English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/157789
Share/Impact:
Statistics
logo share SHARE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

The extended family of protein tyrosine phosphatases

AuthorsAlonso, Andrés ; Nunes-Xavier, Caroline E.; Bayón, Yolanda ; Pulido, Rafael
KeywordsPhosphorylation
Dephosphorylation
His-based phosphatase
Asp-phosphatase
Lipid phosphatase
Tyrosine phosphatase
Issue Date2016
PublisherSpringer Nature
CitationProtein Tyrosine Phosphatases: 1-23 (2016)
SeriesMethods in Molecular Biology 1447
AbstractIn higher eukaryotes, the Tyr phosphorylation status of cellular proteins results from the coordinated action of Protein Tyrosine Kinases (PTKs) and Protein Tyrosine Phosphatases (PTPs). PTPs have emerged as highly regulated enzymes with diverse substrate specificity, and proteins with Tyr-dephosphorylation or Tyr-dephosphorylation-like properties can be clustered as the PTPome. This includes proteins from the PTP superfamily, which display a Cys-based catalytic mechanism, as well as enzymes from other gene families (Asp-based phosphatases, His-based phosphatases) that have converged in protein Tyr-dephosphorylation-related functions by using non-Cys-based catalytic mechanisms. Within the Cys-based members of the PTPome, classical PTPs dephosphorylate specific phosphoTyr (pTyr) residues from protein substrates, whereas VH1-like dual-specificity PTPs dephosphorylate pTyr, pSer, and pThr residues, as well as nonproteinaceous substrates, including phosphoinositides and phosphorylated carbohydrates. In addition, several PTPs have impaired catalytic activity as a result of amino acid substitutions at their active sites, but retain regulatory functions related with pTyr signaling. As a result of their relevant biological activity, many PTPs are linked to human disease, including cancer, neurodevelopmental, and metabolic diseases, making these proteins important drug targets and molecular markers in the clinic. Here, a brief overview on the biochemistry and physiology of the different groups of proteins that belong to the mammalian PTPome is presented.
URIhttp://hdl.handle.net/10261/157789
DOI10.1007/978-1-4939-3746-2_1
Identifiersdoi: 10.1007/978-1-4939-3746-2_1
isbn: 978-1-4939-3744-8
Appears in Collections:(IBGM) Libros y partes de libros
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.