2025
Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions
Robles J, Stiegler A, Boggon T, Turk B. Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions. Journal Of Biological Chemistry 2025, 301: 108348. PMID: 40015635, PMCID: PMC11982978, DOI: 10.1016/j.jbc.2025.108348.Peer-Reviewed Original ResearchShort linear motifsCancer hotspot mutationsLinear motifsERK substratesYeast two-hybrid libraryHotspot mutationsTwo-hybrid libraryCancer-associated mutantsDocking interactionsWild-type ERK2Cancer-associated mutationsDocking motifBinding sequenceKinase ERK2Co-crystal structureMutant formsERK2 mutantsDisordered regionsERK2MotifStructural rationalePeptide bindingMutationsWT kinasePeptide fragments
2024
Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail
Sexton J, Potchernikov T, Bibeau J, Casanova-SepĂşlveda G, Cao W, Lou H, Boggon T, De La Cruz E, Turk B. Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail. Nature Communications 2024, 15: 1426. PMID: 38365893, PMCID: PMC10873347, DOI: 10.1038/s41467-024-45878-9.Peer-Reviewed Original ResearchConceptsN-terminal regionActin bindingSequence requirementsLIM kinaseAnalysis of individual variantsInactivates cofilinS. cerevisiaeRegulatory tailFamily proteinsActin depolymerizationPhosphorylation sitesKinase recognitionSequence variantsInhibitory phosphorylationCofilinN-terminusIndividual variantsFunctional constraintsActinDisordered sequencesPhosphorylationSequenceBiochemical analysisSequence constraintsKinase
2023
Autoregulation of the LIM kinases by their PDZ domain
Casanova-SepĂşlveda G, Sexton J, Turk B, Boggon T. Autoregulation of the LIM kinases by their PDZ domain. Nature Communications 2023, 14: 8441. PMID: 38114480, PMCID: PMC10730565, DOI: 10.1038/s41467-023-44148-4.Peer-Reviewed Original Research
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