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PXD034604-1

PXD034604 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleCardioviruses’ leader proteins retarget RSK kinases toward alternative substrates to perturb nucleocytoplasmic traffic
DescriptionProteins from unrelated pathogens, including some RNA or DNA viruses and bacteria can recruit and activate cellular p90-ribosomal protein S6 kinases (RSKs) through a common linear motif. Data suggested a model where pathogens' proteins act to dock the recruited RSKs toward specific substrates, which then act as effectors to the benefit of the pathogens. Using cardiovirus leader protein (L) as a paradigm, we show that pathogens' proteins can modify the spectrum of RSK substrates in infected cells. L triggers nucleocytoplasmic trafficking perturbation and phenylalanine-glycine (FG)-nucleoporin hyperphosphorylation in an RSK-dependent fashion. Biotin ligase experiments identified FG-nucleoporins as common partners of L and RSK in infected cells. Using cells expressing an analog-sensitive RSK2 mutant, we show that L triggers direct phosphorylation of NUP98 and NUP214 by RSK2 in infected cells. Our data therefore demonstrate a novel virulence mechanism where pathogens' proteins hijack and retarget cellular protein kinases of the RSK family
HostingRepositoryPRIDE
AnnounceDate2022-12-08
AnnouncementXMLSubmission_2022-12-08_01:25:37.944.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterDidierVertommen
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListbiotinylated residue; phosphorylated residue; monohydroxylated residue
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-06-16 03:51:42ID requested
12022-12-08 01:25:38announced
22023-11-14 08:57:22announced2023-11-14: Updated project metadata.
Publication List
Keyword List
submitter keyword: p90 ribosomal S6 kinases, Picornavirus, nucleocytoplasmic traffic, RSK, cardiovirus, phosphorylation, YopM, nucleoporins,linear motifs
Contact List
ThomasMichiels
contact affiliationVIRO unit, de Duve Institute, Université Catholique de Louvain, Brussels, 1200, Belgium
contact emailthomas.michiels@uclouvain.be
lab head
DidierVertommen
contact affiliationUCL - de Duve Institute, Brussels Belgium
contact emaildidier.vertommen@uclouvain.be
dataset submitter
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Dataset FTP location
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