Intra-cellular tyrosine kinase

Rosalyn Irby, Timothy J. Yeatman

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Introduction Protein kinases are proteins that enzymatically add a phosphate, obtained from ATP, to an OH group on certain amino acids in a protein. They are divided into two major groups: serine/threonine kinases phosphorylate serine or threonine residues; tyrosine kinases phosphorylate tyrosine residues (1). Dual-specificity kinases, such as Mek, phosphorylate all three amino acid residues. Phosphorylation causes a conformational change in the target protein by the addition of a bulky, charged group (Figure 19.1) to the protein. This causes alteration of the activity, subcellular location, or protein–protein interactions of phosphorylated proteins. Phosphorylation is a rapid method of activating and inactivating proteins and significantly altering pathway activities. Phosphorylation regulates cell adhesion, cell-cycle progression, transcription-factor activity, and general metabolism in the cell. As a result, phosphorylation events must be tightly regulated. Most tyrosine kinase targets have an associated protein phosphatase, designed to reverse the effects of phosphorylation rapidly. Often phosphorylation results in the addition or removal of a regulatory protein that either interferes with binding of the target protein to a substrate or maintains it in a separate subcellular compartment away from the substrate. Perturbation of the pathways can cause dysregulation of cellular activities and lead to a number of disorders, including malignancy. It has been stated that cancer is fundamentally a disease of aberrant kinase activity and signal transduction (2).

Original languageEnglish (US)
Title of host publicationMolecular Oncology
Subtitle of host publicationCauses of Cancer and Targets for Treatment
PublisherCambridge University Press
Pages231-242
Number of pages12
ISBN (Electronic)9781139046947
ISBN (Print)9780521876629
DOIs
StatePublished - Jan 1 2015

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Protein-Tyrosine Kinases
Phosphorylation
Proteins
Phosphotransferases
General Transcription Factors
Amino Acids
Phosphoprotein Phosphatases
Protein-Serine-Threonine Kinases
Threonine
Cell Adhesion
Protein Kinases
Serine
Tyrosine
Signal Transduction
Neoplasms
Cell Cycle
Carrier Proteins
Adenosine Triphosphate
Phosphates

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

Irby, R., & Yeatman, T. J. (2015). Intra-cellular tyrosine kinase. In Molecular Oncology: Causes of Cancer and Targets for Treatment (pp. 231-242). Cambridge University Press. https://doi.org/10.1017/CBO9781139046947.020
Irby, Rosalyn ; Yeatman, Timothy J. / Intra-cellular tyrosine kinase. Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press, 2015. pp. 231-242
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Irby, R & Yeatman, TJ 2015, Intra-cellular tyrosine kinase. in Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press, pp. 231-242. https://doi.org/10.1017/CBO9781139046947.020

Intra-cellular tyrosine kinase. / Irby, Rosalyn; Yeatman, Timothy J.

Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press, 2015. p. 231-242.

Research output: Chapter in Book/Report/Conference proceedingChapter

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Irby R, Yeatman TJ. Intra-cellular tyrosine kinase. In Molecular Oncology: Causes of Cancer and Targets for Treatment. Cambridge University Press. 2015. p. 231-242 https://doi.org/10.1017/CBO9781139046947.020