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Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Amplifying Signals via Enzymatic Cascade

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

MAPK Signaling Cascades

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...

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Related Experiment Video

Updated: May 21, 2026

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

Using protein microarrays to study phosphorylation-mediated signal transduction.

Hong Zhang¹, Steven Pelech

¹Kinexus Bioinformatics Corporation, Vancouver, Canada. hzhang@kinexus.ca

Seminars in Cell & Developmental Biology

|June 19, 2012

Summary

Protein microarrays, including antibody and reverse-phase protein microarrays (RPPMs), are powerful tools for studying cell signaling and disease biomarkers. Challenges like antibody specificity and data validation are critical for accurate proteomic research.

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Last Updated: May 21, 2026

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

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Published on: September 19, 2018

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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

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Published on: October 23, 2019

Area of Science:

Biomedical research
Proteomics
Cellular signaling

Background:

Understanding cell regulatory systems is crucial for biomedical advancement.
The phosphoproteome offers valuable biomarkers for cell signaling and disease, with kinases as drug targets.
Mass spectrometry has identified over 100,000 phosphorylation sites in the human genome.

Purpose of the Study:

To review the utility of antibody and reverse-phase protein microarrays (RPPMs) in proteomics.
To highlight challenges and solutions in utilizing these microarray technologies.
To showcase successful applications of microarrays in biomedical research.

Main Methods:

Antibody microarrays for ultra-sensitive, semi-quantitative protein and phosphorylation measurements.
Reverse-phase protein microarrays (RPPMs) for tracking target proteins across numerous samples.
Discussion of challenges including antibody specificity, cross-reactivity, low protein abundance, substoichiometric phosphorylation, and complex formation.

Main Results:

Microarrays enable parallel measurement of hundreds of targets in cells and tissues.
RPPMs allow simultaneous tracking of proteins in thousands of samples.
Over a hundred scientific reports demonstrate the benefit of these microarray technologies.

Conclusions:

Antibody and RPPMs are essential tools for broad-based, targeted proteomics research.
Addressing challenges like antibody validation and data interpretation is critical for reliable results.
Complementary validation methods such as immunoblotting and ELISA are necessary.