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PXD064389

PXD064389 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleStructural basis of the cyclin Y/14-3-3 protein-mediated activation of CDK16
DescriptionCyclin-dependent protein kinase 16 (CDK16) regulates both physiological and pathological processes, including autophagy, spermatogenesis and cancer. Unlike other CDKs, CDK16 is regulated by an unclear mechanism involving phosphorylated cyclin Y (CCNY) in complex with 14-3-3 proteins rather than CCNY alone. The present study aims at elucidating this mechanism by structurally characterizing CDK16 in complex with CCNY and 14-3-3 using several biophysical techniques. As shown by cryo-EM analysis and hydrogen/deuterium exchange coupled to mass spectrometry, 14-3-3 binding unmasks a key moiety of the CDK binding surface of CCNY, thereby enabling CDK16 activation. CDK16 interacts with the cyclin box of CCNY, while 14-3-3 provides additional contacts, including with the activation segment of CDK16. CDK16 activation also requires interactions of CCNY with the N-terminal extension of CDK16. These findings not only clarify the role of CCNY and 14-3-3 in CDK16 activation but also highlight the potential of targeting CDK16 protein-protein interactions for cancer therapy.
HostingRepositoryPRIDE
AnnounceDate2026-03-25
AnnouncementXMLSubmission_2026-03-25_00:52:34.746.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterPavla Vankova
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationListphosphorylated residue
InstrumenttimsTOF Pro
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-05-28 17:46:49ID requested
12026-03-25 00:52:35announced
Publication List
10.1038/S41467-026-70778-5;
Keyword List
submitter keyword: CDK16,Cyclin-dependent protein kinase, CCNY, cyclin Y, 14-3-3 protein
Contact List
Tomas Obsil
contact affiliationDepartment of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic Institute of Physiology of the Czech Academy of Sciences, Laboratory of Structural Biology of Signaling Proteins, Division BIOCEV, Vestec, Czech Republic
contact emailtomas.obsil@natur.cuni.cz
lab head
Pavla Vankova
contact affiliationInstitute of Biotechnology of the Czech Academy of Sciences, BioCeV, Prumyslova 595, 252 50 Vestec, Czech Republic
contact emailpavla.vankova@ibt.cas.cz
dataset submitter
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Dataset FTP location
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PRIDE project URI
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