scholarly journals Interactions of the Protein-tyrosine Phosphatase-α with the Focal Adhesion Targeting Domain of Focal Adhesion Kinase Are Involved in Interleukin-1 Signaling in Fibroblasts

2014 ◽  
Vol 289 (26) ◽  
pp. 18427-18441 ◽  
Author(s):  
Qin Wang ◽  
Yongqiang Wang ◽  
Dominik Fritz ◽  
Dhaarmini Rajshankar ◽  
Gregory P. Downey ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Interleukin 1 ◽  
Protein Tyrosine

scholarly journals Focal adhesion kinase regulates the phosphorylation protein tyrosine phosphatase-α at Tyr789 in breast cancer cells

2015 ◽  
Vol 11 (6) ◽  
pp. 4303-4308 ◽  
Author(s):  
XU-QIAN FANG ◽  
XIANG-FAN LIU ◽  
LING YAO ◽  
CHANG-QIANG CHEN ◽  
JIA-FEI LIN ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Focal Adhesion Kinase ◽  
Cancer Cells ◽  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Breast Cancer Cells ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine

scholarly journals Protein-tyrosine Phosphatase PTPD1 Regulates Focal Adhesion Kinase Autophosphorylation and Cell Migration

2008 ◽  
Vol 283 (16) ◽  
pp. 10919-10929 ◽  
Author(s):  
Annalisa Carlucci ◽  
Chiara Gedressi ◽  
Luca Lignitto ◽  
Luigi Nezi ◽  
Emma Villa-Moruzzi ◽  
...  
Keyword(s):  
Cell Migration ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine

scholarly journals Role of Protein-tyrosine Phosphatase SHP2in Focal Adhesion Kinase Down-regulation during Neutrophil Cathepsin G-induced Cardiomyocytes Anoikis

2006 ◽  
Vol 281 (28) ◽  
pp. 19781-19792 ◽  
Author(s):  
Khadija Rafiq ◽  
Mikhail A. Kolpakov ◽  
Malika Abdelfettah ◽  
Daniel N. Streblow ◽  
Aviv Hassid ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cathepsin G ◽  
Down Regulation ◽  
Protein Tyrosine

scholarly journals Protein-tyrosine Phosphatase Shp-2 Regulates Cell Spreading, Migration, and Focal Adhesion

1998 ◽  
Vol 273 (33) ◽  
pp. 21125-21131 ◽  
Author(s):  
De-Hua Yu ◽  
Cheng-Kui Qu ◽  
Octavian Henegariu ◽  
Xiaolan Lu ◽  
Gen-Sheng Feng
Keyword(s):  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Spreading ◽  
Protein Tyrosine

scholarly journals Protein Tyrosine Phosphatase-PEST Regulates Focal Adhesion Disassembly, Migration, and Cytokinesis in Fibroblasts

1999 ◽  
Vol 144 (5) ◽  
pp. 1019-1031 ◽  
Author(s):  
Alexandre Angers-Loustau ◽  
Jean-François Côté ◽  
Alain Charest ◽  
Donald Dowbenko ◽  
Susan Spencer ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Matrix Protein ◽  
Tyrosine Phosphatase ◽  
Control Cell ◽  
Focal Adhesions ◽  
Extracellular Matrix Protein ◽  
Cleavage Furrow ◽  
Protein Tyrosine

In this article, we show that, in transfected COS-1 cells, protein tyrosine phosphatase (PTP)-PEST translocates to the membrane periphery following stimulation by the extracellular matrix protein fibronectin. When plated on fibronectin, PTP-PEST (−/−) fibroblasts display a strong defect in motility. 3 h after plating on fibronectin, the number and size of vinculin containing focal adhesions were greatly increased in the homozygous PTP-PEST mutant cells as compared with heterozygous cells. This phenomenon appears to be due in part to a constitutive increase in tyrosine phosphorylation of p130CAS, a known PTP-PEST substrate, paxillin, which associates with PTP-PEST in vitro, and focal adhesion kinase (FAK). Another effect of this constitutive hyperphosphorylation, consistent with the focal adhesion regulation defect, is that (−/−) cells spread faster than the control cell line when plated on fibronectin. In the PTP-PEST (−/−) cells, an increase in affinity for the SH2 domains of Src and Crk towards p130CAS was also observed. In (−/−) cells, we found a significant increase in the level of tyrosine phosphorylation of PSTPIP, a cleavage furrow–associated protein that interacts physically with all PEST family members. An effect of PSTPIP hyperphosphorylation appears to be that some cells remain attached at the site of the cleavage furrow for an extended period of time. In conclusion, our data suggest PTP-PEST plays a dual role in cell cytoskeleton organization, by promoting the turnover of focal adhesions required for cell migration, and by directly or indirectly regulating the proline, serine, threonine phosphatase interacting protein (PSTPIP) tyrosine phosphorylation level which may be involved in regulating cleavage furrow formation or disassembly during normal cell division.

scholarly journals The Protein Tyrosine Phosphatase SHP-2 Regulates Interleukin-1-induced ERK Activation in Fibroblasts

2003 ◽  
Vol 278 (29) ◽  
pp. 27190-27198 ◽  
Author(s):  
Mairi MacGillivray ◽  
Maria Teresa Herrera-Abreu ◽  
Chung-Wai Chow ◽  
Christina Shek ◽  
Qin Wang ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Interleukin 1 ◽  
Erk Activation ◽  
Protein Tyrosine

scholarly journals Protein tyrosine phosphatase 1B, PTP1B, targets fak and paxillin in cell-matrix adhesions

2021 ◽  
Author(s):  
Ana E. González Wusener ◽  
Ángela González ◽  
María E. Perez Collado ◽  
Melina R. Maza ◽  
Ignacio J. General ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Bimolecular Fluorescence Complementation ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Adhesion Sites ◽  
Cell Matrix Adhesion

Protein tyrosine phosphatase 1B (PTP1B) is an established regulator of cell-matrix adhesion and motility. However, the nature of substrate targets at adhesion sites remains to be validated. Here we used Bimolecular Fluorescence Complementation (BiFC) assays in combination with a substrate trapping mutant of PTP1B to directly examine whether relevant phosphotyrosines on paxillin and FAK are substrates of the phosphatase in the context of cell-matrix adhesion sites. We find that formation of catalytic complexes at cell-matrix adhesions requires intact tyrosine residues Y31 and Y118 on paxillin and the localization of the focal adhesion kinase (FAK) at adhesion sites. In addition, we find that PTP1B specifically targets the Y925 on the focal adhesion target (FAT) domain of FAK at adhesion sites. Electrostatic analysis indicates that dephosphorylation of this residue promotes the closed conformation of the FAT 4-helix bundle, and its interaction with paxillin at adhesion sites.

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