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1 -terminal LIM domains (that bind tubulin and PTP-PEST).
2 lines that we have engineered to overexpress PTP-PEST.
3 P335PPKPPR) within the C-terminal segment of PTP-PEST.
4 major physiologically relevant substrate for PTP-PEST.
5 ify with two other nonreceptor PTPs: PEP and PTP-PEST.
6 PEST at S571, which recruits PIN1 to bind to PTP-PEST.
7 horylation and inhibition of WASP-associated PTP-PEST.
8 e N-terminal region (amino acids 294-497) of PTP-PEST.
9  novel interacting protein that bound to GST-PTP-PEST.
10 ties of VAV2 and p190RhoGAP are regulated by PTP-PEST.
11 ively modified the focal contact phosphatase PTP-PEST.
12 580), were targeted for dephosphorylation by PTP-PEST.
13 alpha(v)beta(3)-regulated phosphorylation of PTP-PEST.
14 rylation status through its association with PTP-PEST.
15 lls, CAKbeta was found to be a substrate for PTP-PEST.
16 y that these kinases might be substrates for PTP-PEST.
17 as dramatically reduced upon coexpression of PTP-PEST.
18 homologue (SKAP-Hom) as a novel substrate of PTP-PEST.
19 teraction with protein-tyrosine phosphatase (PTP)-PEST.
20 etime by recruiting leupaxin, which controls PTP-PEST activity and thereby paxillin phosphorylation a
21                                Expression of PTP-PEST also caused a reduction of phosphotyrosine on p
22 demonstrate severely reduced binding between PTP PEST and both the E250Q and A230T mutant proteins.
23 t comprised of protein tyrosine phosphatase (PTP)-PEST and the extracellular matrix (ECM) adhesion re
24                          Finally, endogenous PTP-PEST and endogenous CAKbeta were found to localize t
25 ST by PIN1 increases the interaction between PTP-PEST and FAK, which leads to the dephosphorylation o
26 y specific nature of the interaction between PTP-PEST and p130cas appears to result from a combinatio
27 sults suggest that CAKbeta is a substrate of PTP-PEST and that FAK is a poor PTP-PEST substrate.
28  the p130cas SH3 domain is to associate with PTP-PEST and thereby facilitate the dephosphorylation of
29 k also binds phosphatases, including PTPN12 (PTP-PEST) and immune-cell PTPN22 (LYP/Pep), which dephos
30 c, PYK2, WASP, protein-tyrosine phosphatase (PTP)-PEST, and Pro-Ser-Thr phosphatase-interacting prote
31    In contrast, FAK was a poor substrate for PTP-PEST, and treatment with PTP-PEST had no effect on F
32                 Therefore, both paxillin and PTP-PEST appear to be critical elements in the generatio
33 entify p130(cas) as a specific substrate for PTP-PEST are potentially applicable to any PTP and shoul
34 , Pyk2, PAK and SRC), tyrosine phosphatases (PTP-PEST), ARF-GAP proteins (p95pkl, PAG3) and papilloma
35 n vitro kinase assays identified phosphatase PTP-PEST as a Pim1 substrate and phosphatase SHP-1 as a
36  kinase 1 and 2-dependent phosphorylation of PTP-PEST at S571, which recruits PIN1 to bind to PTP-PES
37                                          The PTP-PEST binding site on paxillin has been mapped to the
38 ve c-Src or the protein tyrosine phosphatase PTP-PEST, but not by dominant negative Abl.
39 ve investigated the substrate specificity of PTP-PEST by a novel substrate-trapping approach in combi
40          Isomerization of the phosphorylated PTP-PEST by PIN1 increases the interaction between PTP-P
41                                     Further, PTP-PEST can negatively regulate CAKbeta signaling by in
42 talytic domains of the tyrosine phosphatases PTP-PEST, CD45, and PTPbeta did not interact with protei
43 to phosphatase and small interference RNA to PTP-PEST confirmed the involvement of PTP-PEST in sealin
44 ytic domain of protein-tyrosine phosphatase (PTP)-PEST contains a binding site for the focal adhesion
45 ognition mechanisms; the catalytic domain of PTP-PEST contributes specificity to the interaction with
46 osine kinase(s) and the tyrosine phosphatase PTP-PEST coordinate the formation of the sealing ring an
47                      These data suggest that PTP-PEST couples protrusion and retraction by acting on
48 ced c-Abl kinase activation was prolonged in PTP-PEST-deficient cells.
49 l activity: c-Abl was hyperphosphorylated in PTP-PEST-deficient cells; disruption of the c-Abl-PSTPIP
50                                              PTP-PEST-deficient endothelial cells displayed increased
51  primary endothelial cells from an inducible PTP-PEST-deficient mouse, we found that PTP-PEST is not
52            Furthermore, cells overexpressing PTP-PEST demonstrate significantly reduced levels of ass
53 amin-A in HeLa cells was found to reduce the PTP-PEST-dependent multinucleation phenotype.
54                         We further show that PTP-PEST directly targets the upstream regulators of Rac
55             The protein tyrosine phosphatase PTP-PEST displays remarkable substrate specificity, in v
56 3 domain-mediated association of p130cas and PTP-PEST dramatically increases the efficiency of the in
57              Dephosphorylation of CAKbeta by PTP-PEST dramatically inhibited CAKbeta kinase activity.
58                           beta8 integrin and PTP-PEST form protein complexes at the leading edge of m
59 r substrate for PTP-PEST, and treatment with PTP-PEST had no effect on FAK kinase activity.
60                                              PTP-PEST has previously been implicated in the regulatio
61 0.3 microM, 10-fold selectivity for LYP over PTP-PEST, HePTP, and CD45 in vitro, and activity in cell
62 an important mechanism for the regulation of PTP-PEST in activated Ras-induced tumor progression.
63 lains at least in part the essential role of PTP-PEST in embryonic development and viability.
64       Herein we addressed the involvement of PTP-PEST in endothelial cell functions using a combinati
65                               By eliminating PTP-PEST in endothelial cells in vivo, we obtained evide
66 ivo, we obtained evidence that expression of PTP-PEST in endothelial cells is required for normal vas
67 rther support of this finding, expression of PTP-PEST in HeLa cells resulted in the formation of mult
68 colocalization with c-Src, PYK2, PSTPIP, and PTP-PEST in immunostaining analyses.
69 strate-trapping assays and overexpression of PTP-PEST in mammalian cells, CAKbeta was found to be a s
70      Our studies suggest potential roles for PTP-PEST in regulation of p130(cas) function.
71 RNA to PTP-PEST confirmed the involvement of PTP-PEST in sealing ring formation and bone resorption.
72 which was preferentially dephosphorylated by PTP-PEST in vitro.
73 1, and the oxidase, whereas the knockdown of PTP-PEST increased ruffling independent of oxidase activ
74                                   To confirm PTP-PEST interaction with SKAP-Hom, in vitro pull down a
75                        The complexity of the PTP-PEST interactome underscores the necessity to identi
76                Protein tyrosine phosphatase (PTP)-PEST is a critical regulator of cell adhesion and m
77                Protein-tyrosine phosphatase (PTP)-PEST is a cytoplasmic tyrosine phosphatase that can
78                                              PTP-PEST is a cytoplasmic protein-tyrosine phosphatase (
79             The protein tyrosine phosphatase PTP-PEST is a cytosolic enzyme that displays a remarkabl
80                                              PTP-PEST is a cytosolic ubiquitous protein tyrosine phos
81                                Among others, PTP-PEST is a key regulator of cellular motility and cyt
82                                   Therefore, PTP-PEST is a key regulator of integrin-mediated functio
83                                              PTP-PEST is a ubiquitously expressed, cytosolic, mammali
84 ible PTP-PEST-deficient mouse, we found that PTP-PEST is not needed for endothelial cell differentiat
85              However, the mechanism by which PTP-PEST is regulated in response to oncogenic signaling
86 sults suggest that one physiological role of PTP-PEST is to dephosphorylate p130(Cas), thereby contro
87  here that the protein-tyrosine phosphatase, PTP-PEST, is required for the coupling of protrusion and
88  of c-Src or down-regulation of SHP-2 and/or PTP-PEST may promote cancer metastases and invasion by r
89                                            A PTP-PEST mutant defective for binding p130(cas) does not
90                                            A PTP-PEST mutant lacking Pro4 and unable to bind filamin-
91                                              PTP-PEST null cells exhibit enhanced Rac1 activity and d
92                                              PTP-PEST null fibroblasts, which are blocked in migratio
93                               The amounts of PTP-PEST or PTP1D in the soluble fractions were not alte
94 oach is demonstrated by regulating PTP1B and PTP-PEST phosphatases.
95                                              PTP-PEST plays a key role in the dynamic regulation of f
96 phosphorylation of RhoGDI1 by integrin-bound PTP-PEST promotes RhoGDI1 release from the membrane and
97               Further, we identify SHP-2 and PTP-PEST (protein-tyrosine phosphatase proline-, glutama
98                Protein-tyrosine phosphatase (PTP)-PEST (PTPN12) is ubiquitously expressed.
99                      Transient expression of PTP-PEST reduced tyrosine phosphorylation of p130(cas),
100 ver, these results open new avenues by which PTP-PEST regulates cellular migration, a hallmark of met
101  S-transferase-fused proline-rich regions of PTP-PEST revealed coprecipitation of WASP, PYK2, c-Src,
102                                 In contrast, PTP-PEST, Shp2, and PTPmu did not interact with these pr
103 ssentially unchanged in cells overexpressing PTP-PEST; similarly, the extent and time course of mitog
104 lts demonstrate that paxillin can serve as a PTP-PEST substrate in vivo and support the model that a
105 substrate of PTP-PEST and that FAK is a poor PTP-PEST substrate.
106 oupling of the protein tyrosine phosphatase (PTP)-PEST to CD2.
107  recruitment of the protein-Tyr phosphatase (PTP)-PEST to the FA complex are required for Abeta-induc
108 ration and a failure of cells overexpressing PTP-PEST to accomplish the normally observed redistribut
109 ytic domain interaction recruits paxillin to PTP-PEST to facilitate its dephosphorylation.
110 inding and prolyl isomerization of FAK cause PTP-PEST to interact with and dephosphorylate FAK Y397.
111 alanine significantly impairs the ability of PTP-PEST to recognise tyrosine phosphorylated p130cas as
112 ovel PTP related to the previously described PTP PEST type enzymes, murine PTP PEP and murine/human P
113  have investigated the physiological role of PTP-PEST using Rat1 fibroblast-derived stable cell lines
114                            The inhibition of PTP-PEST was accompanied by an increase in tyrosine phos
115 cally, the activity of SHP-2, PTP-1beta, and PTP-PEST was enhanced by LKB1-expressing cells.
116           The site of filamin interaction on PTP-PEST was mapped to the fourth proline-rich region (P
117 ype enzymes, murine PTP PEP and murine/human PTP PEST, was also observed.
118 n of the same signaling proteins, as well as PTP-PEST, was observed with glutathione S-transferase-fu
119 strate, mutant (substrate-trapping) forms of PTP-PEST were generated which lack catalytic activity bu
120 hosphorylates FAK S910 and recruits PIN1 and PTP-PEST, which colocalize with FAK at the lamellipodia
121 activity of the protein tyrosine phosphatase PTP-PEST, which controls paxillin phosphorylation, requi
122                     Expression of mutants of PTP-PEST with deletions in the paxillin-binding site did
123   Hence, we conclude that the interaction of PTP-PEST with filamin-A may function in the control of c
124 tion of the regulatory phosphatases PTEN and PTP-PEST, with consequent activation of focal adhesion k
125                            Given the role of PTP-PEST, wound-healing and trans-well migration assays

 
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