Protein Tyrosine Phosphatases

D. J. Pagliarini, Fred Robinson, C. A. Worby, J. E. Dixon

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The process of reversible phosphorylation is perhaps the cell's most prevalent means of regulation at the molecular level. It has been estimated that up to 30% of all cellular proteins are phosphorylated, and phosphorylation has been shown to play a crucial regulatory role in such diverse cellular events as metabolism, growth and differentiation, vesicular transport, and gene transcription. Phosphorylation and dephosphorylation are carried out by kinases and phosphatases, respectively. There are currently predicted to be 518 kinases and ~125 phosphatases encoded in the human genome, further underscoring the overall importance of phosphorylation in molecular regulation. Phosphatases are generally divided into two main families based on their catalytic mechanism and substrate specificity: the protein phosphatases (PPs), which exclusively desphosphorylate serine and threonine residues, and the protein tyrosine phosphatases (PTPs), which can dephosphorylate tyrosine residues, and are the focus of this article. PTPs can be further classified into subfamilies based on (1) subcellular location (receptor vs. intracellular), (2) substrate preference, and (3) three-dimensional topology. In this article, we describe the different subfamilies of PTPs and their conserved catalytic mechanism. In addition, we briefly discuss human diseases that result from disrupted PTP signaling, and discuss the pursuit of PTPs as drug targets.

Original languageEnglish (US)
Title of host publicationEncyclopedia of Biological Chemistry
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Pages648-653
Number of pages6
ISBN (Electronic)9780123786319
ISBN (Print)9780123786302
DOIs
StatePublished - Feb 15 2013
Externally publishedYes

Fingerprint

Protein Tyrosine Phosphatases
Phosphorylation
Phosphoric Monoester Hydrolases
Phosphotransferases
Genes
Phosphoprotein Phosphatases
Human Genome
Substrates
Threonine
Transcription
Substrate Specificity
Metabolism
Serine
Tyrosine
Topology
Growth
Pharmaceutical Preparations
Proteins

Keywords

  • Homodimerization
  • Laforin
  • Onco-proteins
  • Phosphoenzyme intermediate
  • Protein tyrosine kinases (PTKs)
  • Reversible phosphorylation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Pagliarini, D. J., Robinson, F., Worby, C. A., & Dixon, J. E. (2013). Protein Tyrosine Phosphatases. In Encyclopedia of Biological Chemistry: Second Edition (pp. 648-653). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-378630-2.00366-2

Protein Tyrosine Phosphatases. / Pagliarini, D. J.; Robinson, Fred; Worby, C. A.; Dixon, J. E.

Encyclopedia of Biological Chemistry: Second Edition. Elsevier Inc., 2013. p. 648-653.

Research output: Chapter in Book/Report/Conference proceedingChapter

Pagliarini, DJ, Robinson, F, Worby, CA & Dixon, JE 2013, Protein Tyrosine Phosphatases. in Encyclopedia of Biological Chemistry: Second Edition. Elsevier Inc., pp. 648-653. https://doi.org/10.1016/B978-0-12-378630-2.00366-2
Pagliarini DJ, Robinson F, Worby CA, Dixon JE. Protein Tyrosine Phosphatases. In Encyclopedia of Biological Chemistry: Second Edition. Elsevier Inc. 2013. p. 648-653 https://doi.org/10.1016/B978-0-12-378630-2.00366-2
Pagliarini, D. J. ; Robinson, Fred ; Worby, C. A. ; Dixon, J. E. / Protein Tyrosine Phosphatases. Encyclopedia of Biological Chemistry: Second Edition. Elsevier Inc., 2013. pp. 648-653
@inbook{77b70fa6fe194cad87df03f0acafd735,
title = "Protein Tyrosine Phosphatases",
abstract = "The process of reversible phosphorylation is perhaps the cell's most prevalent means of regulation at the molecular level. It has been estimated that up to 30{\%} of all cellular proteins are phosphorylated, and phosphorylation has been shown to play a crucial regulatory role in such diverse cellular events as metabolism, growth and differentiation, vesicular transport, and gene transcription. Phosphorylation and dephosphorylation are carried out by kinases and phosphatases, respectively. There are currently predicted to be 518 kinases and ~125 phosphatases encoded in the human genome, further underscoring the overall importance of phosphorylation in molecular regulation. Phosphatases are generally divided into two main families based on their catalytic mechanism and substrate specificity: the protein phosphatases (PPs), which exclusively desphosphorylate serine and threonine residues, and the protein tyrosine phosphatases (PTPs), which can dephosphorylate tyrosine residues, and are the focus of this article. PTPs can be further classified into subfamilies based on (1) subcellular location (receptor vs. intracellular), (2) substrate preference, and (3) three-dimensional topology. In this article, we describe the different subfamilies of PTPs and their conserved catalytic mechanism. In addition, we briefly discuss human diseases that result from disrupted PTP signaling, and discuss the pursuit of PTPs as drug targets.",
keywords = "Homodimerization, Laforin, Onco-proteins, Phosphoenzyme intermediate, Protein tyrosine kinases (PTKs), Reversible phosphorylation",
author = "Pagliarini, {D. J.} and Fred Robinson and Worby, {C. A.} and Dixon, {J. E.}",
year = "2013",
month = "2",
day = "15",
doi = "10.1016/B978-0-12-378630-2.00366-2",
language = "English (US)",
isbn = "9780123786302",
pages = "648--653",
booktitle = "Encyclopedia of Biological Chemistry",
publisher = "Elsevier Inc.",

}

TY - CHAP

T1 - Protein Tyrosine Phosphatases

AU - Pagliarini, D. J.

AU - Robinson, Fred

AU - Worby, C. A.

AU - Dixon, J. E.

PY - 2013/2/15

Y1 - 2013/2/15

N2 - The process of reversible phosphorylation is perhaps the cell's most prevalent means of regulation at the molecular level. It has been estimated that up to 30% of all cellular proteins are phosphorylated, and phosphorylation has been shown to play a crucial regulatory role in such diverse cellular events as metabolism, growth and differentiation, vesicular transport, and gene transcription. Phosphorylation and dephosphorylation are carried out by kinases and phosphatases, respectively. There are currently predicted to be 518 kinases and ~125 phosphatases encoded in the human genome, further underscoring the overall importance of phosphorylation in molecular regulation. Phosphatases are generally divided into two main families based on their catalytic mechanism and substrate specificity: the protein phosphatases (PPs), which exclusively desphosphorylate serine and threonine residues, and the protein tyrosine phosphatases (PTPs), which can dephosphorylate tyrosine residues, and are the focus of this article. PTPs can be further classified into subfamilies based on (1) subcellular location (receptor vs. intracellular), (2) substrate preference, and (3) three-dimensional topology. In this article, we describe the different subfamilies of PTPs and their conserved catalytic mechanism. In addition, we briefly discuss human diseases that result from disrupted PTP signaling, and discuss the pursuit of PTPs as drug targets.

AB - The process of reversible phosphorylation is perhaps the cell's most prevalent means of regulation at the molecular level. It has been estimated that up to 30% of all cellular proteins are phosphorylated, and phosphorylation has been shown to play a crucial regulatory role in such diverse cellular events as metabolism, growth and differentiation, vesicular transport, and gene transcription. Phosphorylation and dephosphorylation are carried out by kinases and phosphatases, respectively. There are currently predicted to be 518 kinases and ~125 phosphatases encoded in the human genome, further underscoring the overall importance of phosphorylation in molecular regulation. Phosphatases are generally divided into two main families based on their catalytic mechanism and substrate specificity: the protein phosphatases (PPs), which exclusively desphosphorylate serine and threonine residues, and the protein tyrosine phosphatases (PTPs), which can dephosphorylate tyrosine residues, and are the focus of this article. PTPs can be further classified into subfamilies based on (1) subcellular location (receptor vs. intracellular), (2) substrate preference, and (3) three-dimensional topology. In this article, we describe the different subfamilies of PTPs and their conserved catalytic mechanism. In addition, we briefly discuss human diseases that result from disrupted PTP signaling, and discuss the pursuit of PTPs as drug targets.

KW - Homodimerization

KW - Laforin

KW - Onco-proteins

KW - Phosphoenzyme intermediate

KW - Protein tyrosine kinases (PTKs)

KW - Reversible phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=85042781305&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85042781305&partnerID=8YFLogxK

U2 - 10.1016/B978-0-12-378630-2.00366-2

DO - 10.1016/B978-0-12-378630-2.00366-2

M3 - Chapter

AN - SCOPUS:85042781305

SN - 9780123786302

SP - 648

EP - 653

BT - Encyclopedia of Biological Chemistry

PB - Elsevier Inc.

ER -