ライフサイエンスコーパス: PTB domain

1 at complements an apolar surface of the CKA1 PTB domain.

2 ells depends on the presence of a functional PTB domain.

3 r domain that is immediately adjacent to the PTB domain.

4 l phosphates bind the PH domain, but not the PTB domain.

5 both Syk tyrosine 317 and a functional c-Cbl PTB domain.

6 onger binds phosphotyrosine residues via its PTB domain.

7 n the region of Nak that interacts with Numb PTB domain.

8 rucial for phosphopeptide binding to the Shc PTB domain.

9 nding to the activated receptor via a single PTB domain.

10 phospholipids as a second ligand for the Shc PTB domain.

11 ULP bound directly to GDP-bound Arf6 via its PTB domain.

12 us, including beta 3-integrin binding to the PTB domain.

13 karyotes and nearly 60 human proteins having PTB domains.

14 ics of the cognate ligands for each group of PTB domains.

15 m the canonical NPXY motif targeted by other PTB domains.

16 addition to the RGS domain, contains PDZ and PTB domains.

17 ligands are recognized by the Shc and IRS-1 PTB domains.

18 gth of interaction with both the Shc SH2 and PTB domains.

19 orylated peptides bound to the Shc and IRS-1 PTB domains.

20 ferometry, revealing the role of SH2 and the PTB domains.

21 representing nearly 75% of proteins encoding PTB domains.

22 edominantly via its phosphotyrosine-binding (PTB) domain.

23 that it resembles a phosphotyrosine-binding (PTB) domain.

24 H2) domain, and the phosphotyrosine binding (PTB) domain.

25 s via an N-terminal phosphotyrosine-binding (PTB) domain.

26 that constitutes a phosphotyrosine binding (PTB) domain.

27 n aPKC (PKC3) via a phosphotyrosine binding (PTB) domain.

28 y (PH) domain and a Phosphotyrosine Binding (PTB) domain.

29 interacts with its phosphotyrosine binding (PTB) domain.

30 as well as the ShcD phosphotyrosine-binding (PTB) domain.

31 th any known SH2 or phosphotyrosine-binding (PTB) domain.

32 h an amino-terminal phosphotyrosine binding (PTB) domain.

33 gh their N-terminal phosphotyrosine binding (PTB) domains.

34 omology 2 (SH2) and phosphotyrosine-binding (PTB) domains.

35 s containing SH2 or phosphotyrosine-binding (PTB) domains.

36 mology 2 (SH2) and phospho-tyrosine binding (PTB) domains.

37 n homology (PH) and phosphotyrosine binding (PTB) domains.

38 To identify binding targets for the hJIP-1 PTB domain, a mouse embryo cDNA library was screened usi

39 rises an N-terminal phosphotyrosine binding (PTB) domain, a C-terminal Src homology 2 (SH2) domain an

40 trated that deletion of either the PH or the PTB domain abolished insulin-stimulated phosphorylation

41 The PTB domain also binds specifically to phospholipid bilay

42 of an unstructured region C-terminal to the PTB domain alters local conformation and dynamics of the

43 containing pleckstrin homology [PH] domain, PTB domain and Leucine zipper motif 1) APPL1 for OCRL bi

44 Both Mint1 PTB domain and Mso1p induce vesicle aggregation/clusteri

45 Thus, a PTB domain and PSDs collaborate in a novel fashion in CK

46 a short alpha-helix that folds back onto the PTB domain and sterically hinders APP binding.

47 1-CCM2 interaction by destabilizing the CCM2 PTB domain and that a KRIT1 mutation also disrupts this

48 plasmic domain and between the carboxyl Fe65 PTB domain and the APP cytoplasmic domain.

49 Functional analysis of the N-terminal PTB domain and the C-terminal PRR domain of LvNumb shows

50 ieved through independent mutagenesis of the PTB domain and the CH1 tyrosine residues, and successive

51 that MINTs bind Arfs through a region of the PTB domain and the PDZ2 domain, and Arf-MINT interaction

52 transiently transfected PC12 cells, the ShcA PTB domain and tyrosine phosphorylation in the CH1 domai

53 ified which deletes a critical region of the PTB domain and which does not interact with the EGFR nor

54 ns, an NH2-terminal phosphotyrosine binding (PTB) domain and a COOH-terminal Src homology 2 (SH2) dom

55 logy (PH) domain, a phosphotyrosine binding (PTB) domain and a leucine zipper, classes of motifs defi

56 of IRS-1 contains a phosphotyrosine binding (PTB) domain and a pleckstrin homology (PH) domain, both

57 -6 is composed of a phosphotyrosine-binding (PTB) domain and a proline-rich C-terminal domain with no

58 via its C-terminal phosphotyrosine binding (PTB) domain and affects APP processing and Abeta product

59 ays using the Dok-6 phosphotyrosine binding (PTB) domain and GDNF-activated Ret indicate that Dok-6 b

60 in homology domain, phosphotyrosine binding (PTB) domain and leucine zipper motif).

61 ween the amino Fe65 phosphotyrosine binding (PTB) domain and LRP cytoplasmic domain and between the c

62 , hCED-6 contains a phosphotyrosine-binding (PTB) domain and potential Src-homology domain 3 (SH3) bi

63 with TBC1D1 via its phosphotyrosine binding (PTB) domains and their interactions with TBC1D1 were una

64 ps around the beta sandwich structure of the PTB domain, and its binding is possibly regulated by con

65 APPL1 (adaptor protein containing PH domain, PTB domain, and leucine zipper motif 1) is an Akt/protei

66 ceptors through its phosphotyrosine-binding (PTB) domain, and a role for the PTB domain in phosphotyr

67 logy (PH) domain, a phosphotyrosine-binding (PTB) domain, and C-terminal sites of tyrosine phosphoryl

68 mology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper motif (APPL)-positive en

69 mology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper motif 1 (APPL1) in regul

70 logy (PH) domain, a phosphotyrosine binding (PTB) domain, and, spread over the C-terminal portion, 12

71 Furthermore, the PH and PTB domains are highly homologous (at least 40% identica

72 s of the adapter proteins outside of the SH2/PTB domains are important for stabilizing the binding of

73 st that, in contrast to the SH2 domains, the PTB domains are primarily peptide-binding domains that h

74 n homology (PH) and phosphotyrosine binding (PTB) domains are structurally related regulatory modules

75 ide further support for a role of the TBC1D1 PTB domains as a scaffold for a range of Rab regulators,

76 omology 2 (SH2) and phosphotyrosine binding (PTB) domain, as well as microarrays of mouse PDZ domains

77 In contrast, the PTB domain associated quite well with the receptor yet h

78 ion of the beta8-strand directly weakens the PTB domain association with the FGFR ligand.

79 omology 2 (SH2) and phosphotyrosine binding (PTB) domains at the C terminus of tensin proteins.

80 ckstrin homology-phosphotyrosine binding (PH-PTB) domains at their amino termini.

81 n homology (PH) and phosphotyrosine binding (PTB) domains at their N termini.

82 suggests that DAB binds SEV directly via its PTB domain, becomes tyrosine phosphorylated upon SEV act

83 PTB domains bind both peptides and headgroups of phospha

84 PTB domains bind to the consensus sequence FXNPXY, corre

85 e corresponding amino acids found in the Shc PTB domain binding site of TrkA results in even stronger

86 gulation of ZAP-70 and predict potential Cbl-PTB domain binding sites on other protein tyrosine kinas

87 mal titration calorimetry that the FRS2alpha PTB domain binding to peptides derived from TRKs or FGFR

88 COS-7 cells, we investigated the role of Cbl PTB domain binding to Syk Tyr323 in the negative regulat

89 The PTB domain binds peptide and Ins-1,4,5-P(3) (but not Ins

90 Unlike IRS-1, the Shc PTB domain binds poorly to the insulin-receptor (IR) bet

91 Simultaneously, the Anks1a PTB domain binds Sec23.

92 The mDab1 PTB domain binds to phosphotyrosine-containing proteins

93 nism where the CCM2 phosphotyrosine binding (PTB) domain binds the ubiquitin ligase (E3) Smurf1, cont

94 volved in cell migration) and their isolated PTB domain bound to integrin tails.

95 We found that the Numb PTB domain but not the Shc PTB domain interacts with Nak

96 Shc-PP2A association is mediated by the Shc PTB domain but the interaction is independent of phospho

97 oinositides contact different regions of the PTB domain, but can stably anchor Dab2 to the membrane s

98 terminal PRR domain of LvNumb shows that the PTB domain, but not the PRR domain, is sufficient to rec

99 Because the Shc PTB domain can interact with phospholipids, we postulate

100 PTB domains can be inhibited selectively in cells and re

101 ro studies suggested that binding of SH2 and PTB domains can enhance protein phosphorylation by prote

102 The structure of PTB domains confers specificity for binding peptides hav

103 ases then provides binding sites for SH2 and PTB domain containing molecules in a paradigm of recepto

104 We found that DAB, a PTB domain containing signaling protein that is involved

105 APP interacts with phosphotyrosine binding (PTB) domain containing proteins (Fe65, X11, mDab-1, and

106 In Caenorhabditis elegans, the PDZ and PTB domain-containing protein LIN-10 is required both fo

107 RS docking and suggest that I4R docking to a PTB domain-containing protein regulates activation of th

108 h classes of PTB domains, making them a dual PTB domain-containing protein.

109 n beta tails interact with a large number of PTB domain-containing proteins through a structurally co

110 models for ligand-induced recruitment of SH2/PTB domain-containing proteins to autophosphorylation si

111 We show that the phosphotyrosine-binding (PTB) domain-containing protein Disabled (DAB) binds to t

112 sites for several protein tyrosine binding (PTB) domain-containing proteins such as IRS1 and Shc and

113 cytoplasmic tail to phosphotyrosine-binding (PTB) domain-containing proteins, an interaction proposed

114 GULP/CED-6 is a phosphotyrosine binding (PTB)-domain-containing adaptor protein linked to engulfm

115 Because PTB-domain-containing adaptor proteins influence endocyt

116 n [15, 16], our data support a model wherein PTB-domain-containing adaptor proteins regulate Arf fami

117 s) causes activation, whereas numerous other PTB-domain-containing proteins bind integrins without ac

118 we first identified the residues within the PTB domain critical for phospholipid binding in vitro.

119 y 2 domain (SH2) or phosphotyrosine-binding (PTB) domain deletion mutants by biolayer interferometry,

120 The structure of the Shc PTB domain demonstrated a striking homology to the struc

121 ZAP-70 overexpression is blocked by Cbl in a PTB domain-dependent manner.

122 Cbl acts as a dominant negative to block the PTB domain-dependent negative regulatory role of endogen

123 These results identify a potential Cbl-PTB domain-dependent role for Cbl in the negative regula

124 We also observed that PTB domain-dependent targeting to the membrane preceded

125 ich conformational dynamics of the FRS2alpha PTB domain dictates its association with either fibrobla

126 gment, but constructs containing only single PTB domains did not affect APP or ApoEr2 processing.

127 and ICAP1 bound to CCM1 via their respective PTB domains differentially influence the subcellular loc

128 find that the CCM2 phosphotyrosine binding (PTB) domain displays a preference toward the third of th

129 Ligand binding to the PTB domain does not affect this.

130 The signaling complexes organized by PTB domain encoded proteins are largely unknown and repr

131 Six PTB domain encoded proteins have been found to have muta

132 omology 2 (SH2) and phosphotyrosine binding (PTB) domain encoded in the human genome to measure the e

133 e that Syk phosphotyrosine 317 and the c-Cbl PTB domain enhance, but are not required for, all intera

134 high-affinity interactions, such as SH2 and PTB domains, equilibrium dissociation constants (K(D)s)

135 H has an N-terminal phosphotyrosine-binding (PTB) domain evolutionarily related to that found in Disa

136 such as oligophrenin-1 and Graf, whereas its PTB domain exhibits homology with CED-6, an adaptor prot

137 e Shc to the plasma membrane through the Shc PTB domain facilitating phosphorylation by the insulin r

138 Our data confirm the importance of the PTB domain for Numb function but strongly suggest that t

139 These results suggest that inhibition of PTB domain function in IRS-1 by phosphorylation of Ser(3

140 Proteins encoding phosphotyrosine binding (PTB) domains function as adaptors or scaffolds to organi

141 e N-terminal TBC1D1 phosphotyrosine-binding (PTB) domain has shown a replicated association with fami

142 ructural and biochemical studies of the Dab1 PTB domain have demonstrated that this domain binds to b

143 indicating a new molecular function for the PTB domain; (iii) that growth factor stimulation, or sma

144 ine-binding (PTB) domain, and a role for the PTB domain in phosphotyrosine-mediated signaling has bee

145 ults demonstrate a critical role for the Cbl PTB domain in the recruitment of Cbl to Syk and in Cbl-m

146 d between the Munc-18-1 binding site and the PTB domain in X11alpha.

147 present the crystal structure of the Dok7 PH-PTB domains in complex with a phosphopeptide representin

148 P-1 that contains a phosphotyrosine binding (PTB) domain in addition to a JNK binding domain and an S

149 ral analysis of Shc phosphotyrosine-binding (PTB) domain in complex with the bi-phosphorylated beta(3

150 ue located near the phosphotyrosine-binding (PTB) domain in IRS-1 (Ser(307) in rat IRS-1 or Ser(312)

151 lves interaction of phosphotyrosine-binding (PTB) domain in the N-terminal head of talin (talin-H) wi

152 A PTB domain-inactivating point mutation (G306E), correspo

153 ted how phosphoinositide binding by the Dab1 PTB domain influences Reelin signal transduction.

154 The PTB domain inhibitor had less influence on epidermal gro

155 Dab2, through its phosphotyrosine-binding (PTB) domain, inhibits platelet aggregation by competing

156 nase activity, decreases the strength of the PTB domain interaction and the level of RET-dependent Sh

157 d a molecular model of an integrin beta tail-PTB domain interaction to predict critical interacting r

158 with alanines, resulting in the loss of all PTB domain interaction, causes complete loss of beta1 in

159 gand binding to the PH domain does not alter PTB domain interactions, and vice versa.

160 und that the Numb PTB domain but not the Shc PTB domain interacts with Nak through a peptide of 11 am

161 of wild-type or a mutant version lacking the PTB domain into NIH3T3 fibroblasts inhibited PDGF-induce

162 olutionary and functional analysis to divide PTB domains into three groups represented by phosphotyro

163 al that phosphoinositide binding by the Dab1 PTB domain is necessary for proper membrane localization

164 that neither the PDZ-binding domain nor the PTB domain is necessary for the effects of NOS1AP-L.

165 function but strongly suggest that the Numb PTB domain is not involved in phosphotyrosine-dependent

166 lin and interleukin-4 receptors by the IRS-1 PTB domain is predominantly an enthalpy-driven process.

167 The biological function of the PTB domain is to drive recruitment of signaling adapters

168 lation, whereas the phosphotyrosine binding (PTB) domain is critical for the actions of insulin.

169 firmed that these interactions are canonical PTB domain-ligand interactions.

170 ot contain tyrosine, indicating that the JIP PTB domain, like that of Xll alpha and Numb, binds indep

171 A mutant of IRS-1 lacking the PTB domain loses the ability to inhibit the differentiat

172 CM2 isoform proteins contain both classes of PTB domains, making them a dual PTB domain-containing pr

173 In eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by reco

174 n homology (PH) and phosphotyrosine binding (PTB) domains, mediated phosphorylation of PKB/akt, inhib

175 r different reaction groups, such as SH2 and PTB domain-mediated interactions, the EGFR kinase, and t

176 The Sck and Shc SH2 domains, and not the PTB domain, mediates its interactions with KDR, as recom

177 itration calorimetry (ITC), analysis of Dab1 PTB domain mutants, and nuclear magnetic resonance (NMR)

178 wn that the N-terminal region, including the PTB domain (N-PTB), drives Dab2 to the platelet membrane

179 discovered a unique phosphotyrosine binding (PTB) domain, namely atypical phosphotyrosine binding (aP

180 ha bind to integrin beta tails by means of a PTB domain-NPXY ligand interaction.

181 nt of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interaction that may be a protot

182 Furthermore, the PTB domain of Cbl is shown to bind to phosphorylated Tyr

183 es a binding surface that interacts with the PTB domain of CKA1/CKA1S.

184 The inhibitory effect requires the PTB domain of DOKL.

185 Er2 and FE65 that depended on the N-terminal PTB domain of FE65.

186 We have made a novel finding that the PTB domain of IRS-1 binds to the NPXY motif of Grb14 in

187 f the NPXY motif in Grb14 and binding of the PTB domain of IRS-1 in a phosphorylation-independent man

188 lytic domain of the insulin receptor and the PTB domain of IRS-1.

189 amino acids previously shown to contact the PTB domain of IRS1, Leu489 or Ile491, to Ala had only mi

190 Interestingly, although the PTB domain of JIP was reported to interact with rhoGEF,

191 The PTB domain of mIRS3 is necessary and sufficient for bind

192 NBP interacts with the PTB domain of Numb through a region well conserved among

193 Fusion proteins containing the PTB domain of RGS12 alter the rate of termination of the

194 ombinant protein encompassing the N-terminal PTB domain of RGS12 binds to the synprint region in prot

195 r receptor-bound protein 2) and the isolated PTB domain of Shc (SHC adaptor protein) to the EGF recep

196 phosphorylated on Tyr(682), precipitated the PTB domain of Shc A and Shc C, as well as endogenous ful

197 The PTB domain of Shc also interacted with Ret/ptc2 at tyros

198 t both Ptyr SHIP2 and Ptyr SHIP1 bind to the PTB domain of SHC but not to its SH2 domain.

199 ) tyrosines able to interact with the SH2 or PTB domain of Shc does not affect incorporation of alpha

200 We conclude that the PTB domain of Shc is critical for its phosphorylation by

201 3,4,5-P3 and PtdIns-4,5-P2 also bound to the PTB domain of Shc with similar affinities and lipid bind

202 ion of beta(4) Tyr(1526), which binds to the PTB domain of Shc, but not of Tyr(1422) and Tyr(1440), w

203 An inactivating mutation in the PTB domain of Shc, but not one in its SH2 domain, suppre

204 a phosphorylation-dependent manner with the PTB domain of Shc.

205 rmining if expression of the isolated SH2 or PTB domain of ShcC would inhibit EGFR signaling.

206 By expressing the PTB domain of SNT-1 (SNT-1 PTB) in an inducible manner i

207 The N-terminal domain and C-terminal PTB domain of tensin provide essential recruitment signa

208 We have previously shown that the PTB domain of X11alpha (also known as Mint1) can bind to

209 The specific binding of the PTB domain of X11alpha to the YENPTY motif-containing pe

210 specific interactions were observed with the PTB domains of Dab, EPS8, and tensin.

211 tructs containing both the C- and N-terminal PTB domains of FE65 increased secreted APP, secreted Apo

212 The PTB domains of Shc and insulin receptor substrate bind t

213 The PTB domains of Shc and IRS-1 both recognize autophosphor

214 e structures and support the notion that the PTB domains of Shc and IRS-1 employ functionally distinc

215 the tyrosine-phosphorylated NPXY motif, the PTB domains of Shc and IRS-1 prefer a large hydrophobic

216 tinct from the NPXpY motif recognized by the PTB domains of Shc and IRS-1/2.

217 Interaction with both the SH2 and PTB domains of Shc contributes to the transcriptional ac

218 A resolution of the phosphotyrosine-binding (PTB) domain of ARH in complex with an LDLR tail peptide

219 re conserved in the phosphotyrosine-binding (PTB) domain of beta-amyloid precursor protein-binding Mi

220 dependent upon the phosphotyrosine binding (PTB) domain of CCM2.

221 the amino-terminal phosphotyrosine-binding (PTB) domain of Dab1 binds to the transmembrane glycoprot

222 ne such domain, the phosphotyrosine binding (PTB) domain of Disabled-1 (Dab1), which binds to both pe

223 physically with the phosphotyrosine binding (PTB) domain of Numb.

224 ne interaction (PI)/phosphotyrosine binding (PTB) domain of Shc binds specific tyrosine-phosphorylate

225 (PIPKIgamma), by a phosphotyrosine binding (PTB) domain of talin.

226 recognition by the phosphotyrosine-binding (PTB) domain of the protooncogene product, c-Cbl.

227 The phosphotyrosine binding (PTB) domain of X11 binds to a peptide containing a YENPT

228 Phosphotyrosine binding (PTB) domains of the adaptor protein Shc and insulin rece

229 t is related to the phosphotyrosine binding (PTB) domains of the Shc family of adaptor proteins.

230 tes with the phosphotyrosine-binding domain (PTB domain) of Shc and that phosphorylation of tyrosine

231 ID-CID-PTB), or 4) deletion of both termini (PTB domain only, PTB).

232 tion of Shc by over-expression of its SH2 or PTB domains or PI 3-kinase by either treatment with wort

233 Since PTB domains, originally identified in Shc, mediate intra

234 The PTB domain peptide binding site is fully exposed on the

235 ity of these two key peptide residues in the PTB domain/peptide structures and support the notion tha

236 We propose that the PTB domain permits Dab1 to bind specifically to transmem

237 independent mechanism mediated by the PH and PTB domains promoted antiapoptotic and growth actions of

238 Here, we describe a PTB domain protein, FRIP, that is phosphorylated in resp

239 hese findings indicate that Icap1 alpha is a PTB domain protein, which recognizes the NPXY motif of b

240 ing partner, kindlin-2, a widely distributed PTB domain protein.

241 re we show that the phosphotyrosine-binding (PTB) domain protein Ced-6, a well-established phagocytos

242 nition sequence for phosphotyrosine-binding (PTB) domains, protein modules that are present in a wide

243 termine the ability of RTKs to bind specific PTB domain proteins in vivo, and thus modify the signali

244 nding substrate for phosphotyrosine binding (PTB) domain proteins.

245 ted, interacts with phosphotyrosine-binding (PTB) domain proteins.

246 This behavior parallels SH2 and PTB domain recognition of pTyr peptides.

247 rtance of the Tyr(P) and Y-2 residues in Cbl-PTB domain recognition.

248 PTB domains recognize peptide ligands containing beta tu

249 The FRS2 PTB domain recognizes tyrosine-phosphorylated TRKs at an

250 The SNT-1 phosphotyrosine binding (PTB) domain recognizes activated TRKs at a canonical NPX

251 c's phosphotyrosine interacting domains; the PTB domain regulates haptotaxis, while the SH2 domain is

252 independent Dab-like PTBs, with the Dab-like PTB domains representing nearly 75% of proteins encoding

253 cently identified a phosphotyrosine binding (PTB) domain residing within the N-terminal transforming

254 san and vtn contain protein motifs, NPxY and PTB domain, respectively, known to interact.

255 ndent targeting to the membrane preceded the PTB domain's interaction with the tyrosine-phosphorylate

256 phosphopeptide library and show that the Cbl-PTB domain selects a D(N/D)XpY motif, reminiscent of but

257 A mutant Shc with a disrupted PTB domain (Shc S154) did not localize to the membrane i

258 Nonetheless, the Ced-6 PTB domain specifically recognizes the noncanonical Yolk

259 t differences, which shed new light upon the PTB domain specificity.

260 mutation occurs in a location of the TBC1D1 PTB domain that is predicted to have a function in a put

261 As compared to canonical PTB domains that typically recognize the NPXpY turn moti

262 show that the Mint1 phosphotyrosine binding (PTB) domain that binds to APP is intramolecularly inhibi

263 Each contains a phosphotyrosine-binding (PTB) domain that is structurally unrelated to SH2 domain

264 and a novel non-SH2 phosphotyrosine-binding (PTB) domain that specifically recognizes a phosphorylate

265 Unlike other PTB domains, the Dab1 PTB does not bind to tyrosine-phos

266 rminal domains of ICAP-1alpha, unmasking the PTB domain, thereby permitting ICAP-1alpha binding onto

267 ue signaling intermediate that binds the SHC PTB domain through at least one tyrosine phosphorylated

268 oteins that possess phosphotyrosine-binding (PTB) domains, through which they bind specific activated

269 ion shown to abrogate the ability of the Shc PTB domain to bind residues upstream of the phosphotyros

270 ShcA generally uses its PTB domain to engage activated receptor tyrosine kinases

271 n vitro by examining the binding of the Numb PTB domain to proteins from Schneider S2 cells.

272 e found that DOK1 binds directly through its PTB domain to SHIP1.

273 Binding of the purified Shc PTB domain to Tyr 63 containing peptides shows that the

274 Binding of the Shc PTB domain to tyrosine-phosphorylated peptides from TrkA

275 oncogenic Cbl mutant, 70Z Cbl, requires its PTB domain to upregulate NFAT in unstimulated Jurkat T c

276 d the characteristics of binding of the Dab1 PTB domain to various peptide and PI ligands.

277 mined the binding of a series of recombinant PTB domains to a panel of short integrin beta tails.

278 DOKL and p62(dok) bind through their PTB domains to the Abelson tyrosine kinase in a kinase-d

279 ermodynamics of binding of the Shc and IRS-1 PTB domains to tyrosine-phosphorylated NPXY-containing p

280 inding of the talin phosphotyrosine-binding (PTB) domain to integrin beta subunit cytoplasmic domains

281 associates via its phosphotyrosine binding (PTB) domain to the ZAP-70 pY292 negative regulatory phos

282 r- or Tyr-kinases, SH2, SH3, PDZ, 14-3-3 and PTB domains, together with signature motifs for PtdIns(3

283 ulin receptor is unaffected by disruption of PTB-domain-Tyr960 interactions but requires the IRS-1 PH

284 city of six different PH domains and the Shc PTB domain using all five phosphoinositides.

285 MR and mutational analyses, we show that the PTB domain utilizes distinct sets of amino acid residues

286 In vivo, the PTB domain was essential for localization of Shc to the

287 erminal region of IRS-1 including the PH and PTB domains was identified as essential for targeting IR

288 cture-based, targeted mutagenesis of the Shc PTB domain, we first identified the residues within the

289 o unphosphorylated proteins, and the SH2 and PTB domains were the only signaling domains known to rec

290 st to the positive control involving SH2 and PTB domains where phosphorylation is required for bindin

291 YENPTY motif) or X11alpha (F608V within the PTB domain), which diminishes their interaction, thus de

292 ar signaling pathways downstream of the ShcA PTB domain, which both positively and negatively regulat

293 In contrast to SH2 and PTB domains, which serve mainly to mediate protein-prote

294 ARH contains a phosphotyrosine binding (PTB) domain, which in other proteins binds NPXY motifs i

295 omology 2 (SH2) and phosphotyrosine-binding (PTB) domains, which recognize phosphotyrosine-containing

296 the 2.75 A co-crystal structure of the CCM2 PTB domain with a peptide corresponding to KRIT1(NPX(Y/F

297 ese leukemias, Shc is associated through its PTB domain with a tyrosine-phosphorylated protein of 140

298 n capable of direct interactions through its PTB domain with the tyrosine-phosphorylated calcium chan

299 nding to talin resembles the interactions of PTB domains with peptide ligands.

300 re we show that the phosphotyrosine-binding (PTB) domain within the N-terminal transforming region of