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The protein tyrosine phosphatase PTP-Basophil/Basophil-like
- Source :
- European Journal of Biochemistry. 270:4789-4798
- Publication Year :
- 2003
- Publisher :
- Wiley, 2003.
-
Abstract
- The protein tyrosine phosphatase PTP-Basophil (PTP-Bas) and its mouse homologue, PTP-Basophil-like (PTP-BL), are high molecular mass protein phosphatases consisting of a number of diverse protein-protein interaction modules. Several splicing variants of these phosphatases are known to exist thus demonstrating the complexity of these molecules. PTP-Bas/BL serves as a central scaffolding protein facilitating the assembly of a multiplicity of different proteins mainly via five different PDZ domains. Many of these interacting proteins are implicated in the regulation of the actin cytoskeleton. However, some proteins demonstrate a nuclear function of this protein tyrosine phosphatase. PTP-Bas is involved in the regulation of cell surface expression of the cell death receptor, Fas. Moreover, it is a negative regulator of ephrinB phosphorylation, a receptor playing an important role during development. The phosphorylation status of other proteins such as RIL, IkappaBalpha and beta-catenin can also be regulated by this phosphatase. Finally, PTP-BL has been shown to be involved in the regulation of cytokinesis, the last step in cell division. Although the precise molecular function of PTP-Bas/BL is still elusive, current data suggest clearly that PTP-Bas/BL belongs to the family of PDZ domain containing proteins involved in the regulation of the cytoskeleton and of intracellular vesicular transport processes.
- Subjects :
- animal structures
Protein Conformation
PDZ domain
Phosphatase
Protein Tyrosine Phosphatase, Non-Receptor Type 13
Apoptosis
Ephrin-B1
Protein tyrosine phosphatase
Biology
Models, Biological
environment and public health
Biochemistry
Animals
Humans
fas Receptor
Phosphorylation
Cytoskeleton
In Situ Hybridization
Models, Genetic
Protein phosphatase 2
Actin cytoskeleton
Protein Structure, Tertiary
Cell biology
enzymes and coenzymes (carbohydrates)
PTPN13
RNA
Protein Tyrosine Phosphatases
Signal transduction
Cell Division
Protein Binding
Signal Transduction
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 270
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....40861527840d06d4662e49a54137c1de