Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Video

Updated: Jun 13, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Synthetic Substrate Discovery for Hck Kinase via Phage Display.

Akaash Kannan1, Jason L Heier1, Dhruvi P Motwani1

  • 1University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics, 420 Washington Avenue SE, Minneapolis, Minnesota 55455, United States.

Biochemistry
|June 12, 2026
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Novel terbium-sensitizing peptide substrates for cyclin-dependent kinase 5 (CDK5) and their demonstration in luminescence kinase assays.

RSC chemical biology·2025
Same author

Antibody-free time-resolved terbium luminescence assays designed for cyclin-dependent kinase 5 (CDK5).

bioRxiv : the preprint server for biology·2024
Same author

Novel Substrate Prediction for the TAM Family of RTKs Using Phosphoproteomics and Structure-Based Modeling.

ACS chemical biology·2023
Same author

Novel Bruton's Tyrosine Kinase (BTK) Substrates for Time-Resolved Luminescence Assays.

ACS chemical biology·2022
Same author

Integrated Phosphoproteomics for Identifying Substrates of Human Protein Kinase A (<i>PRKACA</i>) and Its Oncogenic Mutant <i>DNAJB</i>1<i>-PRKACA</i>.

Journal of proteome research·2021
Same author

Lipid Droplet-Derived Monounsaturated Fatty Acids Traffic via PLIN5 to Allosterically Activate SIRT1.

Molecular cell·2020

We developed a new phage display method to identify protein tyrosine kinase substrates. This high-throughput approach precisely profiles kinase activity and reveals novel substrates with strong kinetic properties.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Protein tyrosine kinases (PTKs) are crucial for cell signaling, and their dysregulation is linked to cancer.
  • Understanding PTK substrate specificity is vital for cancer research but current methods lack scale and resolution.

Purpose of the Study:

  • To develop a high-throughput method for comprehensive profiling of PTK substrates.
  • To identify novel substrates and understand kinase-substrate recognition for the Hck kinase.

Main Methods:

  • Utilized a modernized phage display platform integrated with next-generation sequencing.
  • Performed simultaneous assessment of billions of potential substrates for Hck kinase.
  • Analyzed positional and motif enrichment for iterative substrate design.

More Related Videos

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases
06:30

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases

Published on: August 27, 2021

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Related Experiment Videos

Last Updated: Jun 13, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases
06:30

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases

Published on: August 27, 2021

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Main Results:

  • Successfully profiled Hck kinase substrates at an unprecedented scale and resolution.
  • Identified novel substrates with robust kinetic behavior (Km < 30 μM).
  • Gained insights into Hck substrate preferences in multipositional sequence contexts.

Conclusions:

  • The new phage display platform offers a powerful tool for PTK substrate profiling.
  • This method advances our understanding of kinase-substrate interactions and cancer biology.
  • The identified substrates and insights can inform future therapeutic strategies targeting PTKs.