Fig. 5. Expression of either dFMRP or human FMRP does not induce eIF2α phosphorylation.(A) Analysis of eIF2α phosphorylation upon dFMRP expression. Expression.

Slides:

Advertisements

Similar presentations

Overexpression of PAI‐1 reverses the arsenite‐mediated effect on senescence Overexpression of PAI‐1 reverses the arsenite‐mediated effect on senescence.

Advertisements

Sec1p requires Boi1/2p for proper localization.

Calcium regulates ERK nuclear association, but not its activation.

The ΔrlmA mutant strain has impaired CWI pathway activation.

Endogenous SRP19 is localized to the nucleus and the nucleolus.

Volume 14, Issue 1, Pages (January 2004)

Volume 21, Issue 10, Pages (December 2017)

HRTV and SFTSV NSs, but not UUKV NSs, inhibits JAK/STAT IFN signaling.

Neurotensin receptor–1 and –3 complex modulates the cellular signaling of neurotensin in the HT29 cell line Stéphane Martin, Valérie Navarro, Jean Pierre.

Volume 19, Issue 7, Pages (July 2012)

Volume 3, Issue 2, Pages (February 2006)

Fig. 3. HECTD2 contains a naturally occurring polymorphism at A19, which mislocalizes to the cytosol. HECTD2 contains a naturally occurring polymorphism.

Volume 62, Issue 4, Pages (May 2016)

Endogenous SMN1 is not recruited to stress granules in HeLa cells after diverse stresses. Endogenous SMN1 is not recruited to stress granules in HeLa cells.

Inducible DM1 model displays increased autophagy.

Fig. 1. Representative images of the four cell lines using fluorescence microscopy. Representative images of the four cell lines using fluorescence microscopy.

Fig. 2. Morphological changes of cultured adherent fibroblastic cells after OA treatment related to actin microfilament reorganization.(A) Cells observed.

The histidine-rich loop regulates accessibility of the active site and RDEL motif in vivo. The histidine-rich loop regulates accessibility of the active.

A highly conserved six-amino-acid region in the C-terminal CT domain of MARCH8 is responsible for its ability to downregulate TfR. A highly conserved six-amino-acid.

Fig. 2. Histone H3 phosphorylation appears at prometaphase upon C4 treatment.(A) Western blots were realized on cells synchronized at mitotic entry in.

The effects of a dominant negative mutant of lamin B1 on lamin distribution in HeLa cells. The effects of a dominant negative mutant of lamin B1 on lamin.

Colocalization of the palmitoylation-deficient mutants of claudin-14 with the lysosomal membrane protein LAMP-2. Colocalization of the palmitoylation-deficient.

Fig. 1. Lack of Hmga1 and Hmga2 expression in A1/A2-KO mice

Fig. 7. E2F1 acetylation in A1/A2-KO MEFs

Fig. 4. Detection of dFMR1 mRNA in dFMRP granules by FISH

Fig. 2. Ex vivo inducible knockout of PDCD2 in ESCs results in loss of S phase entry and increased p53.(A) Growth curve of inducible knockout and WT ESCs.

Fig. 6. Effect of SAHA and ML on histone acetylation, BAX, and p21CDKN1A expression.PANC-1 and BxPC-3 cells were incubated for 48 hours with 5 µM.

FAK tyrosine phosphorylation is unaffected by loss of LAR activity.

Fig. 3. Rnd proteins induce stronger responses in subconfluent endothelial cells.HUVECs were transfected with Rnd1, Rnd2, Rnd3 or GFP-encoding plasmids.

Fig. 10. A mutant clone homozygous for mip120LL07629 has greatly diminished Mip120 protein levels. hsFLP/+; FRT42B, mip120LL07629/FRT42B, Ubi-GFP-nls females.

ICAM-1 forms distinct complexes with filamin B, α-actinin-4 and cortactin. ICAM-1 forms distinct complexes with filamin B, α-actinin-4 and cortactin. (A)

Fig. 1. TSA at 165 nM induces maximal acetylation of histone H3 and near-maximal acetylation of histone H4.Immunoblot analysis of acetylated histones H3.

GFP–Sec61b mRNA competes with t-ftz mRNA for the ribosome-binding sites on the ER. (A,B) COS7 cells were transfected with plasmid containing a test gene.

Figure 4 DNM1 mutations affect protein levels and self-dimerization (A) HeLa cells were transfected with green fluorescent protein (GFP)-tagged mutant.

RXRa serves as a carrier for TR3 translocation initiated by 9-cis retinoic acid. RXRa serves as a carrier for TR3 translocation initiated by 9-cis retinoic.

Fig. 3. Overexpression of wild-type GFP-CPAP, but not GFP-CPAP-377EE (GFP-377EE), induces cilia formation and promotes the growth of cilia.CAD cells (A,B)

ArfGAP1 expression alters GBF1 recruitment to Golgi membranes.

Crim1 colocalizes with integrin and activates the integrin-FAK-ERK signaling pathway. Crim1 colocalizes with integrin and activates the integrin-FAK-ERK.

Oral administration of CX-4945 suppresses Tau phosphorylation in DYRK1A-overexpressing mice. Oral administration of CX-4945 suppresses Tau phosphorylation.

Mechanism of Akt1 in promoting reprogramming.

Analysis of Cdc7p at the end of meiosis.

Dissociation of HP1α from H3K9me3 is critical to potentiation of steady-state ATM activity. Dissociation of HP1α from H3K9me3 is critical to potentiation.

Tau–RFP–RBPs colocalize with mRNA on microtubules and lead to the wetting of stress granules on microtubules. Tau–RFP–RBPs colocalize with mRNA on microtubules.

SLK/LOK-phosphorylated and activated ezrin prevents MISP localization at the cell cortex. SLK/LOK-phosphorylated and activated ezrin prevents MISP localization.

Expression of active Rho partially rescues Erk1/2 activation and peripheral FA phenotype in RIAM-knockdown cells. Expression of active Rho partially rescues.

Lysine residues in the cytoplasmic region of TfR are involved in the MARCH8-induced downregulation of TfR. Lysine residues in the cytoplasmic region of.

Effect of the siRNA-mediated knockdown of endogenous MARCH8 on the expression levels of MARCH8 substrates, TfR and CD98, in HepG2 cells. Effect of the.

Wrch-1 binds to the regulatory p85 subunit of PI3K and is necessary for Akt activation. Wrch-1 binds to the regulatory p85 subunit of PI3K and is necessary.

Fig. 2. Acetylation stiffens primary cilia.

Fig. 1. Cell adhesion molecule expression and the aggregation of wildtype and mutant ES cells.(A) Wildtype (WT), E-cadherin null (9J), and N-cadherin null.

Fig. 1. p85β localizes at adhesion plaques and associates with FAK

Association of NM-HA and NM-GFP with SGs is transient.

WT MARCH8, but not the CS mutant, specifically ubiquitinates and downregulates TfR. WT MARCH8, but not the CS mutant, specifically ubiquitinates and downregulates.

Fig. 4. Tetracycline-regulated expression of ClC-5 in the HEK293 cells stably expressing gastric H+,K+-ATPase.(A) Alignments of rat ClC-5, human ClC-5,

The regulatory domain of HSF1 is involved in the pro-apoptotic response to TNF. (A) Upper panel, functional domains and potential DAPK phosphorylation.

Fig. 7. Analysis of dFMRP kinetics in dFMRP granules by FRAP

Generation of an inducible form of FOXN1.

Ca2+-mediated differentiation of primary mouse keratinocytes is independent of epiplakin. Ca2+-mediated differentiation of primary mouse keratinocytes.

Effect of ERα Ub-binding ability on E2-induced receptor transcriptional activity. Effect of ERα Ub-binding ability on E2-induced receptor transcriptional.

Mutant MFN2 proteins have normal half-lives and are properly localized to mitochondria. Mutant MFN2 proteins have normal half-lives and are properly localized.

Volume 23, Issue 2, Pages (August 2005)

Fig. 8 C9orf72 knockdown results in an increase in autophagic flux.

Fig. 3 C9ORF72 interacts with SMCR8 in a DENN domain–dependent manner.

PKCζ is tyrosine phosphorylated by EGF and contributes to EGF-induced activation of ERK in Mef cells. PKCζ is tyrosine phosphorylated by EGF and contributes.

Expression of dominant-negative RasN17 completely suppresses Ras activation in Rh1 cells. Expression of dominant-negative RasN17 completely suppresses.

Fig. 5 C9orf72 knockdown disrupts autophagy induction.

SAHA blocks IR-induced increase of RAD51 protein in MM cells.

The interaction of PALB2 with BRCA1 is required for the assembly of PALB2, BRCA2, and RAD51 nuclear foci. The interaction of PALB2 with BRCA1 is required.

Expression and induction of HER2 and HPSE in 231BMBC cells.

EGF induces HPSE nucleolar localization in human BMBC cells.

Presentation transcript:

Fig. 5. Expression of either dFMRP or human FMRP does not induce eIF2α phosphorylation.(A) Analysis of eIF2α phosphorylation upon dFMRP expression. Expression of either dFMRP or human FMRP does not induce eIF2α phosphorylation.(A) Analysis of eIF2α phosphorylation upon dFMRP expression. Following transfection with GFP-dFMRP or its mutants, Schneider cells were lysed and protein content was analyzed by immunoblotting for GFP-dFMRP expression using anti-GFP antibodies. Phosphorylation of eIF2α was analyzed by western blot (P-eIF2α; center panel) using specific antibodies. An extract isolated from arsenite-treated Schneider cells was used as a positive control for eIF2α phosphorylation. Total eIF2α was analyzed using the pan-eIF2α antibodies and used as a loading control (bottom panel). The amount of phosphorylated eIF2α was determined by quantitation of the film signals by densitometry using the Adobe Photoshop and expressed as a percentage of total eIF2α. The results are representative of 5 different experiments. (B) Expression of GFP-hFMRP in HeLa cells induces FMRP granules. Cells expressing GFP-hFMRP or GFP alone were processed for fluorescence to detect GFP or GFP-hFMRP (green). The intracellular localization of the FMRP partner FXR1 in FMRP granules (red) was revealed by immunofluorescence using specific antibodies. The indicated percentage of FMRP granules that are induced by expressing GFP-hFMRP in HeLa cells is representative of 3 different experiments. (C) Analysis of eIF2α phosphorylation upon dFMRP expression. HeLa cells expressing GFP-hFMRP or GFP alone were collected and their protein extracts prepared for western blot analysis of eIF2α phosphorylation and of eIF2α (as loading control) using specific antibodies (bottom panels). GFP-hFMRP and endogenous FMRP were detected using anti-FMRP antibodies (top panel). GFP was detected using anti-GFP antibodies, which also detect the GFP-hFMRP fusion (center panel). The indicated amount of phosphorylated eIF2α was quantified as described in Fig. 2A. (D–H) GFP-hFMRP induces FMRP granules independently of eIF2α phosphorylation. (D) MEF-eIF2α A/A and its WT counterpart cell line were transfected with either GFP or GFP-hFMRP. Cells were then collected and their protein extracts were analyzed by western blotting for the expression of GFP-hFMRP and endogenous mFMRP using anti-FMRP antibodies. (E,G) Expression of GFP-hFMRP induces FMRP granules in both MEF eIF2α A/A (E) and its WT MEF counterparts (G). Cells expressing GFP or GFP-hFMRP were processed for confocal microscopy for GFP and GFP-hFMRP detection (green). The intracellular localization of the FMRP partner FXR1 in FMRP granules (red) is revealed by immunofluorescence using specific antibodies. The indicated percentage of FMRP granules that are induced by expressing GFP-hFMRP in MEF-eIF2a A/A and their WT MEF counterparts is representative of 3 different experiments. (F,H) The indicated cells expressing GFP or GFP-hFMRP were collected and their protein extracts prepared for western blot analysis of eIF2α phosphorylation and of eIF2α as a loading control using specific antibodies. Arsenite treatment was used as a positive control for eIF2α phosphorylation. The indicated percentage of phosphorylated eIF2α was calculated as described in Fig. 5A. Scale bars in B,E,G: 10 µm. Cristina Gareau et al. Biology Open 2013;2:68-81 © 2012. Published by The Company of Biologists Ltd