ライフサイエンスコーパス: SAP97

1 d to GluR1 by synapse-associated protein 97 (SAP97).

2 almitoylation site (PSD95) or an L27 domain (SAP97).

3 +) interneurons show low or no expression of SAP97.

4 owed that Kir2.1 and Kir2.2 co-localize with SAP97.

5 nstrated that Kir2.x channels associate with SAP97.

6 family includes PSD-95, PSD-93, SAP102, and SAP97.

7 othelial cell (EC)-specific knockout of Dlg1/SAP97.

8 d the postsynaptic adaptor proteins CASK and SAP97.

9 iculum subcompartment requires both CASK and SAP97.

10 m HEK293 cells co-expressing CaMKIIalpha and SAP97.

11 he presynaptic growth caused by postsynaptic SAP97.

12 -associated guanylate kinase (MAGUK) protein SAP97.

13 D-aspartate receptor with the PDZ domains of SAP97.

14 main mutants that inhibit multimerization of SAP97.

15 tional "L27" motif, which is also present in SAP97.

16 ggered by NMDAR activation, does not require SAP97.

17 with synaptic scaffolding proteins, such as SAP97.

18 at contrasts with the axonal distribution of SAP97.

19 l domain organization with, PSD-95/SAP90 and SAP97.

20 R and its binding to the PDZ-binding protein SAP97.

21 AR was internalized alone or in complex with SAP97.

22 embrane properties from those not expressing SAP97.

23 ly conserved homolog of mammalian PSD-95 and SAP97.

24 Synapse-associated protein 97 (SAP97), a member of the membrane-associated guanylate ki

25 R1 subunit by synapse-associated protein 97 (SAP97), a membrane-associated guanylate kinase family pr

26 Discs large homolog 1 (DLG1; SAP97), a PDZ protein prominent in both astrocytes and M

27 iological effects of native (WT) and p.P888L SAP97, a common polymorphism.

28 complex also requires the PDZ domain protein SAP97, a member of the MAGUKs family, which binds to Sec

29 omain of Veli-2, and the third PDZ domain of SAP97, a PSD95-related protein.

30 this L27N domain binds to the N terminus of SAP97, a region that was previously reported to be essen

31 We now show that SAP97, a SAP whose function at the synapse has been uncl

32 GluR1 binds to SAP97, a scaffolding protein that is a component of the

33 ivation of PKA stimulates the formation of a SAP97-AKAP/PKA-GluA1 protein complex leading to synaptic

34 Thus, the PDZ and its associated SAP97-AKAP79 complex are involved in targeting the cycli

35 orylation of AMPA receptors is enhanced by a SAP97-AKAP79 complex that directs PKA to GluR1 via a PDZ

36 dens 1)-domain interaction between GluR1 and SAP97, all of which support basal phosphorylation of the

37 Whether SAP97 also plays a role in scaffolding GluR1 at the post

38 nteracts with synapse-associated protein 97 (SAP97; also known as DLG1) by co-immunoprecipitation in

39 nteracts with synapse-associated protein 97 (SAP97; also known as DLG1) by coimmunoprecipitation in h

40 SAP97 and 4.1N are proteins involved in GluA1 traffickin

41 We next examined potential roles of SAP97 and 4.1N in cocaine seeking.

42 Therefore, SAP97 and 4.1N may play a role in the transport and inse

43 SAP97 and 4.1N were developmentally regulated in the sam

44 preferentially phosphorylated a full-length SAP97 and a glutathione S-transferase (GST) fusion prote

45 measurements revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on th

46 interaction domains that link mLin-2/CASK to SAP97 and account for their common phenotype when mutate

47 ntain accumulations of the scaffold proteins SAP97 and AKAP79/150 but are deficient in caveolin-3.

48 phosphorylated and exists in a complex with SAP97 and CaM.

49 they all showed reduced binding affinity for SAP97 and CaM.

50 as regulated by a direct interaction between SAP97 and CASK through L27 protein-interaction domains o

51 asolateral membrane and co-localization with SAP97 and CASK, whereas a dominant interfering form of C

52 e C terminus of NR2B with the PDZ domains of SAP97 and determine the structure of the PDZ1-NR2B compl

53 ins identified the third PDZ domains of DLG1/SAP97 and DLG4/PSD95 as interaction partners for the PDZ

54 ell RT-PCR to assay endogenous expression of SAP97 and exogenous expression of SAP97, we investigated

55 rated a direct interaction between EBP50 and SAP97 and ezrin.

56 We find that interactions involving SAP97 and GluR1 occur early in the secretory pathway, wh

57 om mice trans-expressing human WT or p.P888L SAP97 and in Chinese hamster ovary (CHO)-transfected cel

58 ation is available on interactions involving SAP97 and inward rectifier potassium (Kir2.x) channels t

59 o-IP data show that beta1-AR associates with SAP97 and Kir2.1 and also that Kir2.1 co-IPs with protei

60 by Kv1.5 channels increased similarly in WT-SAP97 and p.P888L-SAP97 cardiomyocytes, while the inward

61 through the C-terminal type I PDZ motif with SAP97 and protein kinase A (PKA)-anchoring protein (AKAP

62 rane-associated guanylate kinases, including SAP97 and PSD-95, and protein kinase A-anchoring protein

63 GFP)-tagged chimeras and deletion mutants of SAP97 and SAP90 were employed to define the molecular me

64 This interaction requires the MRE domain of SAP97 and surprisingly, both the L27N and L27 carboxyl-t

65 tein partners synapse-associated protein 97 (SAP97) and calmodulin (CaM).

66 synapse contained GluR2/3 but lacked GluR1, SAP97, and 4.1N at the time of PF synaptogenesis.

67 ction between the MAGUK proteins, PSD-95 and SAP97, and AKAP79/150.

68 and Mint1, and Veli-3 associates with CASK, SAP97, and Mint1.

69 lated MAGUKs SAP90/PSD95, PSD93/chapsyn-110, SAP97, and SAP102 all bound to the COOH-terminal tail of

70 K) homologs PSD-95/SAP90, PSD-93/chapsyn110, SAP97, and SAP102 are central organizers of the postsyna

71 -tails of aquaporin-2 or GluR1 recycled in a SAP97- and PKA-dependent manner.

72 ed rapid recycling of chimeric beta1-AR in a SAP97- and PKA-independent manner.

73 by the fact that mutations in mLin-2/CASK or SAP97, another MAGUK protein, lead to cleft palate in mi

74 Overexpression of SAP97 antagonized agonist-stimulated CRFR1 internalizati

75 ve glutamatergic synapse scaffolding protein SAP97 are associated with the development of schizophren

76 PSD-95 and SAP97 are scaffolding proteins that have been implicated

77 5 (PSD95) and synapse-associated protein 97 (SAP97) are homologous scaffold proteins with different N

78 (PSD-95) and synapse-associated protein 97 (SAP97) are poorly understood.

79 s, adenomatous polyposis coli (APC) and Dlg1-SAP97, are required for the polarization of migrating as

80 GUKs), including SAP102, PSD-95, PSD-93, and SAP97, are scaffolding proteins for ionotropic glutamate

81 In contrast, in its extended conformation, SAP97 associates with NMDARs, but not with AMPARs.

82 with the Kir2 channels and recruits CASK and SAP97; association of Mint1 with the complex requires Ve

83 of binding partners and the localization of SAP97 at adhesion sites, as well as the clustering of io

84 ts with PDZ proteins such as syntrophins and SAP97 at different locations within the cardiomyocyte, t

85 contrast, these interneuron subtypes express SAP97 at P15, but for adult visual cortex we found that

86 i and synaptic-associated protein of 97 kDa (SAP97) at the basolateral surface of RPE cells, which ov

87 esults suggest that the TC10/exocyst complex/SAP97 axis plays an important role in the tethering of G

88 synapse-associated protein 102 (SAP102), and SAP97 based on coimmunoprecipitation of detergent-solubi

89 Synapse-associated protein 97 (SAP97) belongs to a family of proteins that have been im

90 dogenous forms of PSD-95 (alpha-isoform) and SAP97 (beta-isoform) govern their role in regulating syn

91 As such, SAP97 binding caused an intracellular accumulation of ea

92 ects of short sequences differing in PDZ and SAP97 binding were examined using chimeric mutant beta1-

93 by mutations in the PDZ that interfered with SAP97 binding.

94 Here we show that SAP97 binds two other mLIN-7 binding MAGUK proteins.

95 ated by an amino-terminal domain shared with SAP97 but not found in other MAGUK family members.

96 the inward rectifier current increased in WT-SAP97 but not in p.P888L-SAP97 cardiomyocytes.

97 An additional domain we identified in SAP97 called the MAGUK recruitment (MRE) domain binds th

98 raction between GluR6 and the PDZ1 domain of SAP97 can account for the weak association of GluR6 with

99 These results suggest that SAP97 can affect the synaptic recruitment of AMPA recept

100 results indicate that N-terminal splicing of SAP97 can control synaptic strength by regulating the di

101 These models revealed that SAP97 can exist in a compact U-shaped conformation in wh

102 c homology 3 and guanylate kinase domains in SAP97 can interact with the C-terminal tail of KA2 subun

103 We also demonstrate that SAP97 can interact with the MAGUK protein, DLG2, but not

104 increased similarly in WT-SAP97 and p.P888L-SAP97 cardiomyocytes, while the inward rectifier current

105 ent increased in WT-SAP97 but not in p.P888L-SAP97 cardiomyocytes.

106 he dystrophin-associated protein complex and SAP97, CASK, and Veli.

107 m revealed overlapping expression of Kir2.2, SAP97, CASK, Mint1, with Veli-1 in the granule cell laye

108 , we demonstrated that a complex composed of SAP97, CASK, Veli, and Mint1 associates with Kir2 channe

109 From heart extract purifications, SAP97, CASK, Veli-3, and Mint1 also were found to associ

110 odel whereby Kir2.2 associates with distinct SAP97-CASK-Veli-Mint1 complexes.

111 Kv1 channel tested, through the accretion of SAP97 channel clusters in large (3-5 microm) ER-derived

112 recipitate with both KA2 and GluR6, but only SAP97 coimmunoprecipitates with GluR6.

113 ages revealed increasing levels of EBP50 and SAP97 compared with alphav integrin, a protein expressed

114 icantly alter how PV interneurons expressing SAP97 compared with those not expressing SAP97 would fun

115 ar mechanism by which CASK binding regulates SAP97 conformation and its subsequent sorting and synapt

116 Here, we measured PSD95 and SAP97 conformation in vitro and in postsynaptic densitie

117 SAP97 conformation was regulated by a direct interaction

118 We find that both PSD-95 and SAP97 contain alternative N termini expressing either do

119 Schizophrenia-related perturbations of SAP97 did not affect CA1 pyramidal neuron synapse functi

120 Overexpression or shRNA knockdown of SAP97 did not significantly affect CRFR1-mediated cAMP f

121 The synapse-associated protein SAP97 directly binds GluR1 and participates in its forwa

122 hat two postsynaptic, N-terminal isoforms of SAP97 directly modulate the levels, dynamics, and functi

123 eptors associate with SAP97, suggesting that SAP97 dissociates from the receptor complex at the plasm

124 Here we addressed how SAP97 distinguishes between AMPARs and NMDARs and what r

125 with the PDZ domain-containing protein hDlg/SAP97 (DLG), which is a mammalian homolog of the Drosoph

126 n the binding of the PDZs of both MAGI-I and SAP97/Dlg, the mutation of which abolishes E6's ability

127 6 bound to three PDZ domains from MAGI-1 and SAP97/Dlg.

128 Overexpression of SAP97 drove GluR1 to synapses, potentiated AMPA receptor

129 We found that overexpression of SAP97 during early development traffics AMPARs and NMDA

130 nit, specific intramolecular interactions in SAP97 (e.g. the SAP97 N terminus (S97N) binding to the S

131 PV interneurons expressing SAP97, either endogenously or via exogenous expression,

132 thesis by assessing whether the GK domain in SAP97 encodes an authentic guanylate kinase.

133 In addition, postsynaptic expression of SAP97 enhanced presynaptic function, as measured by incr

134 Synapse-associated protein 97 (SAP97) exhibits protein interactions, such as direct int

135 Four alternative mRNA splice variants of SAP97 expressing combinations of four inserts (I2, I3, I

136 Additionally, SAP97-expressing PV interneurons fired action potentials

137 Furthermore, SAP97-expressing PV interneurons showed increased glutam

138 otropin-releasing factor receptor 1 (CRFR1), SAP97 expression is essential for 5-HT2AR-stimulated ext

139 quences that precede the first PDZ domain in SAP97, facilitated GKAP binding via its association with

140 a2-adrenergic receptor that does not bind to SAP97 failed to recycle except when serine 312 was mutat

141 embers of the synapse-associated protein-97 (SAP97) family of scaffold proteins have been implicated

142 from rat brain, we found that myosin VI and SAP97 form a trimeric complex with the alpha-amino-3-hyd

143 These data suggest that SAP97 forms the molecular backbone of a protein scaffold

144 Using intramolecular SAP97 Forster resonance energy transfer sensors, we demo

145 a13 and PSD95 from brain and of Ggamma13 and SAP97 from taste tissue indicates that Ggamma13 interact

146 expression but does prevent translocation of SAP97 from the cytosol to membranes.

147 2AR expression results in the recruitment of SAP97 from the cytosol to the plasma membrane and that t

148 Furthermore, inhibiting SAP97 function in the dentate gyrus was sufficient to im

149 uced phosphorylation of the scaffold protein SAP97, further establishing that this is a physiological

150 ss-of-function experiments using conditional SAP97 gene deletion, we recorded no deficits in glutamat

151 ture spines and postsynaptic proteins PSD95, SAP97, GluA1, AMPAR-mediated basal synaptic transmission

152 levels of Dlg1, Gria1, and Gria2 (coding for SAP97, GluA1, and GluA2 respectively) were not affected

153 rafficking to and stabilization in synapses; SAP97-GluA1 interactions also influence dendritic growth

154 idues affected by the binding of CaM and the SAP97 GUK domain were determined as well as the dissocia

155 Thus SAP97 has a broader role than its close relative, PSD-95

156 SAP97 has been shown to associate and modulate voltage-g

157 In this regard, SAP97 has been suggested to regulate the synaptic locali

158 ture EPSC (mEPSC) frequency, indicating that SAP97 has both postsynaptic and presynaptic effects on s

159 -associated guanylate kinase (MAGUK) protein SAP97/hDlg as a binding partner in a yeast two-hybrid sc

160 certain tumor suppressors such as MAGI-1 and SAP97/hDlg for degradation.

161 SAP97/hDlg is a scaffold protein that forms multiprotein

162 SAPK3/p38gamma-catalysed phosphorylation of SAP97/hDlg triggers its dissociation from GKAP and there

163 Here we identify SAP97/hDlg, the mammalian homologue of the Drosophila tu

164 ted specifically the expression of DlgS97, a SAP97 homolog, and one of two major protein isoforms enc

165 AR currents was ablated by overexpression of SAP97-I2I5 (which does not bind AKAP79) or by infusion o

166 on protein containing the I3 and I5 inserts (SAP97-I3I5 and GST-SH3-I3I5-GK, respectively) and also s

167 SAP97 immunolocalizes with protein kinase A and beta1-AR

168 xists in a complex with the AMPAR, AP-2, and SAP97 in brain.

169 tial for the lateral membrane recruitment of SAP97 in epithelia.

170 ngle hairpin (shRNA) knockdown of endogenous SAP97 in HEK 293 cells resulted in increased agonist-sti

171 The knockdown of SAP97 in HEK 293 cells results in a reduction in the max

172 UK proteins, DLG3, coimmunoprecipitates with SAP97 in lysates from rat brain and transfected Madin-Da

173 /CASK is crucial for lateral localization of SAP97 in MDCK cells.

174 investigated the functional significance of SAP97 in PV interneurons in layers 2/3 of the visual cor

175 Given the importance of SAP97 in regulating AMPA receptor GluA1 subunit and NMDA

176 However, the role of SAP97 in synaptic regulation is unclear.

177 ve presence and colocalization of PMCA4b and SAP97 in the basolateral membrane of polarized Madin-Dar

178 In HEK cells and rat hippocampal neurons, SAP97 in the compact conformation preferentially associa

179 identify the differential roles of 4.1N and SAP97 in the control of various phases of GluA1 IT.

180 Endogenous SAP97, in contrast, has no effect on receptor clusters b

181 expression of synapse-associated protein 97 (SAP97) increased presynaptic protein content and active

182 Synaptic targeting of SAP97, increased surface AMPA receptors, and increased m

183 Whereas alpha-isoforms of PSD-95 and SAP97 influence AMPA receptor-mediated synaptic strength

184 These results implicate GluR1-SAP97 interactions in mechanisms underlying AMPA recepto

185 Taken together, our studies show that SAP97 interactions with CRFR1 attenuate CRFR1 endocytosi

186 In one complex, SAP97 interacts directly with the Kir2 channels and recr

187 SAP97 interacts with AMPA receptors (AMPARs) and NMDA re

188 nding motif results in the redistribution of SAP97 into the cytoplasm.

189 and zonula occludens-1 (PDZ) domain protein SAP97 is a component of this macromolecular complex.

190 esults indicate that the scaffolding protein SAP97 is a critical molecular factor regulating the inpu

191 SAP97 is a membrane cytoskeletal protein localized at th

192 SAP97 is a modular protein composed of three PDZ domains

193 er PSD-MAGUKs can presumably compensate when SAP97 is conditionally deleted during development.

194 ns in mouse visual cortex, the expression of SAP97 is developmentally regulated, being expressed in a

195 heir exocytosis whereas the interaction with SAP97 is essential for GluA1 IT.

196 Here we show that SAP97 is expressed in the dendrites of granule neurons i

197 nergy transfer sensors, we demonstrated that SAP97 is in "extended" or "compact" conformations in viv

198 h CRFR1 attenuate CRFR1 endocytosis and that SAP97 is involved in coupling G protein-coupled receptor

199 otein-protein docking predicted that p.P888L SAP97 is more likely to form a complex with CaMKII than

200 Thus, it would appear that the GK domain of SAP97 is not involved in the metabolism of guanine nucle

201 Moreover, we find that SAP97 is not responsible for CRFR1-mediated sensitizatio

202 ghtly binds kainate receptor subunits, while SAP97 is only weakly associated, suggesting that this gl

203 These results support the hypothesis that SAP97 is part of the machinery that traffics glutamate r

204 Here we show that SAP97 is present in CaMKII immune complexes isolated fro

205 Similarly, we demonstrated that SAP97 is recruited to the plasma membrane in HEK 293 cel

206 Synapse-associated protein-97 (SAP97) is a membrane-associated guanylate kinase scaffol

207 Synapse-Associated Protein 97 (SAP97) is an anchoring protein that in cardiomyocytes ta

208 The synapse-associated protein-97 (SAP97) is important in the proper trafficking and cell s

209 ly affect CRFR1-mediated cAMP formation, but SAP97 knockdown did significantly attenuate CRFR1-stimul

210 llowed shortly thereafter by generation of a SAP97-KSR1/PKC-GluA4 complex for GluA4 AMPAR subunit del

211 and forms, through CaMKII-actinin-actin-(4.1/SAP97) linkages, additional sites for anchoring AMPARs a

212 localizes at the apical microvilli, whereas SAP97 localizes at the basolateral surface of RPE cells,

213 ical consequences on the myocardium and that SAP97 may affect the integrity of this complex or the na

214 Our findings suggest that SAP97 may be involved in localizing AMPA receptors at po

215 These results suggest that SAP97 may play a central role in the coordinated growth

216 ate that the GluA1 subunit accessory protein SAP97 may represent a novel target for pharmacotherapeut

217 These data suggest that SAP97 may serve as a molecular link between GluR1 and th

218 ficantly shorter in p.P888L-SAP97 than in WT-SAP97 mice.

219 calculated to be 300, whereas the number of SAP97 molecules, contributing 0.9% of the mass of the PS

220 correlated with faster turnover of monomeric SAP97 mutants in dendritic spines.

221 tramolecular interactions in SAP97 (e.g. the SAP97 N terminus (S97N) binding to the Src homology 3 do

222 hich contains a region highly related to the SAP97 N terminus and which binds Camguk, a Drosophila or

223 We find that recombinant SAP97 not only becomes concentrated at synaptic junction

224 ak association of GluR6 with the full-length SAP97 observed in vivo.

225 ow that ion channel clustering by PSD-95 and SAP97 occurs by distinct mechanisms, and suggests that t

226 estigate the functional effects of silencing SAP97 on I(K1) in adult rat ventricular myocytes, SAP97

227 ons with heterologous expression of specific SAP97 or PSD-95 isoforms.

228 SAP97 oriented parallel to the PSD membrane, likely as a

229 othesis directly, we assessed the effects of SAP97 overexpression on surface expression of synaptic A

230 Taken together, our studies show that SAP97 plays a conserved role in regulating 5-HT2AR endoc

231 It has therefore been hypothesized that SAP97 plays an essential role in cellular signaling by r

232 We propose that DlgS97/SAP97 plays an important and conserved role in the devel

233 The p.P888L SAP97 polymorphism increases the I(to,f), a CaMKII-depen

234 diated expression of a microRNA that reduces SAP97 protein expression (HSV miSAP97) in the medial acc

235 ght members of the MAGUK family of proteins (SAP97, PSD-95, Chapsyn-110, SAP102, CASK, Dlg2, Dlg3, an

236 elivery of GluA1-containing AMPARs through a SAP97-PSD95 interaction.

237 GluA4 AMPAR subunit delivery again through a SAP97-PSD95 interaction.

238 Expression of SAP97 recruited a complex of additional postsynaptic pro

239 tage clamp experiments showed that silencing SAP97 reduced I(K1) whole cell density by approximately

240 In contrast, RNAi knockdown of endogenous SAP97 reduced surface expression of both GluR1 and GluR2

241 We identified the GUK domain as the minimal SAP97 region necessary for the Cx32CT interaction.

242 Our results suggest that in cardiac myocytes SAP97 regulates surface expression of channels underlyin

243 ructural presynaptic effects of postsynaptic SAP97 required ligand binding through two of its PDZ (PS

244 MDA receptors (NMDARs) to synapses, and that SAP97 rescues the deficits in AMPAR currents normally se

245 CRFR1 was internalized as a complex with SAP97 resulting in the redistribution of SAP97 to endocy

246 e energy transfer and that overexpression of SAP97 retards 5-HT2AR endocytosis, while single hairpin

247 The N terminus of SAP97 (S97N) has been shown to play a key role in the se

248 r proteins of the Dlg family, including Dlg1/SAP97, SAP102, and PSD95.

249 Recently, the DLG1/SAP97 scaffolding protein was described to interact with

250 The C-terminal GK domain of SAP97 shares a high degree of sequence similarity with l

251 Compared to WT, p.P888L SAP97 significantly increased the charge of the Ca-indep

252 was -1.45 +/- 0.15 pA/picofarads (n = 6) in SAP97-silenced cells as compared with -3.03 +/- 0.37 pA/

253 Furthermore, SAP97 silencing impaired I(K1) regulation by beta(1)-adr

254 ly 75%, an effect that was blunted following SAP97 silencing.

255 tance properties of I(K1) were unaffected by SAP97 silencing.

256 ents with recombinant proteins indicate that SAP97 specifically associates with the C terminus of Glu

257 suggest that CaMKIIalpha targets a specific SAP97 splice variant to disengage AKAP79/150 from regula

258 of the MAGUK synapse-associated protein 97 (SAP97), suggesting that AKAP79 functions to organize eve

259 trast, few synaptic receptors associate with SAP97, suggesting that SAP97 dissociates from the recept

260 ession of GluR1 and its scaffolding proteins SAP97 (synapse-associated protein) and 4.1N during cereb

261 nfer distinct subsynaptic localizations onto SAP97, targeting the palmitoylated alpha-isoform to the

262 terval were significantly shorter in p.P888L-SAP97 than in WT-SAP97 mice.

263 specific alternatively spliced sequences in SAP97 that encode a protein 4.1 binding site.

264 oordinated by synapse-associated protein 97 (SAP97) that contain A-kinase anchoring protein 79/150 (A

265 Lastly, mice in which SAP97, the mammalian homolog of DlgS97, was conditionall

266 e investigated the interaction of GluR1 with SAP97, the only PDZ protein known to interact with GluR1

267 to the lethality of the germline knockout of SAP97, this protein's role in synaptic transmission and

268 that have experienced the overexpression of SAP97 throughout development exhibit enhanced AMPAR and

269 ith SAP97 resulting in the redistribution of SAP97 to endocytic vesicles.

270 The ability of SAP97 to interact with multiple MAGUK proteins is likely

271 nal 7 aa of GluR1 are essential for bringing SAP97 to the plasma membrane, where it acts to translate

272 GluR1 and SAP97 together at the plasma membrane promotes dendrite

273 We also show that 5-HT2AR interacts with SAP97 using bioluminescence energy transfer and that ove

274 ing in vitro protein interaction assays that SAP97, Veli-1, or Veli-3 binds directly to the Kir2.2 C

275 where Veli-1 stably associates with CASK and SAP97, Veli-2 associates with CASK and Mint1, and Veli-3

276 geting of GluR1 through the scaffold protein SAP97 via a mechanism dependent on CaMKII stimulation.

277 d solubilization with sodium dodecylsulfate, SAP97 was associated with GluR1 but not GluR2 or GluR3.

278 ntrast, the interaction of Kv1 channels with SAP97 was independent of Kv1 surface expression, occurre

279 Unbound SAP97 was mostly in the compact conformation, while CASK

280 SAP97 was present in AMPA receptor complexes immunopreci

281 Western blot analysis showed that SAP97 was silenced by approximately 85% on day 3 post-in

282 on I(K1) in adult rat ventricular myocytes, SAP97 was silenced using an adenoviral short hairpin RNA

283 tion with the synapse-associated protein-97 (SAP97) was necessary for LTD-induced ADAM10 trafficking

284 ression of SAP97 and exogenous expression of SAP97, we investigated the functional significance of SA

285 DZ, SH3 and GUK domains, molecular models of SAP97 were generated.

286 Veli-2 and SAP97 were identified in taste tissue and in Ggamma13-ex

287 Within PSDs, PSD95 and SAP97 were largely in the extended conformation, but had

288 rge, a Drosophila melanogaster orthologue of SAP97, which contains a region highly related to the SAP

289 hat is most similar in sequence to mammalian SAP97, which is found at both synapses of the CNS, as we

290 in complexes with the key structural protein SAP97, which tightly regulates the synaptic delivery of

291 Kv1.1 was mediated by the signaling scaffold SAP97, which, through direct protein-protein interaction

292 interactions may regulate the association of SAP97 with its binding partners.

293 s that regulate the interaction of the MAGUK SAP97 with its GUK domain binding partner GKAP (GUK-asso

294 We propose that L27-mediated interactions of SAP97 with itself or other proteins regulate the synapti

295 e investigated the interaction of PSD-95 and SAP97 with voltage-gated or Kv K(+) channels.

296 binds to the first and second PDZ domains of SAP97, with higher affinity for PDZ2; no appreciable bin

297 CaMKIIalpha phosphorylated recombinant SAP97 within immune complexes in vitro and in intact cel

298 ing SAP97 compared with those not expressing SAP97 would function in local networks.

299 llular junction proteins dlg-A, PSD95/SAP90, SAP97, Z01, and Z02 and that contains DHR-, SH3-, and gu

300 sentation where it colocalizes with Kvbeta2, SAP97, ZIP, p56(lck), and CD4.