrantFY2025AddressArginineArginine MethylaseAromatic Amino AcidsBiologicalCell Communication and SignalingCell SignalingDNA DamageDNA InjuryDepositDepositionDockingGoalsHistone (Arginine) MethyltransferaseIntracellular Communication and SignalingKinasesKnowledgeL-ArginineL-LysineLysineMammaliaMammalsMethylationMiceMice MammalsMurineMusMyelin Basic Protein (Arginine) MethyltransferasePhosphotransferase GenePhosphotransferasesPost-Translational Modification Protein/Amino Acid BiochemistryPost-Translational ModificationsPost-Translational Protein ModificationPost-Translational Protein ProcessingPosttranslational ModificationsPosttranslational Protein ProcessingProtein Arginine MethyltransferaseProtein ArrayProtein Methylase IProtein Methyltransferase IProtein ModificationProtein-Arginine N-MethyltransferaseProteinsProteomicsReaderRoleSeriesSignal TransductionSignal Transduction PathwaySignal Transduction SystemsSignalingSiteTransphosphorylasesWorkbiologicbiological signal transductionnovelrecruitresponsesocial role
Description preview
PROJECT SUMMARY/ABSTRACT
Our goal is to broadly understand the biological roles of arginine methylation, a very common post-translational
modification (PTM). This PTM is deposited by at least nine protein arginine methyltransferases (PRMTs) in
mammals. Like lysine methylation, arginine methylation of a substrate often recruits an effector molecule…
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