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Updated: Sep 7, 2025

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

SILAC kinase screen identifies potential MASTL substrates.

Kamila A Marzec¹, Samuel Rogers², Rachael McCloy³

¹ANZAC Research Institute, Concord Hospital, Concord, NSW, 2139, Australia.

Scientific Reports

|June 22, 2022

Summary

This summary is machine-generated.

Microtubule-associated serine/threonine kinase-like (MASTL) may phosphorylate new substrates beyond Arpp-19/ENSA. This kinase

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A Multiplexed Luciferase-based Screening Platform for Interrogating Cancer-associated Signal Transduction in Cultured Cells

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Published on: July 3, 2013

Area of Science:

Cell Biology
Biochemistry
Oncology

Background:

Microtubule-associated serine/threonine kinase-like (MASTL) is a key regulator of mitosis.
MASTL is implicated as an oncogene in various cancers.
Currently, Arpp-19/ENSA are the sole identified substrates of MASTL.

Purpose of the Study:

To identify novel substrates of MASTL.
To determine the optimal consensus motif for MASTL activity.
To understand MASTL's expanding biological roles in cancer.

Main Methods:

Utilized a whole cell lysate in vitro kinase screen.
Employed stable isotope labeling with amino acids in cell culture (SILAC) for substrate identification.
Validated potential substrates using subsequent in vitro kinase assays.

Main Results:

Identified 59 phospho-sites on 67 proteins regulated by active MASTL.
The kinase screen, validated with AKT1/2, identified known and novel substrates.
hnRNPM, YB1, and TUBA1C were suggested as potential MASTL substrates in vitro.

Conclusions:

MASTL likely phosphorylates additional substrates beyond Arpp-19/ENSA.
These findings offer insights into MASTL's role in cancer progression and therapy resistance.
Further research into MASTL substrates is crucial for developing targeted cancer therapies.