Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1

Related Experiment Video

Updated: Jun 22, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

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

Published on: May 3, 2018

Mei Jiang1, Yankun Gao, Tao Yang

  • 1State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, SIBS, Chinese Academy of Sciences, Shanghai, China.

FEBS Letters
|June 16, 2009
PubMed

Insights

A novel cyclin, CCNY, interacts with PFTK1 kinase, enhancing its activity and altering cellular location. This interaction is crucial for CCNY

Area of Science:

  • Molecular and Cellular Biology
  • Protein Interactions
  • Cell Signaling

Background:

  • Protein kinases play critical roles in cellular signaling pathways.
  • Cyclins are key regulators of cell cycle progression and other cellular processes.
  • Understanding novel protein interactions is essential for elucidating complex biological functions.

Purpose of the Study:

  • To identify and characterize novel interacting partners of PFTK1.
  • To elucidate the functional significance of the interaction between CCNY and PFTK1.
  • To investigate the subcellular localization and regulation of CCNY.

Main Methods:

  • Yeast two-hybrid screening to identify interacting proteins.
  • In vivo and in vitro assays to confirm protein-protein interactions.
  • Northern blot analysis to detect CCNY transcripts.
  • Subcellular localization studies using myristoylation signal analysis.

Main Results:

  • A novel cyclin, CCNY, was identified as a PFTK1 interacting protein.
  • The cyclin box of CCNY and the PFTAIRE motif of PFTK1 are essential for their interaction.
  • CCNY exists in two transcript forms (4 and 2kb) and localizes to the plasma membrane.
  • An N-terminal myristoylation signal directs CCNY to the plasma membrane.

Conclusions:

  • CCNY binds to PFTK1, enhancing its kinase activity.
  • The interaction between CCNY and PFTK1 influences PFTK1's intracellular localization.
  • CCNY represents a novel regulator of PFTK1 function and localization.

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