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1 in part by the C-terminal activation helix (AF-2).
2 pendent transcriptional activation function (AF-2).
3 ond located in the carboxyl-terminal region (AF-2).
4 and the second in the COOH-terminal region (AF-2).
5 f coactivators for AR activation function 2 (AF-2).
6 f E2-mediated coactivator recruitment to the AF-2.
7 s not suppressed by the physically separated AF-2.
8 this activity requires a functional receptor AF-2.
9 ependent transcriptional activation function AF-2.
10 uterus of mice with mutations in the ERalpha AF-2.
11 strengths with and coactivator effects on AR AF-2.
12 a ligand-dependent transactivation function, AF-2.
13 d both contain activation functions AF-1 and AF-2.
14 activating functional domains (AF), AF-1 and AF-2.
15 Cs (pDC), using mouse lacking either AF-1 or AF-2.
16 ugh two activation functions (AFs): AF-1 and AF-2.
17 through intact AF-1, but not through mutated AF-2.
18 A mutation in the hAR activation function-2 (AF-2) abrogates N-to-C interaction, DNA binding, and tra
21 ly (p160 coactivators) bind to the conserved AF-2 activation function found in the hormone binding do
23 t is still not fully understood how AF-1 and AF-2 activities are regulated cooperatively by ligands.
24 identified as an allosteric modulator of the AF-2 activity and is termed binding function-3 (BF-3).
25 51Y mutation allows weak tamoxifen-dependent AF-2 activity but that this activity is only detectable
27 h IC(50) approximately 50 microM and inhibit AF-2 activity in cells were detected: three nonsteroidal
28 e inhibitory effect of region F on the HNF-4 AF-2 activity is a unique feature among members of the n
29 the N terminus of the receptor protein, and AF-2 activity is dependent on helix 12 of the C-terminal
30 n the N terminus of the receptor protein and AF-2 activity is dependent on helix 12 of the C-terminal
34 e nuclear receptors, and it is essential for AF-2 activity, but it is not necessary for dimerization
35 es the AF-1 activity of ERalpha, but not the AF-2 activity, suggesting that hMMS19 may be an AF-1-spe
38 ligand binding domain of ERalpha C terminus (AF-2) and a ligand-independent activation function in th
40 50 and DRIP205 functionally link GR AF-1 and AF-2, and represent important mediators of GR transcript
41 ix 12 (H12) in the LBD is a component of the AF-2, and the configuration of H12 is ligand-inducible t
42 RAM-1 binding site in rat TRbeta1 outside of AF-2, as TRAM-1 shows weak ligand-dependent interaction
45 and enhanced the activity of the C-terminal AF-2 but not the N-terminal AF-1 transactivation domain
46 lpha (ERalpha) activation functions AF-1 and AF-2 classically mediate gene transcription in response
48 in ER transactivation is dependent on the ER AF-2 coactivator binding site, prompting us to examine r
50 nal (AF-1-containing) and carboxyl-terminal (AF-2-containing) regions of ER as separate polypeptides
52 ranscriptional activation functions AF-1 and AF-2, controls the transcription of target genes presuma
53 wo FXR transactivation-deficient mutants (an AF-2 deletion and a W469A point mutant) failed to transa
54 to the promoter complex; the second step is AF-2 dependent and entails entry of preinitiation comple
55 nvolves primary HNF-4 activation function 2 (AF-2)-dependent interactions with the TRAP220 subunit of
58 h NBD-1 and NBD-2 showed similar ligand- and AF-2-dependent interactions with TR in solution, these t
59 suggesting that the AF-1 is regulated in an AF-2-dependent manner in the male reproductive tract.
62 and ERalpha in the activation helix and the AF-2 dimerization helix indicates that TERP-1 acts predo
63 indings we hypothesized that the mutation of AF-2 disrupted its ability to suppress AF-1, causing the
66 o-terminal FXXLF motif and carboxyl-terminal AF-2 domain (N/C interaction) prevented toxicity and AR
69 idues 405-419 on delta419 with the conserved AF-2 domain from the vitamin D3 receptor or the estrogen
70 ndings suggest that an important role of the AF-2 domain in the native ER is to mask the activation p
71 demonstrate that p120 interacts with the TR AF-2 domain in the presence of ligand through a 111-amin
72 nesis studies demonstrated that a functional AF-2 domain is essential for toxicity, a finding corrobo
74 DR translocation, demonstrate that an intact AF-2 domain is required for this translocation, and indi
76 A1, and this interaction was mediated by the AF-2 domain of ER-alpha and two domains of BRCA1, the am
80 PPARalpha, indicating that the COOH-terminal AF-2 domain of PPAR is not the target of STAT5b inhibiti
81 activator-1 (PGC-1) requires both the intact AF-2 domain of PPARgamma and the LXXLL domain of PGC-1 f
83 lls that harbor a truncated ligand-dependent AF-2 domain of RARalpha do not demonstrate any changes i
85 heterodimer binds directly to DNA, with the AF-2 domain of tethered CAR mediating transcriptional ac
87 n potential of PGC-1alpha requires an intact AF-2 domain of VDR and the LXXLL motif in PGC-1alpha.
88 eins are coactivators that interact with the AF-2 domain of VDR to augment 1,25-dihydroxyvitamin D3-d
89 t chromatin remodeling, but mutations in the AF-2 domain that abolish activity in the native ER also
90 that helix H3 functions in concert with the AF-2 domain to form a transactivation surface for bindin
92 RAR in response to ligand displaces the RXR AF-2 domain, allowing RXR ligands to bind and promote th
98 re, we found that the activation function-2 (AF-2) domain of the retinoid X receptor interferes with
99 nteraction between the activator function-2 (AF-2) domain of the VDR and C terminus of beta-catenin.
100 terized C-terminal AR activation function-2 (AF-2) domain was critical for strong, ligand-dependent a
101 inding domain, the human ER hormone binding (AF-2) domain, and the VP16 activation domain, functions
103 e results demonstrate directly that AF-1 and AF-2 domains accomplish their transactivation activities
104 two signal input domains (one that binds NR AF-2 domains and one that binds AF-1 domains of some but
105 OPR1 and its longer variant COPR2 target the AF-2 domains of NR but exhibit quantitative differences
107 mice and mice with mutations in the ERalpha AF-2 (ERalphaAF-2(0)) were treated with ICI, estradiol,
108 A ligand-inducible transactivation function (AF-2) exists in the extreme carboxyl terminus of the vit
110 ; COPR2, 32.4 kDa), and strict dependence on AF-2 for interaction distinguish COPR1 and COPR2 from th
111 evaluate the physiological role of AF-1 and AF-2 for the tissue-selective function of TAM, we genera
113 ndent interactions between the ERalpha D351Y AF-2 function and GRIP1, a representative p160, can be d
114 essing L543A,L544A mutations in H12 disrupts AF-2 function and reverses antagonists such as fulvestra
115 se they were completely dependent on the RXR AF-2 function but independent of both the RXR A/B domain
117 iated activation by BPA and BPAF was via the AF-2 function of ERalpha, but Zea activated via both the
122 a small compound-binding surface adjacent to AF-2 has been identified as an allosteric modulator of t
127 nding cavity were mapped to helix H3 and the AF-2 helix H12, indicating conformational changes in the
129 Activation of PPARgamma by AJA requires the AF-2 helix of the receptor, suggesting that AJA activate
131 e most striking of which is a packing of the AF-2 helix onto the LBD adjacent to helices H3 and H4.
134 phenylalanine 435 and a displacement of the AF-2 helix relative to the unliganded structures with li
136 on of RXR results from a rotation of the RXR AF-2 helix that places it in contact with the RAR coacti
137 from the C2 symmetry, allowing the PPARgamma AF-2 helix to interact with helices 7 and 10 of RXRalpha
138 g domain (LBD) of hPXR, interacting with the AF-2 helix to stabilize the LBD for coactivator binding.
140 the cofactor binding site is occupied by the AF-2 helix, thus preventing ligand-independent activatio
147 MFA-1 binds with its D ring-facing helix 12 (AF-2) in a manner reminiscent of hormone binding to clas
148 dependent transcriptional activation domain (AF-2) in the C-terminal region of the human vitamin D re
149 vitro, the F domain was found to obscure an AF-2-independent binding site for GRIP1 that did not map
150 titutive, ligand-independent AR activity was AF-2-independent but instead dependent on N-terminal AR
156 e-dependent activation domain (named tauc or AF-2) inhibits the ability of RXR-PPARgamma heterodimers
157 two activating functions of HNF-4, AF-1 and AF-2, interact with the N terminus and the N and C termi
158 was selectively impaired in interaction with AF-2-interacting coactivator proteins such as SRC-1 and
160 oborated by a genetic screen that identified AF-2 interactors as dominant modifiers of degeneration.
163 1 is localized in the N-terminal region, and AF-2 is distributed in the C-terminal ligand-binding dom
164 kably, the full transactivation potential of AF-2 is inhibited by the region spanning residues 371-46
166 ntexts, the synergistic activity of AF-1 and AF-2 is required for full estradiol (E2)-stimulated acti
167 s a predominant ligand response, whereas RXR AF-2 is required for liganded RAR AF-2 to efficiently tr
168 ligand-independent AF-1 and ligand-dependent AF-2, located in the A/B and E domains, respectively.
170 activation, a conformational change releases AF-2-mediated repression and transcriptional activation
172 response requires the DNA binding domain and AF-2 motif of CAR3 and is markedly enhanced by retinoid
173 strong ligand-dependent interaction with an AF-2 mutant of TR (E457A), while SRC-1 fails to interact
177 ent for 3 wk beginning at age 21 d activated AF-2-mutated ERalpha (AF2ER) and restored expression of
178 e-selective function of TAM, we generated an AF-2-mutated ERalpha knock-in (AF2ERKI) mouse model.
181 These results indicate that the ERalpha AF-2 mutation results in male infertility, suggesting th
183 n domains, ID1 and ID2, whereas the putative AF-2 of ARP1 was required for interaction with CTIP1.
185 t mouse lacking the transactivation function AF-2 of ERalpha (ERalpha-AF2(0)) provided selective loss
186 ng coactivator protein(s) interacts with the AF-2 of PR or TR and mediates transactivation by the lig
188 nd estrogen-dependent activation function 2 (AF-2) of ERalpha, AKT increased the activity of only AF-
189 vents the carboxy-terminal activation helix (AF-2) of the receptor from assuming the active conformat
191 functions (activation function 1 [AF-1] and AF-2) or receptor dimerization fail to fully inhibit cel
193 rated that the activation function 2 domain (AF-2) plays an essential role in VDR transactivation.
195 is conclusion, we have identified an ERalpha AF-2 point mutant (L540Q) that selectively binds and rec
199 nteraction also requires the presence of the AF-2 region of RXR to interact with the LXXLL motif of P
206 ion activities through different mechanisms: AF-2 requires GRIP1 as a coactivator, but AF-1 does not.
207 -terminal transcriptional activation domain, AF-2, retained elevated basal activity, while mutation o
208 c binding pocket on the outer surface at the AF-2 site and fitted comfortably, making interactions wi
211 id expressing rat CAR lacking the C-terminal AF-2 subdomain inhibited squalestatin 1-inducible CYP2B1
213 by ERbeta, probably by interacting with the AF-2 surface and blocking the binding of endogenous coac
214 e that E(2)-mediated repression requires the AF-2 surface and the participation of coactivators or ot
218 vered a role for coactivators binding to the AF-2 surface of the vitamin D receptor (VDR) in its nega
220 othesized to bind the activation function-2 (AF-2) surface on the exterior of PXR when agonists are c
222 tains a transcriptional activation function (AF-2) that mediates hormone-dependent binding of coactiv
223 elical region, termed activation function-2 (AF-2), that forms part of the ligand-binding pocket and
224 ds at the AR surface reveals weak binding at AF-2, the most potent inhibitors bind preferentially to
226 nRXR alpha) lacking transactivation function AF-2 to differentiated suprabasal keratinocytes in the e
227 hereas RXR AF-2 is required for liganded RAR AF-2 to efficiently trans-activate target genes, and (2)
229 -binding domain linked to the ligand binding/AF-2 trans-activation domain of PPARalpha, indicating th
230 ostructure, but an important pocket near the AF-2 transactivation domain becomes accessible only in s
231 SHP proteins specifically interact with the AF-2 transactivation domain of LRH-1 both in vivo and in
232 ocusing on the C-terminal ligand-binding and AF-2 transactivation domains, an assembly of an active t
238 FP) chimeras with full-length VDR (VDR-GFP), AF-2-truncated VDR (AF-2del-VDR-GFP), and ligand-binding
240 ) of RARgamma but not the C-terminal domain (AF-2) was required for association with beta-catenin, wh
241 n transcriptional synergism between AF-1 and AF-2, we expressed the amino terminal (AF-1-containing)
242 ion with beta-catenin, whereas both AF-1 and AF-2 were necessary for inhibition of beta-catenin trans
243 at the N terminus (AF-1) and the C terminus (AF-2) which work synergistically to confer full HNF-4 ac
244 transcription activation functions AF-1 and AF-2, which act in a promoter- and cell-specific manner.
245 transactivation domains, designated AF-1 and AF-2, which activate transcription in a cell type-indepe
247 l activation domains, tau1 (AF-1), tau2, and AF-2, which were initially defined using transiently tra
248 istinct activation functions (AFs), AF-1 and AF-2, whose respective involvement varies in a cell type
250 oxy-terminal transactivation function termed AF-2 within the last 15 amino acids of the ligand bindin
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