ライフサイエンスコーパス: lamin A

1 ress the GFP-tagged nuclear envelope protein lamin A.

2 erexpression of the nuclear envelope protein lamin A.

3 e caused by mutations in the nuclear protein lamin A.

4 of cells with well defined levels of ectopic lamin A.

5 the C-terminus of prelamin A to yield mature lamin A.

6 of progerin, a truncated splicing mutant of lamin A.

7 used by a truncated and farnesylated form of Lamin A.

8 n immediately after the last codon of mature lamin A.

9 step, mediated by ZMPSTE24, releases mature lamin A.

10 is frequently caused by an R482W mutation in lamin A.

11 ajor role in converting prelamin A to mature lamin A.

12 iched with the intermediate filament protein lamin A.

13 lpha and the mechanosensitive nuclear marker lamin-A.

14 s in the brain produce lamin C but almost no lamin A, a consequence of the removal of prelamin A tran

15 Lamin A, a key component of the nuclear lamina, is gener

16 d that Nelfinavir impaired the maturation of lamin A, a structural component of the nuclear envelope,

17 processed form of the nuclear lamina protein lamin A, accumulated in calcifying human VSMCs in vitro

18 Interleukin-1beta treatment inhibited lamin A accumulation, whereas treatment with prostagland

19 n E(2) (PGE(2) ) caused a marked increase in lamin A accumulation.

20 ilford progeria syndrome fibroblasts (mutant lamin A) also show evidence of H3K4me3 mesas, suggesting

21 otein 1alpha, and localize in proximity with Lamin A and B1 accumulation, whereas in newborn mice and

22 odes the essential nuclear envelope proteins lamin A and C (lamin A/C).

23 Lamin A and C are fundamental components of the nuclear

24 tations of the nuclear-architecture proteins lamin A and C cause misshapen nuclei and altered chromat

25 s the nuclear intermediate filament proteins lamin A and C, two major architectural elements of the m

26 Mutations in LMNA (lamin A/C), which encodes lamin A and C, typically cause age-dependent cardiac phe

27 of LAP2alpha, a protein that interacts with lamin A and chromatin, has no such effect on genome dyna

28 factor, (4) chromatin condensation, nuclear lamin A and DNA cleavage, fragmentation of the nuclear e

29 in C is abundant in the mouse brain, whereas lamin A and its precursor prelamin A are restricted to e

30 mina dispersion by direct phosphorylation of lamin A and lamin B1 in neuronal cells and primary corti

31 ssociated with an increased distance between lamin A and matrin-3.

32 ed by nuclear deformability as controlled by lamin-A and -B, and (ii) lamin levels directly modulate

33 rythroid differentiation is promoted by high lamin-A and low lamin-B1 expression whereas megakaryocyt

34 teomics-detected targets of mechanosensitive lamin-A and retinoids underscore the convergent synergy

35 The nuclear lamina is composed mainly of lamins A and C (A-type lamins) and lamins B1 and B2 (B-t

36 a silent mutation of the LMNA gene encoding lamins A and C (lamin A/C).

37 Since lamins A and C are fundamental determinants of nuclear s

38 Lamins A and C associate with lamina-associated polypept

39 Defects in lamins A and C cause an array of human diseases, includi

40 The relevance of lamins A and C in the brain remains unclear, but it is i

41 ear lamins are usually classified as A-type (lamins A and C) or B-type (lamins B1 and B2).

42 Lamins A and C, alternatively spliced products of the LM

43 Mutations in the LMNA gene, encoding lamins A and C, cause a variety of diseases collectively

44 ens inhibited the phosphorylation of nuclear lamins A and C, prevented the entry of DLAD into the nuc

45 gene encoding the nuclear envelope proteins lamins A and C, represent a diverse group of diseases th

46 functions of B-type lamins are subserved by lamins A and C.

47 the NE, visualized by fluorescently labeled lamin A, and of the chromatin globule surface (CGS) unde

48 ntibodies were found to co-immunoprecipitate lamin A, and the lamin-A binding domain was mapped to th

49 NA, lamin C and prelamin A (the precursor to lamin A), are produced in similar amounts in most tissue

50 gonist to increase or maintain expression of lamin-A as well as for RARG-agonist to repress expressio

51 n-Gilford progeria syndrome caused by mutant lamin A, as well as cells from patients with the disease

52 However, net migration was also biphasic in lamin-A, as wild-type lamin-A levels protected against s

53 expression of progerin, a truncated form of lamin A associated with premature aging.

54 established an activation barrier, with high lamin-A:B producing extruded nuclear shapes after migrat

55 cropipette aspiration both appear limited by lamin-A:B stoichiometry across hematopoietic lineages.

56 n A tail, 17 (13%) were previously described lamin A binding partners.

57 oss of function of differentiation-dependent lamin A binding to the MIR335 locus.

58 und to co-immunoprecipitate lamin A, and the lamin-A binding domain was mapped to the carboxy-termina

59 Here we seek to identify on a global scale lamin A-binding partners whose interaction is affected b

60 ome library, we identified and validated 337 lamin A-binding proteins.

61 The role of protein farnesylation in lamin A biogenesis and the pathogenesis of progeria has

62 aracterized the supramolecular structures of lamin A, C, B1, and B2 in mouse embryo fibroblast nuclei

63 ntractility thus tenses the nucleus to favor lamin-A,C accumulation and suppress soft tissue phenotyp

64 show that tension-dependent stabilization of lamin-A,C and myosin-IIA can suitably couple nuclear and

65 ess couples to myosin-II activity to promote lamin-A,C dephosphorylation at Ser22, which regulates tu

66 leoplasm, and phosphorylation is enriched on lamin-A,C fragments and is suppressed by a cyclin-depend

67 The nucleoskeletal protein lamin-A,C increases with matrix stiffness, confers nucle

68 Lamin-A,C knockdown in primary MSCs suppresses transcrip

69 Phosphorylated lamin-A,C localizes to nucleoplasm, and phosphorylation

70 Lamin-A,C phosphorylation is low in interphase versus di

71 enesis (a soft lineage) indeed increases LBR:lamin-A,C protein stoichiometry in MSCs versus osteogene

72 y diverse tissues and MSCs further show that lamin-A,C's increase with tissue or matrix stiffness ant

73 Levels of myosin-IIA thus parallel levels of lamin-A,C, with phosphosite mutants revealing a key role

74 traction force microscopy and from increased lamin-A,C.

75 ss resulting from increases in myosin-II and lamin-A,C.

76 are variants in two AD cardiomyopathy genes, lamin A/C (LMNA) and myosin binding protein C (MYBPC3).

77 Lamin A/C (LMNA) cardiomyopathy is a genetic disease wit

78 ical behavior of cardiomyocytes carrying the lamin A/C (LMNA) D192G mutation known to cause defective

79 Mutations in the Lamin A/C (LMNA) gene-encoding nuclear LMNA cause lamino

80 t malignant ventricular arrhythmias (MVA) in Lamin A/C (LMNA) mutation carriers.

81 ined diseases associated with alterations in lamin A/C (LMNA) splicing.

82 vestigate the gene and protein expression in Lamin A/C (LMNA)-mutated dilated cardiolaminopathy (DCM)

83 A mutation in the gene encoding Lamin A/C (LMNAp.R331Q ) led to reduced maximal force de

84 nd the non-sarcomeric gene mutation encoding lamin A/C (LMNAp.R331Q ).

85 iac phenotype in many laminopathies, whereby lamin A/C and emerin regulate gene expression through mo

86 deformation was governed by restructuring of Lamin A/C and increased heterochromatin content.

87 e determined that progerin binds directly to lamin A/C and induces profound nuclear aberrations.

88 UPR or not, prevents the phosphorylation of lamin A/C and LFCD in maturing LFCs in vivo, as well as

89 stablish the separate roles of chromatin and lamin A/C and show that they determine two distinct mech

90 aused nuclear morphology defects and reduced lamin A/C and SUN2 staining at the NE.

91 ions in patterns of H3K27me3 deposition, DNA-lamin A/C associations, and, at late passages, genome-wi

92 as a model, we found that reduced levels of lamin A/C at the onset of differentiation led to an anti

93 h the ability to block pathological progerin-lamin A/C binding may represent a promising strategy for

94 4, and JH13) that efficiently block progerin-lamin A/C binding.

95 Collectively, our results indicate that lamin A/C can modulate transcription through the regulat

96 The LAP2alpha-lamin A/C complex negatively affects cell proliferation.

97 CIP deficiency combined with lamin A/C deletion resulted in severe dilated cardiomyop

98 Here, we show that lamin A/C expressing cells can form an actin cap to resi

99 uclear stiffness is decreased by suppressing lamin A/C expression.

100 cytoskeleton) complex proteins together with lamin A/C for nuclear aberrations induced by Cofilin/ADF

101 (Sad1p/UNC84)-domain containing proteins and lamin A/C form the LInker of Nucleoskeleton-and-Cytoskel

102 SUMO1-dependent complex protects both RB and Lamin A/C from proteasomal turnover.

103 del for understanding both laminopathies and lamin A/C function is the Lmna(-/-) mouse.

104 Mutations in the lamin A/C gene (LMNA) cause a diverse spectrum of diseas

105 Mutations in the lamin A/C gene (LMNA) cause several disorders referred t

106 e, a mouse model of cardiomyopathy caused by lamin A/C gene (LMNA) mutation, and found that the extra

107 Cardiomyopathy caused by lamin A/C gene (LMNA) mutations (hereafter referred as L

108 Cardiomyopathy caused by lamin A/C gene mutations (LMNA cardiomyopathy) is charac

109 the data can be interpreted to suggest that lamin A/C has a role in the restart of stalled replicati

110 ng the differential effects of chromatin and lamin A/C in cell nuclear mechanics and their alteration

111 The role of actin and Lamin A/C in modulating these fluctuations is described.

112 method to profile the dynamic interactome of lamin A/C in multiple cell and tissue types under variou

113 We also find that lamin A/C interacts with TRF2 and that reduction in leve

114 Here, we show that lamin A/C is evolutionarily required for correct PcG pro

115 providing structure to the nuclear envelope, lamin A/C is involved in transcriptional regulation.

116 ere we show that SUMO1 conjugation of RB and Lamin A/C is modulated by the SUMO protease SENP1 and th

117 We propose that lamin A/C is required for maintaining genomic stability

118 w algorithms for image analysis reveals that lamin A/C knock-down leads to PcG protein foci disassemb

119 In contrast, lamin A/C levels control nuclear strain stiffening at la

120 ons, or a transcriptional down-regulation of lamin A/C levels in the constrained and isotropic geomet

121 However, how nuclear lamin A/C mediates the ability of the actin cap to regul

122 as demonstrated by significant reduction in lamin A/C mRNA levels and reduced lamin A/C protein in H

123 We found that a dominant negative lamin A/C mutant complemented the replication defect of

124 rces from the cytoskeleton and rigidity from lamin A/C nucleoskeleton can together regulate nuclear a

125 We identify additional roles for lamin A/C of the nuclear lamina and linkers of nucleus t

126 effects of the interaction between TRF2 and lamin A/C on chromosome structure.

127 ina during infection, and phosphorylation of lamin A/C on serine 22, which antagonizes lamin polymeri

128 vation induces CDK1, and CDK1 phosphorylates lamin A/C on serine 22.

129 ts with TRF2 and that reduction in levels of lamin A/C or mutations in LMNA that cause an autosomal d

130 These cells also showed decreased lamin A/C phosphorylation and metaphase arrest.

131 The suppression of lamin A/C phosphorylation and metaphase transition induc

132 lls have a much higher level of constitutive lamin A/C phosphorylation than do 293 cells over residue

133 h large T and small t contribute to enhanced lamin A/C phosphorylation.

134 There is evidence that lamin A/C plays a role in gene expression.

135 nce that the nuclear lamina filament protein Lamin A/C protects RB from proteasomal degradation.

136 duction in lamin A/C mRNA levels and reduced lamin A/C protein in HaCaT keratinocyte cells.

137 ll as regarding myocardial expression of the lamin A/C protein.

138 Mutations in lamin A/C result in a range of tissue-specific disorders

139 We found that lamin A/C serine 22 phosphorylation during HCMV infectio

140 However, lamin A/C siRNA pre-complexed with a commercial lipid-ba

141 owing recovery from the microneedle surface, lamin A/C siRNA retained full activity, as demonstrated

142 tion-induced changes in caldesmon 1 isoform, lamin A/C transcript variant 1, DEAD (Asp-Glu-Ala-Asp) b

143 In parallel, Lamin A/C was investigated in myocardial samples from DC

144 l dominant forms: LGMD1A (myotilin), LGMD1B (lamin A/C), LGMD1C (caveolin-3), LGMD1D (desmin), LGMD1E

145 Mutations in LMNA (lamin A/C), which encodes lamin A and C, typically cause

146 lized by co-localization with A-type lamins (lamin A/C).

147 ial nuclear envelope proteins lamin A and C (lamin A/C).

148 on of the LMNA gene encoding lamins A and C (lamin A/C).

149 response required the presence of vimentin, lamin A/C, and SUN (Sad1p, UNC-84)-domain protein linkag

150 it chromatin-remodeling molecules, including lamin A/C, barrier-to-autointegration factor (BAF), and

151 Knockdown of YY1 or lamin A/C, but not lamin A, led to a loss of lamina asso

152 P53, plus the nuclear architecture proteins Lamin A/C, in three different human cell lines.

153 levels of essential nuclear factors such as lamin A/C, lamin B, and HP1.

154 Finally, the mechanosensitive proteins YAP, Lamin A/C, Lamin B, MRTF-A, and MRTF-B were analyzed on

155 de, an intact F-actin, cytoskeletal tension, Lamin A/C, or substrate rigidity.

156 ctivity of pUL97 is to phosphorylate nuclear lamin A/C, resulting in altered nuclear morphology and i

157 ar envelope-associated components (Lamin B1, Lamin A/C, Sun1, Nesprin-3, Plectin) compared with contr

158 The finding of a mutation in lamin A/C, the cause of approximately 6% of idiopathic D

159 sphorylation of the nuclear lamina component lamin A/C, which disrupts the nuclear lamina.

160 at endogenous loci appear to be dependent on lamin A/C, YY1, H3K27me3, and H3K9me2/3 for maintenance

161 ts (cisplatin, camptothecin, and mitomycin), lamin A/C-deficient cells displayed normal gamma-H2AX fo

162 wing hydroxyurea-induced replication stress, lamin A/C-deficient cells had an increased frequency of

163 Here, we report that lamin A/C-deficient cells have a normal response to ioni

164 us recombination pathway, which is intact in lamin A/C-deficient cells.

165 in fibroblasts from laminopathy patients and lamin A/C-deficient mouse embryonic fibroblasts stably e

166 These functions are abrogated in lamin A/C-deficient mouse embryonic fibroblasts that rec

167 atin organization, and fitness of both human lamin A/C-depleted cells and HGPS-derived patient cells

168 This study reveals how the nuclear lamin A/C-mediated formation of the perinuclear apical a

169 In senescent cells, lamin A/C-negative, but strongly gamma-H2AX-positive and

170 Lamin B and primary human erythroblasts only Lamin A/C.

171 l interaction with nuclear envelope proteins lamin A/C.

172 7, -8, -9, poly (ADP-ribose) polymerase, and lamin A/C.

173 induce phosphorylation and reorganization of lamin A/C.

174 PK in HeLa cells or C2C12 myoblasts disrupts Lamin-A/C and Lamin-B1 localization and causes nuclear f

175 the expression of multiple lamins, including lamin-A/C, lamin-B1, and lamin-B2, in mammals has made i

176 Here we report in mice that lamin-A/C-deficient (Lmna(-/-)) and Lmna(N195K/N195K) mu

177 nuclear deformations after transmigration in lamin-A/C-deficient cells, whereas the wild-type cells s

178 izes to the NE and coimmunoprecipitates with Lamin-A/C.

179 Lamins A/C are encoded by LMNA, a single heterozygous mu

180 ibroblasts null for the expression of either lamins A/C or lamin B1, the remaining lamin meshworks ar

181 cleoplasm and interacts with the fraction of lamins A/C that is not associated with the peripheral nu

182 leads to loss of LAP2alpha and nucleoplasmic lamins A/C, impaired proliferation, and down-regulation

183 n to its cell cycle-inhibiting function with lamins A/C, LAP2alpha can also regulate extracellular ma

184 acellular matrix components independently of lamins A/C, which may help explain the proliferation-pro

185 pression but not the levels of nucleoplasmic lamins A/C.

186 on in LMNA, resulting in a truncated form of lamin A called progerin.

187 results in expression of a truncated form of Lamin A, called progerin.

188 By contrast, only lamin-A can ensure the localization of emerin within the

189 the failure to convert prelamin A to mature lamin A causes cardiomyopathy (at least in the absence o

190 Progerin, a mutated lamin A, causes the severe premature-aging syndrome Hutc

191 ibroblasts that express the Progerin form of lamin A, causing a major defect in nuclear import of the

192 A drug that inhibits pre-lamin A cleavage mimics the effects of progerin by disru

193 e aging disorder wherein a mutant version of lamin A, Delta50 lamin A, retains its farnesylation.

194 markers, and RARG-antagonist strongly drives lamin-A-dependent osteogenesis on rigid substrates, with

195 The tail domain of lamin A directly binds 21 known partners, including acti

196 Thus, Lmna(LAO/LAO) mice synthesize mature lamin A directly, bypassing prelamin A synthesis and pro

197 Testing them against 89 known lamin A disease mutations identified 50 disease-associat

198 Transfected chondrocytes that expressed lamin A displayed markers of early senescence/apoptosis.

199 mutant form of the nuclear scaffold protein lamin A distorts nuclei and sequesters nuclear proteins.

200 Depleting normal lamin A or inducing mutant lamin A expression are each sufficient to drive nucleola

201 r, administration of the exon 11 ASO reduced lamin A expression in wild-type mice and progerin expres

202 Lamin A expression was markedly elevated in OA cartilage

203 These effects of exogenous PGE(2) on lamin A expression were mediated via the EP(2) /EP(4) re

204 xpression of miR-9 in cultured cells reduced lamin A expression, and this effect was abolished when t

205 and cleavage of the nuclear membrane protein lamin A, expression of pro-apoptotic proteins c-Jun N-te

206 oteolytic event, caused by a mutation in the lamin A gene (LMNA) that eliminates the ZMPSTE24 cleavag

207 isease, is caused by a point mutation in the lamin A gene (LMNA).

208 matrix, cytoskeletal force dipoles, and the lamin A gene circuit illustrate the wide range of testab

209 mulation of progerin, an altered form of the Lamin A gene.

210 in mice and that direct synthesis of mature lamin A has little if any effect on the targeting of lam

211 Our results suggest that levels of lamin A have a marked effect on the ability of neutrophi

212 Mapping of the interaction sites on lamin A identified the immunoglobulin G (IgG)-like domai

213 On the basis of the position of K486 on the lamin A Ig-fold, we hypothesize the SUMO1 E2 enzyme reco

214 However, despite ubiquitous expression of lamin A in all differentiated cells, the HGPS mutation r

215 this study was to examine the expression of lamin A in cartilage from patients with osteoarthritis (

216 gest a novel mode of functional control over lamin A in cells.

217 The levels of mature lamin A in Lmna(LAO/LAO) mice were indistinguishable fro

218 t analysis confirmed increased expression of lamin A in OA compared with non-OA cartilage.

219 , and that increased nuclear accumulation of lamin A in response to catabolic stress may account for

220 eripheral tissues, but there was very little lamin A in the brain.

221 lecular regulation of chromatin diffusion by lamin A in the nuclear interior is critical for the main

222 ) embryonic fibroblasts; however, the mature lamin A in the tissues of Lmna(LAO/LAO) mice was positio

223 The posttranslational processing pathway of lamin A includes farnesylation of the C-terminus, likely

224 both actomyosin assembly and nucleoskeletal lamin-A increase.

225 eractors and suggest loss of tissue-specific lamin A interactions as a mechanism for the tissue-speci

226 present a systematic map of disease-relevant lamin A interactors and suggest loss of tissue-specific

227 ered biophysical properties and the matrin-3-lamin A interface is positioned to contribute to these d

228 Lamin A is formed from prelamin A by four post-translati

229 ly" mice (Lmna(PLAO/PLAO)), where all of the lamin A is produced from prelamin A.

230 ay also impact their deformability; although lamin A is typically down-regulated during granulopoiesi

231 The results of this study suggest that lamin A is up-regulated in OA chondrocytes, and that inc

232 Expression of lamin-A is known to be controlled by retinoic acid recep

233 A progerin allele of lamin-A is regulated in the same manner in iPSC-derived

234 Association of progerin, the lamin A isoform responsible for the premature aging diso

235 lation site to a conserved site in mammalian lamin A (LA), S268.

236 We apply BioID to lamin-A (LaA), a well-characterized intermediate filamen

237 Mutations in LMNA, the gene encoding lamin A, lead to a diverse set of inherited conditions i

238 nt form of the nuclear architectural protein lamin A, leading, through unknown mechanisms, to diverse

239 Knockdown of YY1 or lamin A/C, but not lamin A, led to a loss of lamina association.

240 nd decrease in cell fluidity with increasing lamin A levels.

241 n was also biphasic in lamin-A, as wild-type lamin-A levels protected against stress-induced death, w

242 into fat on soft matrix was enhanced by low lamin-A levels, whereas differentiation into bone on sti

243 Tissue stiffness and stress thus increase lamin-A levels, which stabilize the nucleus while also c

244 to bone on stiff matrix was enhanced by high lamin-A levels.

245 is caused by a single point mutation in the lamin A (LMNA) gene, resulting in the generation of prog

246 One protein not previously linked to lamin A, matrin-3, was selected for further study, becau

247 Three-dimensional mapping of the lamin A-matrin-3 interface showed that the LMNA truncati

248 rated by application to meshworks of nuclear lamin A, minifilaments of myosin II, and extracellular m

249 e human premature aging disorder caused by a lamin A mutant named progerin.

250 The lamin A mutation further promotes spatial clustering of

251 Our results link a laminopathy-causing lamin A mutation to an unsuspected deregulation of chrom

252 bly expressing a broad panel of laminopathic lamin A mutations, we found that several mutations assoc

253 atalytic activity is critical for processing lamin A on the inner nuclear membrane and clearing clogg

254 In lamin A-only knockin mice, where alternative splicing is

255 s this issue, we created mice with a "mature lamin A-only" allele (Lmna(LAO)), which contains a stop

256 Depleting normal lamin A or inducing mutant lamin A expression are each s

257 s assessed using precursor accumulation (for lamin A) or a MAPLE3 photoconvertible tag (for lamin B1)

258 Applying our system to lamin-A overexpressing fibrosarcoma cells, we found a ma

259 The lamin A-overexpressing neutrophil-type cells showed simi

260 The effects of lamin A overexpression on mitochondrial function and apo

261 We show in this study that the lamin A p.R482W hot spot mutation prevents adipogenic ge

262 lation correlated with downregulation of the lamin A processing enzyme Zmpste24/FACE1, and FACE1 mRNA

263 actor 2 (SRSF2), and SRSF2 knockdown lowered lamin A production in cells and in murine tissues.

264 Lamin A protects nuclei from the impact of actomyosin ac

265 To gain insight about lamin A protein interactions, binding proteins associate

266 tic splice donor site, resulting in a mutant lamin A protein known as progerin.

267 NA and the production of a dominant-negative lamin A protein, known as progerin.

268 LMNA that produces the farnesylated aberrant lamin A protein, progerin.

269 s budding involves phosphorylation of A-type lamin, a protein linked to muscular dystrophies.

270 Matrix stiffness directly influenced lamin-A protein levels, and, although lamin-A transcript

271 clear entry of RA receptors was modulated by lamin-A protein.

272 Lamin-A proved rate-limiting in 3D migration of diverse

273 The nuclear structure protein lamin A provides one example, with protein and transcrip

274 Progerin is a mutant form of lamin A responsible for Hutchinson-Gilford progeria synd

275 The mutant form of lamin A responsible for the premature aging disease Hutc

276 wherein a mutant version of lamin A, Delta50 lamin A, retains its farnesylation.

277 ed that levels of the nucleoskeletal protein lamin-A scaled with tissue elasticity, E, as did levels

278 Interestingly, depletion of lamin A strikingly alters genome dynamics, inducing a dr

279 brane (INM) by comparative BioID analysis of lamin A, Sun2 and a minimal INM-targeting motif.

280 membrane association of farnesylated Delta50 lamin A tail domains requires calcium.

281 orting this model, SUMO1-modification of the lamin A tail is reduced by two FPLD-causing mutations, G

282 0 nuclear proteins found associated with the lamin A tail, 17 (13%) were previously described lamin A

283 or new posttranslational modification of the lamin A tail.

284 constitutive attachment of a mutant form of lamin A (termed progerin) to the nuclear membrane.

285 romosomal inter-chain interactions formed by lamin A throughout the nucleus contribute to chromatin d

286 te that this mutation impairs the ability of lamin A to repress the anti-adipogenic miR-335, providin

287 s widely assumed to be crucial for targeting lamin A to the nuclear envelope.

288 has little if any effect on the targeting of lamin A to the nuclear rim in mouse tissues.

289 uenced lamin-A protein levels, and, although lamin-A transcription was regulated by the vitamin A/ret

290 l as retinoic acid addition, which regulates lamin-A transcription.

291 In a mouse model for HGPS, a similar Lamin A variant causes the proliferative arrest and deat

292 This mutation generates the lamin A variant progerin, which we show here leads to lo

293 an interaction hotspot and demonstrated that lamin A variants, which destabilize the Ig-like domain,

294 The nucleoskeletal protein lamin-A varies both within and between cell types and wa

295 binding proteins associated with the tail of lamin A were characterized.

296 nto prelamin A transcripts, large amounts of lamin A were found in peripheral tissues, but there was

297 role in the posttranslational processing of lamin A, which may be important in disease pathogenesis.

298 associated polypeptide-alpha) interacts with lamin A, while its interaction with progerin is signific

299 t a conformational change induced in Delta50 lamin A with divalent cations plays a regulatory role in

300 polarize quickly, increasing nucleoskeletal lamin-A yet expressing the 'scar marker' smooth muscle a