2025
Deep mutational scanning of the Trypanosoma brucei developmental regulator RBP6 reveals an essential disordered region influenced by positive residues
Rojas-Sánchez S, Kolev N, Tschudi C. Deep mutational scanning of the Trypanosoma brucei developmental regulator RBP6 reveals an essential disordered region influenced by positive residues. Nature Communications 2025, 16: 1168. PMID: 39885181, PMCID: PMC11782513, DOI: 10.1038/s41467-025-56553-y.Peer-Reviewed Original ResearchConceptsN-terminal intrinsically disordered regionRNA binding protein 6RNA recognition motifDeep mutational scanningMutational scanningDisordered regionsProtein-RNA interactionsIntrinsically disordered regionsComplex developmental programPositively charged residuesSingle-point variantsProtein-RNARNA recognitionDeleterious mutationsMutational constraintsProcyclic formsAnimal African trypanosomiasisTrypanosoma bruceiCharged residuesPrimary structureRegained infectivityDevelopmental programRegulatory roleProtein 6Positive residues
2021
A pentameric protein ring with novel architecture is required for herpesviral packaging
Didychuk A, Gates S, Gardner M, Strong L, Martin A, Glaunsinger B. A pentameric protein ring with novel architecture is required for herpesviral packaging. ELife 2021, 10: e62261. PMID: 33554858, PMCID: PMC7889075, DOI: 10.7554/elife.62261.Peer-Reviewed Original ResearchConceptsViral genomeAccessory factorsBind double-stranded DNAPositively charged central channelContext of KSHV infectionDouble-stranded DNA virusesPositively charged residuesOncogenic herpesvirus Kaposi's sarcoma-associated herpesvirusKaposi's sarcoma-associated herpesvirusDouble-stranded DNASarcoma-associated herpesvirusGenome packagingHomologous proteinsNascent capsidsDNA bindingProtein ringGenomePackaging motorDNA virusesCharged residuesProgeny virionsMolecular motorsCentral channelKSHV infectionMutants
2001
Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail
Blott E, Bossi G, Clark R, Zvelebil M, Griffiths G. Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail. Journal Of Cell Science 2001, 114: 2405-2416. PMID: 11559749, DOI: 10.1242/jcs.114.13.2405.Peer-Reviewed Original ResearchConceptsProline-rich domainSecretory lysosomesPlasma membraneCytoplasmic tailSH3 domain-containing proteinsCell surface receptor FasFas ligandCell surface expression of FasLSH3-domain-containingSurface expression of FasLCell typesPositively charged residuesMis-sortingSorting motifDeletion mutantsExpression of FasLReceptor FasEndogenous FasLInduce apoptosisCharged residuesCell surface expressionLysosomal compartmentFasLLysosomesMotif
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