Abstract
Protein tyrosine phosphatase, PTPL1, (also known as PTPN13, FAP-1, PTP-BAS, PTP1E) is a non-receptor type PTP and, at 270 kDa, is the largest phosphatase within this group. In addition to the well-conserved PTP domain, PTPL1 contains at least 7 putative macromolecular interaction domains. This structural complexity indicates that PTPL1 may modulate diverse cellular functions, perhaps exerting both positive and negative effects. In accordance with this idea, while certain studies suggest that PTPL1 can act as a tumor-promoting gene other experimental studies have suggested that PTPL1 may function as a tumor suppressor. The role of PTPL1 in the cancer cell is therefore likely to be both complex and context dependent with possible roles including the modulation of growth, stress-response, and cytoskeletal remodeling pathways. Understanding the nature of molecular complexes containing PTPL1, its interaction partners, substrates, regulation and subcellular localization are key to unraveling the complex personality of this protein phosphatase.
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Abbreviations
- ESFT:
-
Ewing’s Sarcoma Family of Tumors
- FERM:
-
band 4.1/ezrin/radixin/moesin
- IκBα:
-
Inhibitor of nuclear factor kappa-B alpha
- KIND:
-
Kinase non-catalytic C-lobe domain
- PARG1:
-
PTPL1-associated RhoGAP1
- PDZ:
-
PSD-95/Discs-large/ZO-1
- PIP:
-
Phosphatidylinositol biphosphates
- PIP3:
-
Phosphatidylinositol triphosphates
- PKA:
-
Protein kinase-A
- PTP:
-
Protein Tyrosine Phosphatase
- TAPP:
-
Tandem-PH-domain-containing proteins
- TNFR:
-
Tumor necrosis factor-receptor
- TRIP6:
-
Thyroid Hormone Receptor-interacting Protein 6
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The authors would like to thank Toretsky Lab members for helpful discussions and Ms. Audrey Kubetin for editorial assistance.
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Abaan, O.D., Toretsky, J.A. PTPL1: a large phosphatase with a split personality. Cancer Metastasis Rev 27, 205–214 (2008). https://doi.org/10.1007/s10555-008-9114-2
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DOI: https://doi.org/10.1007/s10555-008-9114-2