scholarly journals Importance of Protein-tyrosine Phosphatase-α Catalytic Domains for Interactions with SHP-2 and Interleukin-1-induced Matrix Metalloproteinase-3 Expression

2010 ◽  
Vol 285 (29) ◽  
pp. 22308-22317 ◽  
Author(s):  
Qin Wang ◽  
Dhaarmini Rajshankar ◽  
Carol Laschinger ◽  
Ilana Talior-Volodarsky ◽  
Yongqiang Wang ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Interleukin 1 ◽  
Protein Tyrosine ◽  
Matrix Metalloproteinase 3 ◽  
Catalytic Domains

scholarly journals Intra- and intermolecular interactions of the catalytic domains of human CD45 protein tyrosine phosphatase

FEBS Letters ◽  
2000 ◽  
Vol 468 (1) ◽  
pp. 68-72 ◽  
Author(s):  
Keiko Hayami-Noumi ◽  
Tomofusa Tsuchiya ◽  
Yoshinori Moriyama ◽  
Takato Noumi
Keyword(s):  
Intermolecular Interactions ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Catalytic Domains

scholarly journals Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts

2014 ◽  
Vol 25 (11) ◽  
pp. 1808-1818 ◽  
Author(s):  
Eynat Finkelshtein ◽  
Sutada Lotinun ◽  
Einat Levy-Apter ◽  
Esther Arman ◽  
Jeroen den Hertog ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Bone Matrix ◽  
Protein Tyrosine Phosphatases ◽  
Structure Stability ◽  
Cellular Organization ◽  
Production Structure ◽  
Protein Tyrosine ◽  
Catalytic Domains

Female mice lacking protein tyrosine phosphatase ε (PTP ε) are mildly osteopetrotic. Osteoclasts from these mice resorb bone matrix poorly, and the structure, stability, and cellular organization of their podosomal adhesion structures are abnormal. Here we compare the role of PTP ε with that of the closely related PTP α in osteoclasts. We show that bone mass and bone production and resorption, as well as production, structure, function, and podosome organization of osteoclasts, are unchanged in mice lacking PTP α. The varying effects of either PTP on podosome organization in osteoclasts are caused by their distinct N-termini. Osteoclasts express the receptor-type PTP α (RPTPa), which is absent from podosomes, and the nonreceptor form of PTP ε (cyt-PTPe), which is present in these structures. The presence of the unique 12 N-terminal residues of cyt-PTPe is essential for podosome regulation; attaching this sequence to the catalytic domains of PTP α enables them to function in osteoclasts. Serine 2 within this sequence regulates cyt-PTPe activity and its effects on podosomes. We conclude that PTPs α and ε play distinct roles in osteoclasts and that the N-terminus of cyt-PTPe, in particular serine 2, is critical for its function in these cells.

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-α and Src Functionally Link Focal Adhesions to the Endoplasmic Reticulum to Mediate Interleukin-1-induced Ca2+Signaling

2009 ◽  
Vol 284 (31) ◽  
pp. 20763-20772 ◽  
Author(s):  
Qin Wang ◽  
Dhaarmini Rajshankar ◽  
Donald R. Branch ◽  
Katherine A. Siminovitch ◽  
Maria Teresa Herrera Abreu ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Interleukin 1 ◽  
Focal Adhesions ◽  
Protein Tyrosine
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