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Protein Kinases and Phosphatases

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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...

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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

Discovery of cellular substrates for protein kinase A using a peptide array screening protocol.

F Donelson Smith¹, Bret K Samelson, John D Scott

¹Howard Hughes Medical Institute, Department of Pharmacology, University of Washington School of Medicine, 1959 Pacific Avenue NE, Seattle, WA 98195, USA. smithdon@uw.edu

The Biochemical Journal

|June 8, 2011

Summary

This study identifies new substrates for protein kinase A (PKA) using peptide arrays and motif-specific antibodies. Researchers discovered that protein kinase D (PKD) and MAP-regulating kinase 3 (MARK3) are PKA substrates, along with the adapter protein RIL.

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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

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Published on: October 23, 2019

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Area of Science:

Cellular Biology
Molecular Biology
Biochemistry

Background:

Post-translational modification, particularly protein phosphorylation, is a fundamental cellular regulatory mechanism.
Protein kinases catalyze phosphorylation, influencing protein activity, localization, and stability, thereby driving cellular events.
While ~30% of intracellular proteins are phosphorylated, the full phosphoproteome remains incompletely catalogued.

Purpose of the Study:

To develop and apply a strategy using peptide arrays and motif-specific antibodies to identify novel substrate sequences for protein kinase A (PKA).
To characterize previously unrecognized PKA substrates and understand their functional implications.

Main Methods:

Utilized peptide arrays to screen for potential PKA substrates.
Employed motif-specific antibodies for validation and characterization.
Investigated PKA-mediated phosphorylation of specific proteins, including PKD, MARK3, and RIL, within cellular contexts.

Main Results:

Identified novel substrate sequences for PKA.
Demonstrated that protein kinase D (PKD) and MAP-regulating kinase 3 (MARK3) are direct substrates of PKA.
Confirmed that the adapter protein RIL is phosphorylated by PKA on Ser(119) in cells, suggesting a role in regulating cell growth.

Conclusions:

The developed strategy effectively identifies new PKA substrates.
PKA plays a role in phosphorylating PKD, MARK3, and RIL, expanding the known PKA substrate repertoire.
PKA-mediated phosphorylation of RIL on Ser(119) may be a critical regulatory mechanism influencing cell growth.