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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 homologue (SKAP-Hom) as a novel substrate of PTP-PEST.
13 580), were targeted for dephosphorylation by PTP-PEST.
14 alpha(v)beta(3)-regulated phosphorylation of PTP-PEST.
15 rylation status through its association with PTP-PEST.
16 lls, CAKbeta was found to be a substrate for PTP-PEST.
17 y that these kinases might be substrates for PTP-PEST.
18 as dramatically reduced upon coexpression of PTP-PEST.
19 teraction with protein-tyrosine phosphatase (PTP)-PEST.
21 demonstrate severely reduced binding between PTP PEST and both the E250Q and A230T mutant proteins.
22 t comprised of protein tyrosine phosphatase (PTP)-PEST and the extracellular matrix (ECM) adhesion re
24 ST by PIN1 increases the interaction between PTP-PEST and FAK, which leads to the dephosphorylation o
25 y specific nature of the interaction between PTP-PEST and p130cas appears to result from a combinatio
27 the p130cas SH3 domain is to associate with PTP-PEST and thereby facilitate the dephosphorylation of
28 c, PYK2, WASP, protein-tyrosine phosphatase (PTP)-PEST, and Pro-Ser-Thr phosphatase-interacting prote
29 In contrast, FAK was a poor substrate for PTP-PEST, and treatment with PTP-PEST had no effect on F
31 entify p130(cas) as a specific substrate for PTP-PEST are potentially applicable to any PTP and shoul
32 , Pyk2, PAK and SRC), tyrosine phosphatases (PTP-PEST), ARF-GAP proteins (p95pkl, PAG3) and papilloma
33 n vitro kinase assays identified phosphatase PTP-PEST as a Pim1 substrate and phosphatase SHP-1 as a
34 kinase 1 and 2-dependent phosphorylation of PTP-PEST at S571, which recruits PIN1 to bind to PTP-PES
37 ve investigated the substrate specificity of PTP-PEST by a novel substrate-trapping approach in combi
40 talytic domains of the tyrosine phosphatases PTP-PEST, CD45, and PTPbeta did not interact with protei
41 to phosphatase and small interference RNA to PTP-PEST confirmed the involvement of PTP-PEST in sealin
42 ytic domain of protein-tyrosine phosphatase (PTP)-PEST contains a binding site for the focal adhesion
43 ognition mechanisms; the catalytic domain of PTP-PEST contributes specificity to the interaction with
44 osine kinase(s) and the tyrosine phosphatase PTP-PEST coordinate the formation of the sealing ring an
47 l activity: c-Abl was hyperphosphorylated in PTP-PEST-deficient cells; disruption of the c-Abl-PSTPIP
49 primary endothelial cells from an inducible PTP-PEST-deficient mouse, we found that PTP-PEST is not
54 3 domain-mediated association of p130cas and PTP-PEST dramatically increases the efficiency of the in
59 0.3 microM, 10-fold selectivity for LYP over PTP-PEST, HePTP, and CD45 in vitro, and activity in cell
60 an important mechanism for the regulation of PTP-PEST in activated Ras-induced tumor progression.
64 ivo, we obtained evidence that expression of PTP-PEST in endothelial cells is required for normal vas
65 rther support of this finding, expression of PTP-PEST in HeLa cells resulted in the formation of mult
67 strate-trapping assays and overexpression of PTP-PEST in mammalian cells, CAKbeta was found to be a s
69 RNA to PTP-PEST confirmed the involvement of PTP-PEST in sealing ring formation and bone resorption.
71 1, and the oxidase, whereas the knockdown of PTP-PEST increased ruffling independent of oxidase activ
82 ible PTP-PEST-deficient mouse, we found that PTP-PEST is not needed for endothelial cell differentiat
84 sults suggest that one physiological role of PTP-PEST is to dephosphorylate p130(Cas), thereby contro
85 here that the protein-tyrosine phosphatase, PTP-PEST, is required for the coupling of protrusion and
86 of c-Src or down-regulation of SHP-2 and/or PTP-PEST may promote cancer metastases and invasion by r
93 phosphorylation of RhoGDI1 by integrin-bound PTP-PEST promotes RhoGDI1 release from the membrane and
97 ver, these results open new avenues by which PTP-PEST regulates cellular migration, a hallmark of met
98 S-transferase-fused proline-rich regions of PTP-PEST revealed coprecipitation of WASP, PYK2, c-Src,
100 ssentially unchanged in cells overexpressing PTP-PEST; similarly, the extent and time course of mitog
101 lts demonstrate that paxillin can serve as a PTP-PEST substrate in vivo and support the model that a
104 recruitment of the protein-Tyr phosphatase (PTP)-PEST to the FA complex are required for Abeta-induc
105 ration and a failure of cells overexpressing PTP-PEST to accomplish the normally observed redistribut
107 inding and prolyl isomerization of FAK cause PTP-PEST to interact with and dephosphorylate FAK Y397.
108 alanine significantly impairs the ability of PTP-PEST to recognise tyrosine phosphorylated p130cas as
109 ovel PTP related to the previously described PTP PEST type enzymes, murine PTP PEP and murine/human P
110 have investigated the physiological role of PTP-PEST using Rat1 fibroblast-derived stable cell lines
115 n of the same signaling proteins, as well as PTP-PEST, was observed with glutathione S-transferase-fu
116 strate, mutant (substrate-trapping) forms of PTP-PEST were generated which lack catalytic activity bu
117 hosphorylates FAK S910 and recruits PIN1 and PTP-PEST, which colocalize with FAK at the lamellipodia
119 Hence, we conclude that the interaction of PTP-PEST with filamin-A may function in the control of c
120 tion of the regulatory phosphatases PTEN and PTP-PEST, with consequent activation of focal adhesion k
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