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Interacting partners of FEN1 and its role in the development of anticancer therapeutics

Chandrasekhar Kathera1, Jing Zhang1, Avilala Janardhan1

  • 1Jiangsu Key Laboratory for Molecular and Medical Biotechnology, College of Life Sciences, Nanjing Normal University, Nanjing, China.

Oncotarget
|February 11, 2017
PubMed

Insights

Protein-protein interactions (PPI) are crucial for cell signaling and can be used to create network biomarkers for cancer diagnosis. Flap endonuclease 1 (FEN1) dysregulation is linked to cancer, highlighting its potential in biomarker development.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cancer Research

Background:

  • Protein-protein interactions (PPIs) are fundamental to cellular processes, including signaling pathways.
  • Dysregulation of Flap endonuclease 1 (FEN1) is implicated in various cancers.
  • FEN1 plays a critical role in cellular metabolism, DNA replication, and repair.

Purpose of the Study:

  • To review the types, detection methods, and significance of PPIs in cancer.
  • To explore the role of FEN1 interacting partners in cancer development.
  • To discuss the potential of PPI data for developing network-based cancer biomarkers and therapeutics.

Main Methods:

  • Literature review of protein-protein interactions.
  • Analysis of FEN1's role in cellular metabolism and cancer.
  • Examination of PPI data for biomarker and therapeutic development.

Main Results:

  • PPIs form complex networks involving hubs and nodes critical for signaling.
  • Altered FEN1 expression levels are observed in numerous cancer types.
  • FEN1's interacting partners are involved in DNA replication and repair processes.

Conclusions:

  • PPIs offer a promising avenue for developing network-based biomarkers for early cancer diagnosis.
  • Understanding FEN1's interaction network can aid in developing targeted anticancer therapeutics.
  • FEN1's central role in metabolism and DNA repair makes it a key focus for cancer research.
Keywords:
FEN1modificationsposttranslationalprotein-protein interactionsmall molecular inhibitors

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