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 e caused by mutations in the nuclear protein lamin A.

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

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

5 iched with the intermediate filament protein lamin A.

6 erexpression of the nuclear envelope protein lamin A.

7 ed precursor of the nuclear scaffold protein lamin A.

8 lpha and the mechanosensitive nuclear marker lamin-A.

9 cular weight human heart proteoforms such as lamin A (72 kDa) and trifunctional enzyme subunit alpha

10 We also identified that Lamin A, a cell nuclear lamina member, is a unique marke

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

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

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

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

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

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

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

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

19 Our findings establish a direct link between lamin A and PcG epigenetic silencing and indicate that l

20 Deficiencies in lamin-A and repair factors exacerbate these effects, but

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

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

23 Lamins A and C are intermediate filaments that provide s

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

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

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

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

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

29 Increased levels of lamin A are known to increase the rigidity of nuclei, in

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

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

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

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

34 repair factors exacerbate these effects, but lamin-A-associated defects are rescued by repair factor

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

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

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

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

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

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

41 low phosphorylation and slow degradation of lamin-A by matrix-metalloprotease-2 (MMP2), and inhibiti

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

43 eus, including nuclear morphology, levels of lamin A,C, and histone deacetylation, as these tensile s

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

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

46 essing HCV proteins showed downregulation of lamin-A,C and upregulation of beta-actin, corroborating

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

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

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

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

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

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

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

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

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

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

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

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

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

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

61 Lamin A/C (LMNA) gene mutations are a known cause of fam

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

63 Lamin A/C (LMNA) is one of the most frequently mutated g

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

65 178 patients (37%): 54 (11%) Titin; 19 (4%) Lamin A/C (LMNA); 24 (5%) structural cytoskeleton-Z disk

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

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

68 Mutations in LMNA encoding lamin A/C and EMD encoding emerin cause cardiomyopathy a

69 Mice without lamin A/C and emerin are born at the expected Mendelian

70 erozygous deletion of this gene lacking both lamin A/C and emerin are born at the expected Mendelian

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

72 slower heart rates in the mice lacking both lamin A/C and emerin.

73 d a shorter lifespan than those only lacking lamin A/C and emerin.

74 nd recruitment of PKC-delta to phosphorylate lamin A/C and facilitate porcine circoviral nuclear egre

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

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

77 to LRRK2 knockdown, cause disorganization of lamin A/C and leakage of nuclear proteins.

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

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

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

81 ane, hence abolishing the phosphorylation of lamin A/C and the rearrangement of nuclear lamina.

82 utations mostly abolish the interaction with lamin A/C and, similar to LRRK2 knockdown, cause disorga

83 We identify increased levels of lamin A/C as a robust molecular phenotype in the heart o

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

85 aa 41 to 60) of p17 and p17 colocalized with lamin A/C at the nuclear envelope.

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

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

88 New pS22-Lamin A/C binding was accompanied by increased histone a

89 4, and JH13) that efficiently block progerin-lamin A/C binding.

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

91 l changes observed in cells of patients with Lamin A/C cardiomyopathies.

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

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

94 otype in the heart of SMA mice and show that lamin A/C dysregulation is also apparent in SMA patient

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

96 In addition, altered lamin A/C expression is found in various cancers.

97 Furthermore, the lamin A/C expression was increased and redistributed to

98 Lamin A/C expression was regulated in vitro by knockdown

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 Mutations in the lamin A/C gene (LMNA) are identified in patients with va

104 Mutations in the lamin A/C gene (LMNA) cause an autosomal dominant inheri

105 Mutations in the lamin A/C gene (LMNA) cause cardiomyopathy and also disr

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

107 Mutations in the lamin A/C gene cause several diseases belonging to the c

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

109 pathogenic mechanism in heart failure due to lamin A/C haploinsufficiency.

110 dually, lamin B1 highlights acute leukemias, lamin A/C helps distinguish normal from neoplastic matur

111 We catalogued all known lamin A/C human mutations and their associated phenotype

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

113 further decouples the roles of chromatin and lamin A/C in compression, showing they separately resist

114 identify a novel interplay between SIRT7 and Lamin A/C in L1 repression.

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

116 Remarkably, mutation of lamin A/C in muscles or motoneurons had no effect on NMJ

117 These results reveal a role of lamin A/C in NMJ maintenance and suggest that nuclear dy

118 These results reveal a role of lamin A/C in NMJ maintenance and suggest that nuclear dy

119 Here, we provide evidence that loss of lamin A/C in skeletal muscles, but not osteoblast (OB)-l

120 pS22-Lamin A/C interacted with a subset of putative active en

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

122 The nuclear lamina protein lamin A/C is a key component of the nuclear envelope.

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

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

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

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

127 Knockdown of hnRNP A1 or lamin A/C led to inhibition of nucleocytoplasmic shuttli

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

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

130 The increased lamin A/C levels in the hearts of SMA mice therefore pro

131 Therapeutic strategies directed at lamin A/C may therefore offer a new approach to target c

132 latory rather than LAD tethering function of Lamin A/C may underlie the pathogenesis of disorders cau

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

134 rovides novel insights into how hnRNP A1 and lamin A/C modulate nucleocytoplasmic shuttling of the AR

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

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

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

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

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

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

141 atal defects are primarily driven by loss of lamin A/C or lamina-associated polypeptide 1 rather than

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

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

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

145 Reports indicate that lamin A/C plays a role in DNA double strand break repair

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

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

148 These results suggest that Lamin A/C regulates gene expression by enhancer binding.

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

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

151 Here we report that hnRNP A1 and lamin A/C serve as carrier and mediator proteins to modu

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

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

154 LMNA encodes nuclear Lamin A/C that tethers lamina-associated domains (LADs)

155 suggest a critical role for skeletal muscle lamin A/C to prevent cellular senescence, IL-6 expressio

156 clear membrane, which further phosphorylates lamin A/C to promote the rearrangement of nuclear lamina

157 channel expression and increased binding of Lamin A/C to the promoter of SCN5A, the channel's gene.

158 We report that Ser22-phosphorylated (pS22) Lamin A/C was localized to the nuclear interior in human

159 this work, the interaction site of p17 with lamin A/C was mapped within the amino terminus (aa 41 to

160 Mutations in the LMNA (lamin A/C) gene have been associated with neuromuscular

161 Mutations in the LMNA gene, encoding LMNA (lamin A/C), are responsible for laminopathies.

162 The A-type lamins (lamin A/C), encoded by the LMNA gene, are important stru

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

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

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

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

167 STATEMENT This study provides evidence that lamin A/C, a scaffolding component of the nuclear envelo

168 In particular, lamin A/C, an intermediate filament protein critical for

169 ivity to 4 antigens, vimentin, beta-tubulin, lamin A/C, and apolipoprotein L2, was significantly diff

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

171 autophagy, which promotes the degradation of lamin A/C, B1, and B2 in iDCs only.

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

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

174 d lamin-depleted MCF-10A cells revealed that lamin A/C, but not lamin B2, protects the nuclear membra

175 in LMNA, which encodes the nuclear proteins Lamin A/C, can cause cardiomyopathy and conduction disor

176 Mutation in the LMNA gene, encoding lamin A/C, causes a diverse group of diseases called lam

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

178 tors LEMD2 or emerin, and to a lesser extent lamin A/C, increased the duration of nucleus ruptures, c

179 nd in the nucleus it directly interacts with lamin A/C, independent of its kinase activity.

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

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

182 Cap to the nuclear membrane to phosphorylate lamin A/C, resulting in a rearrangement of nuclear lamin

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

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

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

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

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

188 /C-binding sites were lost, whereas new pS22-Lamin A/C-binding sites emerged in normally quiescent lo

189 ogeria-patient fibroblasts, a subset of pS22-Lamin A/C-binding sites were lost, whereas new pS22-Lami

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

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

192 atment with the conditioned medium (CM) from lamin A/C-deficient muscle cells.

193 tosidase (SA-beta-gal), p16Ink4a, and p53 in lamin A/C-deficient muscles and C2C12 muscle cells, and

194 6, whose expression is markedly increased in lamin A/C-deficient muscles.

195 ovide evidence for reduced BER efficiency in lamin A/C-depleted cells (Lmna null MEFs and lamin A/C-k

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

197 lamin A/C-depleted cells (Lmna null MEFs and lamin A/C-knockdown U2OS).

198 Knockout (KO) of IL-6 in muscle lamin A/C-KO mice diminishes the deficits in trabecular

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

200 ovide mechanistic insights into hnRNP A1 and lamin A/C-modulated nucleocytoplasmic shuttling of the A

201 ocus restored muscle stem cell properties in lamin A/C-null dystrophic mice.

202 Surprisingly, in contrast to lamin A/C-null mice, SUN2-null mice fail to show coincid

203 ve shorter lifespans than those lacking only lamin A/C.

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

205 7, -8, -9, poly (ADP-ribose) polymerase, and lamin A/C.

206 ncodes the nuclear lamina-associated protein lamin A/C.

207 induce phosphorylation and reorganization of lamin A/C.

208 ith mutations in LMNA, which encodes nuclear lamin A/C.

209 C-CMs) with a haploinsufficient mutation for lamin A/C.

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

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

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

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

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

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

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

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

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

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

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

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

222 substitution mutation in the gene coding for lamin A, causing the production of a toxic isoform calle

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

224 r mechanisms involved in the pathogenesis of lamin A-dependent dystrophies are still largely unknown.

225 d PcG epigenetic silencing and indicate that lamin A-dependent muscular dystrophy can be ascribed to

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

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

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

229 ticity cause rapid and reversible changes in lamin-A, DNA damage, and cell cycle.

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

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

232 zed mechanosensitive markers, but found that lamin A expression, as well as YAP and MRTF-A nuclear tr

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

234 rogeria syndrome, in which a mutation in the lamin A gene yields an altered form of the protein, name

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

236 We show that lamin A has the greatest effect on chromatin viscoelasti

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

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

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

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

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

242 both actomyosin assembly and nucleoskeletal lamin-A increase.

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

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

245 G) of proteins are epigenetic repressors and lamin A interactors, primarily involved in the maintenan

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

247 Lamin A is a component of the inner nuclear membrane tha

248 Lamin A is a nuclear intermediate filament protein criti

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

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

251 Lamin-A is thus stress stabilized to mechano-protect the

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

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

254 Lamin A, lamin C, and progerin, products of the Lmna gen

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

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

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

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

259 elopmental Cell, Cho et al. (2019) find that lamin-A levels in the nuclear envelope are regulated in

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

261 muscular dystrophy (EDMD), we show here that lamin A loss deregulated PcG positioning in muscle satel

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

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

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

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

266 roblasts expressing a cardiomyopathy-causing lamin A mutant.

267 The lamin A mutation further promotes spatial clustering of

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

269 existence of degenerative diseases linked to lamin A mutations suggests that perinuclear binding of c

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

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

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

273 wofold overexpression of the nuclear protein lamin A or we introduce into the cells stiff polystyrene

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

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

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

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

278 on of specific LMNA mutant-driven changes to lamin A phosphorylation and protein structure was perfor

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

280 Here we show that reduction of lamin A/progerin by a single-dose systemic administratio

281 Lamin A protects nuclei from the impact of actomyosin ac

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

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

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

285 pression mechanism where coiled coils in the lamin A rod can slide onto each other to contract rod le

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

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

288 0 nuclear proteins found associated with the lamin A tail, 17 (13%) were previously described lamin A

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

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

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

292 lloprotease-2 (MMP2), and inhibition of this lamin-A turnover and also actomyosin contractility are s

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

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

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

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

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