ライフサイエンスコーパス: aPKC

1 aPKC adopts a polarised localisation in PrE cells only a

2 aPKC associated with Mst1/2, which uncoupled Mst1/2 from

3 aPKC functions to promote GLI1 association with LAP2alph

4 aPKC, an apical polarity regulator, maintains the robust

5 aPKC-iota/lambda and its polarity signalling partners co

6 aPKC-iota/lambda functions downstream of SMO to phosphor

7 aPKC-lambda has recently been implicated in epidermal di

8 aPKC-lambda, as well as Par3, localizes at the presumpti

9 e context of the full-length, purified Par-6-aPKC complex.

10 e anterior/lateral localisation of the Par-6/aPKC complex and the posterior recruitment of Par-1, whi

11 or axis of the oocyte by targeting the Par-6/aPKC complex for degradation at the oocyte posterior.

12 The Par-6/aPKC complex is ectopically localised to the posterior o

13 The Par-3/Par-6/aPKC complex is the primary determinant of apical polari

14 phila neuroblasts, the Inscuteable/Baz/Par-6/aPKC complex recruits Pins apically to induce vertical s

15 Aberrant aPKC activity disrupts polarity, yet the mechanisms that

16 polarize cells, these proteins must activate aPKC within a spatially defined membrane domain on one s

17 Activated aPKC-iota/lambda is upregulated in SMO-inhibitor-resista

18 to phosphorylation by mitotically activated aPKC kinase and thought to promote asymmetric cell divis

19 Overexpression of activated aPKC blocks the neuronal differentiation-promoting activ

20 localization, Par-6 allosterically activates aPKC to allow for high spatial and temporal control of s

21 dimerization, and this interaction activates aPKC by displacing the pseudosubstrate, although full ac

22 How PIP3 activates aPKC is unknown.

23 ontrast, expression of constitutively active aPKC elevates basolateral accumulation of Smo and promot

24 6, vang, pk, and fmi are upregulated, and an aPKC mutation suppresses the Rbf1-induced phenotypes.

25 he B-cell differentiation program through an aPKC lambda/iota-Erk dependent Etv5/Satb2 chromatin repr

26 lpha (TNFalpha) is necessary for iPMF via an aPKC-dependent mechanism.

27 Incubation with an aPKC pseudosubstrate recapitulates the phenotype of PKCi

28 on with junctional components; the tjp-2 and aPKC mRNA-rescued embryos also had 24 and 45% decreases

29 Par-6 and aPKC interact via PB1 domain heterodimerization, and thi

30 In T2DM, whereas Akt and aPKC activation are diminished in muscle, and hepatic Ak

31 Additionally, Akt and aPKC activities in muscle improved, as did glucose intol

32 resting/basal and insulin-stimulated Akt and aPKC activities were diminished in muscle, but in liver,

33 uestered to cell-cell junctions by Amot, and aPKC overexpression resulted in loss of Amot expression

34 Both Bazooka and aPKC regulate Canoe localization despite being "downstre

35 Further, Rap1, Bazooka, and aPKC, but not Canoe, regulate columnar cell shape.

36 We searched for overlapping BH and aPKC phosphorylation site motifs (i.e., putative phospho

37 ng the formation of a cable where Crumbs and aPKC are localized.

38 ts divisions, but Inscuteable expression and aPKC, dlg and pins mutants have no effect.

39 ncident manner by both JNK-dependent Fos and aPKC-mediated Yki transcription.

40 reciprocal interactions between Crb, Moe and aPKC during cellular morphogenesis.

41 Furthermore, Moe and aPKC functioned antagonistically, suggesting that Moe li

42 lin promotes the association of both p62 and aPKC with the insulin-regulated scaffold IRS-1.

43 Specifically, we show that Par3 and aPKC promote the apical positioning of centrioles, where

44 ymmetry in various systems, whereas Par3 and aPKC/Par6 can also act independently.

45 ot essential for the recruitment of Par6 and aPKC to the membrane, it is required for their apical lo

46 Our results suggest that Rab14 and aPKC interact to regulate trafficking of claudin-2 out o

47 human Lgl2 in both its unphosphorylated and aPKC-phosphorylated states.

48 Thus, Yrt and aPKC are involved in a reciprocal antagonistic regulator

49 sults reveal how Par3/Baz CR3 can antagonize aPKC in stable apical Par complexes and suggests that mo

50 Slmb function is required to restrain apical aPKC activity in a manner that is independent of endolys

51 Here, we show that the function of the Baz/aPKC/Par6 apical polarity complex in somatic cyst cells

52 agonistic intermolecular competition between aPKC isoforms directs the establishment of neuronal pola

53 unctional complex, especially aPKC, and both aPKC and Bves are indispensable to claudin expression.

54 Here, we show that deletion of both aPKC isoforms resulted in a deficit in asymmetric divisi

55 y by controlling the phosphorylation of both aPKC isoforms.

56 osphorylation experiments revealed that both aPKC isoforms were substrates of PHLPP.

57 o sorting into the retromer pathway via both aPKC-dependent and -independent mechanisms.

58 Both aPKCs have pleiotropic context-dependent functions that

59 e 2 leads to translocation of membrane-bound aPKC to the cytosol, concurrent with its activation and

60 tex but were displaced into the cytoplasm by aPKC.

61 and assembly of zBves were not influenced by aPKC-MO.

62 ggest that peridermal polarity, initiated by aPKC, is transduced in a stepwise manner by E-cadherin t

63 ted potential independently of regulation by aPKC.

64 eta-propeller structure that is unchanged by aPKC phosphorylation of an unstructured loop in its seco

65 iPMF requires atypical protein kinase C (aPKC) activity within spinal segments containing the phr

66 ith expression of atypical protein kinase C (aPKC) at the contact-free domain, nuclear expression of

67 ling intermediate atypical protein kinase C (aPKC) constrains food intake, weight gain, and glucose i

68 Atypical protein kinase C (aPKC) controls cell polarity by modulating substrate cor

69 larvae (Lgl) and atypical Protein Kinase C (aPKC) ensures self-renewal of a daughter neuroblast and

70 Atypical protein kinase C (aPKC) enzymes signal on protein scaffolds, yet how they

71 AR-6, CDC-42, and atypical protein kinase C (aPKC) form a core unit of the PAR protein network, which

72 naling to Akt and atypical protein kinase C (aPKC) in liver and muscle and hepatic enzyme expression

73 ulin signaling to atypical protein kinase C (aPKC) in muscle and liver that generate cardiovascular r

74 Atypical protein kinase C (aPKC) is a key apical-basal polarity determinant and Par

75 Activity of the atypical protein kinase C (aPKC) is a key output of the Par complex as phosphorylat

76 suggests that the atypical Protein Kinase C (aPKC) is a key regulator of cell fate decisions in metaz

77 The atypical protein kinase C (aPKC) is a key regulator of polarity and cell fate in lo

78 al loss of either atypical protein kinase C (aPKC) isoform, PKCzeta or PKClambda/iota, partially impa

79 Atypical protein kinase C (aPKC) isoforms are overexpressed and activated in many c

80 Atypical protein kinase C (aPKC) isoforms zeta and lambda interact with polarity co

81 The atypical protein kinase C (aPKC) isotypes PKClambda/iota and PKCzeta are both expre

82 Atypical protein kinase C (aPKC) isozymes are unique in the PKC superfamily in that

83 Atypical protein kinase C (aPKC) isozymes modulate insulin signaling and cell polar

84 Atypical protein kinase C (aPKC) isozymes, PKClambda/iota and PKCzeta, are now cons

85 r, we report that atypical protein kinase C (aPKC) phosphorylates Yrt to prevent its premature apical

86 nserved Par3/Par6/atypical protein kinase C (aPKC) polarity cassette that restricts migration of baso

87 show that the PAR-atypical protein kinase C (aPKC) polarity complex inhibits EMT and invasion by prom

88 ctor complex Par6-atypical protein kinase c (aPKC) regulate multiple steps during epithelial differen

89 roteins Par-6 and atypical protein kinase C (aPKC) to specific cortical sites.

90 complex component atypical Protein Kinase C (aPKC) to the essential spindle orientation factor GukHol

91 ylation of Lgl by atypical protein kinase C (aPKC), a component of the partitioning-defective (Par) c

92 ere, we show that atypical protein kinase C (aPKC), a protein associated with apicobasal polarity, is

93 x, which contains atypical protein kinase C (aPKC), Bazooka (Par-3), and Par-6, is required for estab

94 rectly antagonize atypical protein kinase C (aPKC), but may instead restrict aPKC localization by ena

95 kinases, Akt and atypical protein kinase C (aPKC), were maximally increased.

96 The protein atypical protein kinase C (aPKC)--a component of the Par complex, which localizes t

97 The PAR-3-atypical protein kinase C (aPKC)-PAR-6 complex has been implicated in the developme

98 ens junctions and atypical protein kinase C (aPKC).

99 al maintenance of atypical protein kinase C (aPKC).

100 ele of Drosophila atypical Protein Kinase C (aPKC).

101 nd the downstream atypical protein kinase C (aPKC).

102 file of proteins (atypical protein kinase C [aPKC], Cdc42, Sec8, Rab11a, and Rab8) and ceramide speci

103 ical actin nucleation that depends on Cdc42, aPKC, and Par6.

104 actions, recruitment of Sdt-aPKC-Par6-cdc42, aPKC phosphorylation of Crb, and recruitment of Expanded

105 to more lateral cell surfaces enables Cdc42/aPKC/Par6 to take on a mitosis-specific function-aiding

106 determines spatiotemporal patterns of Cdc42/aPKC activation during endothelial morphogenesis.

107 Pharmacological inhibition of CNS aPKC activity acutely increases food intake and worsens

108 increases in activity of cocompartmentalized aPKC.

109 3's second PDZ domain and a highly conserved aPKC PDZ-binding motif (PBM) that is required in the con

110 In contrast, aPKC activity associated with WD40/ProF was increased.

111 ong with the molecular pathways that control aPKC and those that are responsive to changes in its cat

112 ts polarity, yet the mechanisms that control aPKC remain poorly understood.

113 ts previously described roles in controlling aPKC localization, Par-6 allosterically activates aPKC t

114 Conversely, aPKC protects Par6B from proteasomal degradation, in a k

115 e absence of lgl function, elevated cortical aPKC kinase activity perturbs unequal partitioning of th

116 To investigate how increased cortical aPKC function induces formation of excess neuroblasts, w

117 neuroblasts triggered by increased cortical aPKC function.

118 propose that precise regulation of cortical aPKC kinase activity distinguishes the sibling cell iden

119 In return, Yrt counteracts aPKC functions to prevent apicalization of the plasma me

120 In 2D cultures, aPKC induced cells to grow as stratified epithelia, wher

121 de prevents activation of HDAC6 by cytosolic aPKC and AurA, which promotes acetylation of tubulin in

122 Defective aPKC signaling results in a dramatically simplified glom

123 netically encoded reporter that we designed, aPKC-specific C kinase activity reporter (aCKAR), we fou

124 idues in the Akt pleckstrin homology domain, aPKCs lack this domain.

125 account for the selective signaling of each aPKC isotype.

126 hese results led us to propose that elevated aPKC function in the cortex of mitotic neuroblasts reduc

127 ic alternative transcript, and Prkcl encodes aPKC-lambda.

128 Prkcz encodes aPKC-zeta and PKM-zeta, a truncated, neuron-specific alt

129 We conclude that epithelial aPKC acts upstream of multiple mechanisms that participa

130 ay of the PAR junctional complex, especially aPKC, and both aPKC and Bves are indispensable to claudi

131 rk has implicated the apical polarity factor aPKC, the junctional protein APC2, and basal integrins i

132 RECENT FINDINGS: aPKC and Akt mediate the insulin effects on glucose tran

133 Of importance, Yap1 was necessary for aPKC-mediated overgrowth but did not restore cell polari

134 A form of Lgl that is a substrate for aPKC, but not Aurora kinases, can restore cell polarity

135 ation of the Par-3 phosphorylation site from aPKC's kinase domain but does not disrupt the Par-3 PDZ2

136 We achieved full aPKC down-regulation in small intestine villi and colon

137 Furthermore, aPKC and other apical polarity factors disappear from th

138 Furthermore, aPKC-deficient podocytes failed to form the normal netwo

139 Key polarity genes aPKC, par6, vang, pk, and fmi are upregulated, and an aP

140 ortical polarity pathway (NuMA, p150(glued), aPKC).

141 Hepatic aPKC is a unifying target for treating multiple clinical

142 Imbalance between muscle and hepatic aPKC activation (and expression of PKC-iota in humans) b

143 epatic Akt activation is diminished, hepatic aPKC activation is conserved.

144 of hyperinsulinemia by inhibition of hepatic aPKC and improvement in systemic insulin resistance, bra

145 Indeed, selective inhibition of hepatic aPKC by adenoviral-mediated expression of kinase-inactiv

146 Conserved activation of hepatic aPKC in hyperinsulinemic states of T2DM, obesity and Met

147 Moreover, inhibition of hepatic aPKC reduced its association with WD40/ProF, restored WD

148 gation of aPKC toward the anterior but holds aPKC in an inactive state, and a CDC-42-dependent assemb

149 However, aPKC helps to sharpen the pattern of Miranda, by keeping

150 These data implicate aPKC as a novel regulator of energy and glucose homeosta

151 al for HH-dependent processes and implicates aPKC-iota/lambda as a new, tumour-selective therapeutic

152 xpression of PHLPP resulted in a decrease in aPKC phosphorylation at both the activation loop and the

153 viral-mediated expression of kinase-inactive aPKC, or newly developed small-molecule biochemicals, dr

154 ry neuroblast phenotype induced by increased aPKC function.

155 es; conversely, knockdown of PHLPP increased aPKC phosphorylation.

156 However, whether increased aPKC function triggers formation of excess neuroblasts b

157 aPKC (>90%) led to loss in biguanide-induced aPKC phosphorylation, it had no effect on Met-stimulated

158 (ZIP), has been extensively used to inhibit aPKC activity; however, we have previously shown that ZI

159 member Par-6, previously thought to inhibit aPKC, is a potent activator of aPKC in our assays.

160 l cortical displacement assay to investigate aPKC regulation.

161 onic hippocampal neurons, two aPKC isoforms, aPKC-lambda and PKM-zeta, are expressed.

162 smantles the apical domain, showing that its aPKC-mediated exclusion is crucial for epithelial cell p

163 Upon recruitment to primordial junctions, aPKC phosphorylates JAM-A at S285 to promote the maturat

164 e apically localized serine/threonine kinase aPKC directly phosphorylates an N-terminal site of the c

165 er the influence of another polarity kinase, aPKC/PKC-3.

166 eraction with GukH at cortical sites lacking aPKC.

167 hrough atypical protein kinase Ciota/lambda (aPKC) and HDAC1.

168 ntify atypical protein kinase C iota/lambda (aPKC-iota/lambda) as a novel GLI regulator in mammals.

169 thered to the acidic surface on p62, locking aPKC in an open, signaling-competent conformation.

170 strate sequence are required for maintaining aPKCs in an inactive state and are targeted by PIP3 for

171 However, whether mammalian aPKCs control stem cells and fate in vivo is not known.

172 it was necessary for MZ localization of Moe, aPKC and F-actin.

173 Moreover, aPKC has an additional positive role in Hh signaling by

174 We demonstrate that the resulting mutant aPKC kinase can be specifically inhibited in vitro and i

175 find that the localization and activation of aPKC involve distinct, specialized aPKC-containing assem

176 In HeLa cells, S1P-dependent activation of aPKC suppressed apoptosis.

177 n is problematic, as excessive activation of aPKC-dependent lipogenic, gluconeogenic and proinflammat

178 ht to inhibit aPKC, is a potent activator of aPKC in our assays.

179 P does not inhibit the catalytic activity of aPKC isozymes in cells.

180 inical data reveal the concerted activity of aPKC, cortactin, and dynamin-2, which control the traffi

181 hate (S1P) promoted the cellular activity of aPKC.

182 ggesting that it antagonizes the activity of aPKC.

183 studies demonstrated that the aggregation of aPKC around the cell junctions had disintegrated in zBve

184 ramide reestablishes membrane association of aPKC, restores primary cilia, and accelerates neural pro

185 Cycling of aPKC between these distinct functional assemblies, which

186 However, although cellular depletion of aPKC (>90%) led to loss in biguanide-induced aPKC phosph

187 sotropy leads to anisotropic distribution of aPKC, which in turn can negatively regulate Rok, thus pr

188 ectly bound to the purified kinase domain of aPKC and relieved autoinhibitory constraints, thereby ac

189 In contrast, the effect of aPKC on Hippo/Yap signaling and overgrowth in NMuMG cell

190 ation of Yap1, indicating that the effect of aPKC on transformed growth by deregulating Hippo/Yap1 si

191 Finally, increased expression of aPKC in human cancers strongly correlated with increased

192 Finally, the expression of aPKC is up-regulated by Hh signaling in a Ci-dependent m

193 zation of aPKCs and reduced the formation of aPKC-Par3 complex.

194 the biochemical and biological functions of aPKC.

195 Inactivation of aPKC by either RNAi or a mutation inhibits Smo basolater

196 rthermore, we demonstrate that inhibition of aPKC by small-molecule pharmacological modulation or Tri

197 ted in vitro and in vivo Acute inhibition of aPKC during NB polarity establishment abolishes asymmetr

198 We show that inhibition of aPKC from the mid blastocyst stage not only prevents sor

199 Inhibition of aPKC, AurA, or a downstream target of AurA, HDAC6, resto

200 ur findings indicate a direct involvement of aPKC in Hh signaling beyond its role in cell polarity.

201 The levels of aPKC and Par-6 are significantly increased in slmb mutan

202 t in only one aPKC isoform, complete loss of aPKC unexpectedly increased CD8(+) T cell differentiatio

203 Genetic or pharmacological loss of aPKC-iota/lambda function blocks HH signalling and proli

204 reviously undescribed molecular mechanism of aPKC regulation, a molecular target for S1P in cell surv

205 mide-binding but dominant-negative mutant of aPKC suppresses ciliogenesis, indicating that the associ

206 ome of the diverse physiological outcomes of aPKC's function in differentiation, along with the molec

207 Silencing of PKM-zeta or overexpression of aPKC-lambda in hippocampal neurons alters neuronal polar

208 formin induced activation/phosphorylation of aPKC in L6 myotubes.

209 e associated with reduced phosphorylation of aPKC, disruption of Par-complex localization, and spindl

210 ng in displacement of the pseudosubstrate of aPKC and re-engagement in the substrate-binding cavity.

211 Finally, we show that down-regulation of aPKC, involved in cell polarity, decreases the number of

212 tion, we showed that PDK1 aids the rescue of aPKC in in vitro rephosphorylation assays using immunode

213 To assess the role of aPKC in PrE formation, we interfered with its activity u

214 y cues and promotes efficient segregation of aPKC toward the anterior but holds aPKC in an inactive s

215 ne localization, indicating sequestration of aPKC by IRS-1 away from MARK2.

216 Silencing of aPKC in invasive breast-tumor cell lines impaired the de

217 Genetic or pharmacological targeting of aPKC impairs human oncogenic addicted leukemias.

218 caffolds serving as allosteric activators of aPKCs, tethering them in an active conformation near spe

219 altered the apical membrane localization of aPKCs and reduced the formation of aPKC-Par3 complex.

220 port a model in which the pseudosubstrate of aPKCs is tethered to the acidic surface on p62, locking

221 hanism underlying the negative regulation of aPKCs remains largely unknown.

222 ional assemblies, which appears to depend on aPKC activity, effectively links cue-sensing and effecto

223 unlike CD8(+) T cells deficient in only one aPKC isoform, complete loss of aPKC unexpectedly increas

224 odulation of CR3 inhibitory arms or opposing aPKC pockets would perturb the interaction, promoting Pa

225 depleted for the apical determinants Par6 or aPKC had identical ectopic seamed tube defects.

226 larized lipid domains and failure of the Par/aPKC/Cdc42 polarity complex to localize to the apical me

227 polarity protein complexes such as the Par3-aPKC-Par6 complex and the CRB3-Pals1-PATJ complex, which

228 in mislocalization of several apical (Par6, aPKC, and Pals1) and basolateral (Llgl1 and Llgl2) ident

229 However, membrane localization of Baz, Par6-aPKC and Crb all depend on Cdc42.

230 photoreceptor, membrane recruitment of Par6-aPKC also depends on Baz.

231 at this factor promotes the handover of Par6-aPKC from Baz onto Crb.

232 together with the Par complex (Baz/Par3-Par6-aPKC), Crumbs (Crb/CRB3) and Stardust (Sdt/PALS1).

233 rove process-specific activation of the Par6-aPKC pathway, stimulating the transition from junction f

234 cadherin) endocytosis by limiting Cdc42/Par6/aPKC complex activity.

235 d the apical recruitment of a Par3/Par6alpha/aPKC/Rac1 signaling module for a robust, spatially local

236 Paradoxically, aPKC also phosphorylates Par3/Baz, provoking its relocal

237 e domain but does not disrupt the Par-3 PDZ2-aPKC PBM interaction.

238 of the steady-state levels of atypical PKC (aPKC [PKCiota/lambda and zeta]) and is blocked in inflam

239 Atypical PKC (aPKC) isoforms are activated by the phosphatidylinositol

240 his study, we demonstrate that atypical PKC (aPKC) regulates Smo phosphorylation and basolateral accu

241 amide and its interaction with atypical PKC (aPKC), both of which distribute to the primary cilium an

242 he polarity complex made up of atypical PKC (aPKC, isoforms iota and zeta), Par6, and Par3 determine

243 Atypical PKCs (aPKCs) are implicated as key regulators of epithelial po

244 Atypical PKCs (aPKCs) have been implicated in Met-stimulated GU, and in

245 te progression are interdependent, and place aPKC as a central player in the segregation of epiblast

246 Under intact apical-basal polarity, aPKC kinases phosphorylate S249 of SNAI1, which leads to

247 Loss of apical-basal polarity prevents aPKC-mediated SNAI1 phosphorylation and stabilizes the S

248 rms a tight inhibitory complex with a primed aPKC kinase domain, blocking substrate access.

249 Initially, the Par proteins aPKC and Bazooka form discrete foci at the apical cortex

250 PDK1, pT555-aPKC, and pAkt were dependent on dynamin activity.

251 identify a novel role of PHLPP in regulating aPKC and cell polarity.

252 and analyzed the stability of the remaining aPKC pool.

253 The ability of Yrt to bind and restrain aPKC signaling is central for its role in polarity, as r

254 in kinase C (aPKC), but may instead restrict aPKC localization by enabling the aPKC-inhibiting activi

255 nveils a novel mechanism by which scaffolded aPKC is maintained in an active conformation.

256 ular domain interactions, recruitment of Sdt-aPKC-Par6-cdc42, aPKC phosphorylation of Crb, and recrui

257 t of apical-basal polarity (A-BP) signaling, aPKC, also inhibits Dishevelled1-induced Frizzled3 hyper

258 ha is sufficient to elicit pMF via a similar aPKC-dependent mechanism.

259 vation of aPKC involve distinct, specialized aPKC-containing assemblies: a PAR-3-dependent assembly t

260 via a TNFalpha-dependent increase in spinal aPKC activity.

261 o iPMF, TNFalpha-induced pMF required spinal aPKC activity, as intrathecal delivery of a zeta-pseudos

262 Upstream signal(s) leading to spinal aPKC activation are unknown.

263 MO-inhibitor-resistant tumours and targeting aPKC-iota/lambda suppresses signalling and growth of res

264 Both scaffolds tether aPKC in an active conformation as assessed through pharm

265 These results demonstrate that aPKC-iota/lambda is critical for HH-dependent processes

266 We find that aPKC is autoinhibited by two domains within its NH(2)-te

267 Here we tested the hypothesis that aPKC has a dual function in epithelia, inhibiting the NF

268 elial cells (MDCK and NMuMG), we report that aPKC gain of function overcomes contact inhibited growth

269 In this paper, we show that aPKC can interact directly with JAM-A in a PAR-3-indepen

270 The results show that aPKC is dispensable for polarity after cell differentiat

271 We previously showed that aPKC is down-regulated in intestinal epithelia under inf

272 me-wide transcriptional profiling shows that aPKC-iota/lambda and SMO control the expression of simil

273 Our results suggest that aPKC isoforms orchestrate the formation of the podocyte

274 Our data suggest that aPKC phosphorylates JAM-A at S285 to regulate cell-cell

275 The aPKC defect resulted in increased NF-kappaB activity, wh

276 The aPKC-mediated phosphorylation of Smo at Ser680 promotes

277 ied by Crumbs (Crb), Stardust (Sdt), and the aPKC-Par6-cdc42 complex.

278 flanking its PKC consensus site disrupts the aPKC kinase N lobe, separating P-loop/alphaB/alphaC cont

279 -lambda for binding to Par3 and disrupts the aPKC-lambda-Par3 complex.

280 d restrict aPKC localization by enabling the aPKC-inhibiting activity of Lgl.

281 rically dividing Drosophila neuroblasts, the aPKC PBM is required for cortical targeting, consistent

282 Consistent with this, overexpression of the aPKC antagonist Lgl strongly rescues the polarity defect

283 for its role in polarity, as removal of the aPKC binding site neutralizes Yrt activity.

284 Similarly, selective deletion of the aPKC isoform Pkc-lambda in proopiomelanocortin (POMC) ne

285 tially control the catalytic activity of the aPKC PKCzeta, thus promoting activity toward localized s

286 Using the aPKC substrate MARK2 as another readout for activity, we

287 ila optic lobe neuroepithelial cells through aPKC activity-dependent myosin II regulation.

288 he role of basic arginine residues common to aPKC pseudosubstrate sequences.

289 that both classes of SMO variants respond to aPKC-iota/lambda or GLI2 inhibitors that operate downstr

290 The ACBD3 binding region of Numb harbors two aPKC phosphorylation sites, serines 48 and 52.

291 that, in embryonic hippocampal neurons, two aPKC isoforms, aPKC-lambda and PKM-zeta, are expressed.

292 that ZIP inhibits the activity of wild-type aPKC, but not a construct lacking the pseudosubstrate.

293 cule A (JAM-A) to primordial junctions where aPKC is activated by Rho family small guanosine triphosp

294 promote its mitotic relocalization, whereas aPKC kinase activity is required only for polarization o

295 te, and a CDC-42-dependent assembly in which aPKC is active but poorly segregated.

296 o doing, unveiled a novel mechanism by which aPKCs are maintained in an active conformation on a prot

297 cating that the association of ceramide with aPKC is critical for the formation of this complex.

298 PKM-zeta competes with aPKC-lambda for binding to Par3 and disrupts the aPKC-la

299 When co-localized with aPKC, Dlg is phosphorylated in its SH3 domain which disr

300 ly with phospholipids and also overlaps with aPKC phosphorylation sites.