Related Experiment Video

Updated: Mar 21, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

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Structural basis of the cyclin Y/14-3-3 protein-mediated activation of CDK16

Klara Kohoutova1,2, Dalibor Kosek2, Adam Brzezina1

  • 1Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic.

Nature Communications
|March 20, 2026
PubMed

Insights

Cyclin-dependent protein kinase 16 (CDK16) activation involves cyclin Y (CCNY) and 14-3-3 proteins. Structural studies reveal how 14-3-3 binding to CCNY enables CDK16 activity, offering cancer therapy insights.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Cyclin-dependent protein kinase 16 (CDK16) plays roles in physiological and pathological processes, including cancer.
  • CDK16 regulation is unique, involving cyclin Y (CCNY) complexed with 14-3-3 proteins, unlike other CDKs.

Purpose of the Study:

  • To elucidate the mechanism of CDK16 activation by structurally characterizing the CDK16-CCNY-14-3-3 complex.
  • To understand the specific roles of CCNY and 14-3-3 proteins in regulating CDK16 activity.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for structural determination.
  • Hydrogen/deuterium exchange mass spectrometry (HDX-MS) to analyze protein dynamics and interactions.

Main Results:

  • 14-3-3 binding alters CCNY conformation, facilitating CDK16 binding and activation.
  • CDK16 interacts with CCNY's cyclin box, while 14-3-3 provides additional contacts, including with CDK16's activation segment.
  • CCNY's N-terminal extension is crucial for CDK16 activation through interactions with CDK16.

Conclusions:

  • The study clarifies the mechanism of CDK16 activation mediated by the CCNY-14-3-3 complex.
  • Findings suggest targeting CDK16 protein-protein interactions as a potential cancer therapy strategy.

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