scholarly journals Cell-permeable bicyclic peptidyl inhibitors against T-cell protein tyrosine phosphatase from a combinatorial library

2017 ◽  
Vol 15 (45) ◽  
pp. 9595-9598 ◽  
Author(s):  
Hui Liao ◽  
Dehua Pei
Keyword(s):  
T Cell ◽  
Protein Tyrosine Phosphatase ◽  
Combinatorial Library ◽  
Tyrosine Phosphatase ◽  
Biologically Active ◽  
Cell Protein ◽  
Protein Tyrosine ◽  
Peptidyl Inhibitors

Cell-permeable, biologically active bicyclic peptidyl inhibitors against T-cell protein-tyrosine phosphatase were directly isolated from a combinatorial library.

scholarly journals Loss of T-Cell Protein Tyrosine Phosphatase Induces Recycling of the Platelet-derived Growth Factor (PDGF) β-Receptor but Not the PDGF α-Receptor

2006 ◽  
Vol 17 (11) ◽  
pp. 4846-4855 ◽  
Author(s):  
Susann Karlsson ◽  
Katarzyna Kowanetz ◽  
Åsa Sandin ◽  
Camilla Persson ◽  
Arne Östman ◽  
...  
Keyword(s):  
T Cell ◽  
Growth Factor ◽  
Cell Surface ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Dominant Negative ◽  
Platelet Derived Growth Factor ◽  
Cell Protein ◽  
Protein Tyrosine ◽  
Β Receptor

We have previously shown that the T-cell protein tyrosine phosphatase (TC-PTP) dephosphorylates the platelet-derived growth factor (PDGF) β-receptor. Here, we show that the increased PDGF β-receptor phosphorylation in TC-PTP knockout (ko) mouse embryonic fibroblasts (MEFs) occurs primarily on the cell surface. The increased phosphorylation is accompanied by a TC-PTP–dependent, monensin-sensitive delay in clearance of cell surface PDGF β-receptors and delayed receptor degradation, suggesting PDGF β-receptor recycling. Recycled receptors could also be directly detected on the cell surface of TC-PTP ko MEFs. The effect of TC-PTP depletion was specific for the PDGF β-receptor, because PDGF α-receptor homodimers were cleared from the cell surface at the same rate in TC-PTP ko MEFs as in wild-type MEFs. Interestingly, PDGF αβ-receptor heterodimers were recycling. Analysis by confocal microscopy revealed that, in TC-PTP ko MEFs, activated PDGF β-receptors colocalized with Rab4a, a marker for rapid recycling. In accordance with this, transient expression of a dominant-negative Rab4a construct increased the rate of clearance of cell surface receptors on TC-PTP ko MEFs. Thus, loss of TC-PTP specifically redirects the PDGF β-receptor toward rapid recycling, which is the first evidence of differential trafficking of PDGF receptor family members.

scholarly journals The YRD Motif Is a Major Determinant of Substrate and Inhibitor Specificity in T-cell Protein-tyrosine Phosphatase

2001 ◽  
Vol 276 (28) ◽  
pp. 26036-26043 ◽  
Author(s):  
Ernest Asante-Appiah ◽  
Kristen Ball ◽  
Kevin Bateman ◽  
Kathryn Skorey ◽  
Rick Friesen ◽  
...  
Keyword(s):  
T Cell ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Major Determinant ◽  
Cell Protein ◽  
Inhibitor Specificity ◽  
Protein Tyrosine ◽  
The Yrd

scholarly journals The role of T‐cell protein tyrosine phosphatase in epithelial carcinogenesis

2019 ◽  
Vol 58 (9) ◽  
pp. 1640-1647
Author(s):  
Liza D. Morales ◽  
Anna K. Archbold ◽  
Serena Olivarez ◽  
Thomas J. Slaga ◽  
John DiGiovanni ◽  
...  
Keyword(s):  
T Cell ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Protein ◽  
Protein Tyrosine

scholarly journals Molecular mechanism of T-cell protein tyrosine phosphatase (TCPTP) activation by mitoxantrone

2013 ◽  
Vol 1834 (10) ◽  
pp. 1988-1997 ◽  
Author(s):  
Mikko Ylilauri ◽  
Elina Mattila ◽  
Elisa M. Nurminen ◽  
Jarmo Käpylä ◽  
Sanna P. Niinivehmas ◽  
...  
Keyword(s):  
T Cell ◽  
Molecular Mechanism ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Protein ◽  
Protein Tyrosine
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