Receptor protein tyrosine phosphatases and cancer: New insights from structural biology

There is general agreement that many cancers are associated with aberrant phosphotyrosine signaling, which can be caused by the inappropriate activities of tyrosine kinases or tyrosine phosphatases. Furthermore, incorrect activation of signaling pathways has been often linked to changes in adhesion...

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Bibliographic Details
Published in:Cell adhesion & migration 2012-07, Vol.6 (4), p.356-364
Main Authors: Nikolaienko, Roman M., Agyekum, Boadi, Bouyain, Samuel
Format: Article
Language:English
Subjects:
Animals
Binding
Biology
Bioscience
Calcium
Cancer
Cell
cell adhesion
Cell Communication
crystal structure
Cycle
Gene Expression
Humans
inactivating somatic mutations
Landes
Models, Molecular
Mutation
Neoplasms - enzymology
Neoplasms - genetics
Neoplasms - pathology
oncogene
Organogenesis
phosphatase
phosphorylation
Protein Interaction Domains and Motifs
Protein Structure, Quaternary
Proteins
receptor overexpression
receptor protein tyrosine phosphatase
Receptor-Like Protein Tyrosine Phosphatases - chemistry
Receptor-Like Protein Tyrosine Phosphatases - genetics
Receptor-Like Protein Tyrosine Phosphatases - metabolism
Review
tumor suppressor
Citations: Items that this one cites
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Summary:There is general agreement that many cancers are associated with aberrant phosphotyrosine signaling, which can be caused by the inappropriate activities of tyrosine kinases or tyrosine phosphatases. Furthermore, incorrect activation of signaling pathways has been often linked to changes in adhesion events mediated by cell surface receptors. Among these receptors, receptor protein tyrosine phosphatases (RPTPs) both antagonize tyrosine kinases as well as engage extracellular ligands. A recent wealth of data on this intriguing family indicates that its members can fulfill either tumor suppressing or oncogenic roles. The interpretation of these results at a molecular level has been greatly facilitated by the recent availability of structural information on the extra- and intracellular regions of RPTPs. These structures provide a molecular framework to understand how alterations in extracellular interactions can inactivate RPTPs in cancers or why the overexpression of certain RPTPs may also participate in tumor progression.
ISSN:1933-6918
1933-6926
DOI:10.4161/cam.21242