T H E J O U R N A L O F C E L L B I O L O G Y
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1 Supplemental material Chairoungdua et al., T H E J O U R N A L O F C E L L B I O L O G Y Figure S1. Expression of CD9 and CD82 inhibits Wnt/ -catenin signaling activated by Wnt3a condition medium. HEK 293T cells stably expressing CD9, CD82, or empty vector were transfected with TOPflash and the Renilla luciferase vector and incubated with Wnt3a conditioned medium (Wnt3a-CM) for 24 h. Activity of the -catenin signaling pathway was quantified by measuring relative firefly luciferase activity units (RLUs) normalized to Renilla luciferase. Data are presented as the fold change as compared with the control condition (cells transfected with pcdna3.1 empty vector and not exposed to Wnt3a-CM). S1
2 Figure S2. CD9 and CD82 inhibition of Wnt/ -catenin signaling is GSK-3 independent. (A) CD9 and CD82 but not CD63 inhibit TOPflash activity stimulated by mutant S45 -catenin. 24 h after transfection with the indicated plasmids, cells were harvested for TOPflash luciferase assay. Data are presented as the fold change as compared with the control condition (transfected with empty vector pcdna3.1 alone). (B) CD9 and CD82 reduce cytosolic and nuclear pools of mutant S45 -catenin protein. Cell fractions prepared from HEK 293T cells transfected with the indicated plasmids were immunoblotted using anti-xpress ( -catenin) and anti -actin antibodies. (C and D) 12 h after transfection with TOPflash, Renilla luciferase vector, and the indicated plasmids, HEK 293T cells were treated with NaCl (50 mm), LiCl (50 mm), SB (20 µm), or DMSO (SB216763( )) for 12 h. Activity of the -catenin signaling pathway was quantified by measuring relative firefly luciferase activity units (RLUs) normalized to Renilla luciferase. Data are presented as the fold change as compared with the control conditions (transfected with empty vector pcdna3.1 and not exposed to SB or LiCl). S2
3 Figure S3. The targeting of b-catenin into exosomes does not require either TSAP6 or ESCRT components. (A) Exosome-associated -catenin resides within the lumens of exosome vesicles. Exosomes recovered from untransfected or from CD82-transfected HEK293 cells were incubated with or without 0.05% trypsin for 30 min at 20 C in the absence or presence of 1% Triton X-100. The exosome protein was separated by SDS-PAGE, transferred to nitrocellulose, and analyzed by Western blotting using an antibody directed against -catenin. In the absence of the detergent the -catenin associated with CD82-induced exosomes is protected from trypsin, whereas in the presence of the detergent the -catenin is completely degraded. Thus, exosome-associated - catenin resides within the lumens of the exosome vesicles. (B) Overexpression of TSAP6 has no effect on CD82-induced exosome release of -catenin. Exosomes were purified from HEK 293T cells cotransfected with the indicated plasmids. Equal amounts of exosome protein (1 µg) were analyzed by Western blotting with the indicated antibodies. (C) ESCRT-independent release of -catenin. Exosomes were purified from HEK 293T cells cotransfected with the indicated plasmids encoding wild-type and dominant-negative versions of ESCRT complex components. Total lysate and exosome fractions were analyzed for -catenin by Western blotting. S3
4 Figure S4. CD82 interacts with -catenin. HEK 293T cells were transfected with the indicated plasmids. -Catenin was detected in anti-flag immunoprecipitates from FLAG-CD82 stably transfected cells and not from cells transfected with empty FLAG vector (A) or FLAG-CD63 (B). S4
5 Figure S5. Exosome release of -catenin is E-cadherin dependent. Purified exosomes from CHO cells cotransfected with wild-type -catenin (A) or mutant S33Y -catenin (B) and the indicated plasmids were analyzed by Western blotting. The exosome release of both wild-type -catenin and mutant S33Y catenin is E-cadherin dependent. (C) Effects of CD9 on exosome release in vivo. Exosomes were purified from BMDCs derived from CD9 wild-type and knockout mice as described in Materials and methods and analyzed by transmission electron microscopy. The average number of morphologically recognizable exosomes present per medium power field was determined using five separate images from each of three separate preparations of exosomes from wild-type and CD9 nulls. Three times as many exosomes are detectable in micrographs of material derived from wild-type versus CD9 null cells. S5
Supplementary Figure 1.TRIM33 binds β-catenin in the nucleus. a & b, Co-IP of endogenous TRIM33 with β-catenin in HT-29 cells (a) and HEK 293T cells
Supplementary Figure 1.TRIM33 binds β-catenin in the nucleus. a & b, Co-IP of endogenous TRIM33 with β-catenin in HT-29 cells (a) and HEK 293T cells (b). TRIM33 was immunoprecipitated, and the amount of
More informationCD82 and CD9 are tetraspanin membrane proteins
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A 7 6 5 4 3 2 1 DMSO DAPT 1..8.6.4.2 C 1 2 3 4 JAGFC (ug/ml) D 5 6 JAG1Fc Wnt1 CM Fold change in expression 1..8.6.4.2 *** 1..8.6.4.2 * JAG1Fc Wnt1 CM JAG1Fc Dvl2 Fig. S1. Dishevelled inhibits Notch signalling.
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Supplementary Figure S A) The blots shown in Figure B were qualified by using Gel-Pro analyzer software (Rockville, MD, USA). The ratio of LC3II/LC3I to actin was then calculated. The data are represented
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Supplementary Table 1. Cell sphingolipids and S1P bound to endogenous TRAF2. Sphingolipid Cell pmol/mg TRAF2 immunoprecipitate pmol/mg Sphingomyelin 4200 ± 250 Not detected Monohexosylceramide 311 ± 18
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SUPPLEMENTAL FIGURE LEGENDS Supplemental Figure S1: Endogenous interaction between RNF2 and H2AX: Whole cell extracts from 293T were subjected to immunoprecipitation with anti-rnf2 or anti-γ-h2ax antibodies
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SUPPLEMENTARY FIGURE 1 0 20 50 80 100 IL-17RD (ng) S1a S1b S1c IL-17RD β-actin kda S1d - si sc Il17rd Il17ra rig/s15-574 - 458-361 bp S1f S1g S1h S1i S1j Supplementary Figure 1. Knockdown of IL-17RD enhances
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SUPPLEMENTARY METHODS 3D culture and cell proliferation- MiaPaCa-2 cell culture in 3D was performed as described previously (1). Briefly, 8-well glass chamber slides were evenly coated with 50 µl/well
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Supplementary Figure Legends Figure S1. Tankyrase inhibition suppresses cell proliferation in an axin/β-catenin independent manner. (A) SW480, DLD1, RKO and HCT116 cells were treated with DMSO or XAV939
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SUPPLEMENTARY FIGURES AND TABLE Supplementary Figure S1: Characterization of IRE1α mutants. A. U87-LUC cells were transduced with the lentiviral vector containing the GFP sequence (U87-LUC Tet-ON GFP).
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More informationTel: ; Fax: ;
Tel.: +98 216 696 9291; Fax: +98 216 696 9291; E-mail: mrasadeghi@pasteur.ac.ir Tel: +98 916 113 7679; Fax: +98 613 333 6380; E-mail: abakhshi_e@ajums.ac.ir A Soluble Chromatin-bound MOI 0 1 5 0 1 5 HDAC2
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doi:10.1038/nature11700 Figure 1: RIP3 as a potential Sirt2 interacting protein. Transfected Flag-tagged Sirt2 was immunoprecipitated from cells and eluted from the Sepharose beads using Flag peptide.
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Supplementary figure legends Supplementary Figure 1. Expression of Shh signaling components in a panel of gastric cancer. (A) RT-PCR for components of the Shh/Gli pathway in normal fetus cell (MRC-5) and
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Supplementary Materials Supplementary Figure S1 Regulation of Ubl4A stability by its assembly partner A, The translation rate of Ubl4A is not affected in the absence of Bag6. Control, Bag6 and Ubl4A CRISPR
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Supplementary Figure 1 YAP negatively regulates IFN- signaling. (a) Immunoblot analysis of Yap knockdown efficiency with sh-yap (#1 to #4 independent constructs) in Raw264.7 cells. (b) IFN- -Luc and PRDs
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Shao-Ming Shen et al Role of I in MT of cancers MO reports xpanded View igures igure V1. nalysis of the expression of I isoforms in cancer cells and their interaction with PTN. RT PR detection of Ish and
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MO reports PR3 dephosphorylates TZ Xian-o Lv et al xpanded View igures igure V1. PR3 dephosphorylates and inactivates YP/TZ., Overexpression of tight junction proteins Pals1 () or LIN7 () has no effect
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DOI:.38/ncb2822 a MTC02 FAO cells EEA1 b +/+ MEFs /DAPI -/- MEFs /DAPI -/- MEFs //DAPI c HEK 293 cells WCE N M C P AKT TBC1D7 Lamin A/C EEA1 VDAC d HeLa cells WCE N M C P AKT Lamin A/C EEA1 VDAC Figure
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Supplementary Figure 1 Supplementary Figure 1. Neither the activation nor suppression of the MAPK pathway affects the ASK1/Vif interaction. (a, b) HEK293 cells were cotransfected with plasmids encoding
More information293T cells were transfected with indicated expression vectors and the whole-cell extracts were subjected
SUPPLEMENTARY INFORMATION Supplementary Figure 1. Formation of a complex between Slo1 and CRL4A CRBN E3 ligase. (a) HEK 293T cells were transfected with indicated expression vectors and the whole-cell
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doi: 10.1038/nature05732 SUPPLEMENTARY INFORMATION Supplemental Data Supplement Figure Legends Figure S1. RIG-I 2CARD undergo robust ubiquitination a, (top) At 48 h posttransfection with a GST, GST-RIG-I-2CARD
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Supplemental Figure 1 1a 1c PD-1 MFI fold change 6 5 4 3 2 1 IL-1α IL-2 IL-4 IL-6 IL-1 IL-12 IL-13 IL-15 IL-17 IL-18 IL-21 IL-23 IFN-α Mut Human PD-1 promoter SBE-D 5 -GTCTG- -1.2kb SBE-P -CAGAC- -1.kb
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Figure S1. (A) SDS-PAGE separation of GST-fusion proteins purified from E.coli BL21 strain is shown. An equal amount of GST-tag control, LRRK2 LRR and LRRK2 WD40 GST fusion proteins (5 µg) were loaded
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SUPPLEMENTARY FIGURE LEGENDS Supplemental FIG. 1. Localization of myosin Vb in cultured neurons varies with maturation stage. A and B, localization of myosin Vb in cultured hippocampal neurons. A, in DIV
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SUPPLEMENTARY MATERIAL AND METHODS Soft Agar Assay. For each cell pool, 100,000 cells were resuspended in 0.35% (w/v) top agar (LONZA, SeaKem LE Agarose cat.5004) and plated onto 0.5% (w/v) basal agar.
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Supplemental Figure Legends Supplemental Figure 1. Western blot analysis indicated that was detected in the fractions of plasma membrane and cytosol but not in nuclear fraction isolated from Pkd1 null
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Figure S1 Nucleotide binding status of RagA mutants. Wild type and mutant forms of MycRagA was transfected into HEK293 cells and the transfected cells were labeled with 32 Pphosphate. MycRagA was immunoprecipitated
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Supplementary Figure 1 Constitutive EGFR signaling does not activate canonical EGFR signals (a) U251EGFRInd cells with or without tetracycline exposure (24h, 1µg/ml) were treated with EGF for 15 minutes
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SUPPLEMENTARY INFORMATION doi:1.138/nature9814 a A SHARPIN FL B SHARPIN ΔNZF C SHARPIN T38L, F39V b His-SHARPIN FL -1xUb -2xUb -4xUb α-his c Linear 4xUb -SHARPIN FL -SHARPIN TF_LV -SHARPINΔNZF -SHARPIN
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Table S1. Primer sequences used for qrt-pcr. ACTB LCOR KLF6 CTBP1 CDKN1A CDH1 ATF3 PLAU MMP9 TFPI2 CACCATTGGCAATGAGCGGTTC AGGTCTTTGCGGATGTCCACGT AAGTCCATGTGCTGGCAGCACT ATCACCACTCCGAAGTCCGTCT CGGCTGCAGGAAAGTTTACA
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