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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...

PI3K/mTOR/AKT Signaling Pathway

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a rapamycin-insensitive companion...

Receptor Tyrosine Kinases

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...

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...

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...

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Related Experiment Video

Updated: Jul 10, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Structure and function of the protein kinase R.

A J Sadler¹, B R G Williams

¹Monash Institute of Medical Research, Monash University, Melbourne, Victoria 3168, Australia.

Current Topics in Microbiology and Immunology

|November 1, 2007

Summary

Protein Kinase R (PKR) acts as a cellular stress sensor, activated by viral dsRNA and other molecules. It regulates protein synthesis and has broader roles in cell signaling, disease, and normal cell functions.

Area of Science:

Molecular Biology
Cellular Stress Response
Signal Transduction

Background:

Protein Kinase R (PKR) is an intracellular sensor.
PKR is activated by double-stranded RNA (dsRNA) during viral infections.
Activation of PKR arrests protein synthesis by phosphorylating eIF2.

Purpose of the Study:

To explore the multifaceted roles of PKR beyond viral infection.
To highlight PKR's function as a signaling molecule for diverse physiological stresses.
To investigate PKR's involvement in various cellular processes and diseases.

Main Methods:

Review of existing literature on PKR activation and substrates.
Analysis of PKR's role in response to multiple stimuli (dsRNA, PACT, heparin, etc.).

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Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

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Last Updated: Jul 10, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

Published on: March 5, 2019

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Examination of PKR's substrates and their implications in cellular regulation.

Main Results:

PKR is activated by dsRNA, PACT, and heparin, responding to indirect stimuli like LPS and ceramide.
PKR regulates protein synthesis and has additional substrates involved in transcription and signal transduction.
PKR is implicated in tumorigenesis, neurodegenerative diseases, cell differentiation, and calcification.

Conclusions:

PKR functions as a versatile signaling molecule, sensing a wide array of cellular stresses.
PKR's substrates support its roles in both infected and uninfected cells, impacting disease pathogenesis.
PKR is crucial for normal cellular processes like differentiation and calcification, in addition to stress responses.