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Fig. 4 | Acta Neuropathologica Communications

Fig. 4

From: C9orf72-associated SMCR8 protein binds in the ubiquitin pathway and with proteins linked with neurological disease

Fig. 4

Immunofluorescence microscopy shows evidence for association of endogenous SMCR8 protein with cytoplasmic aggregates. a FLAG-tagged SMCR8 and RFP-tagged ubiquitin transfected in 2102Ep cells colocalize in a structure consistent with the aggresome. b Overexpression of V5-tagged C9orf72 does not induce stress granule formation in unstressed U2OS cells. c Exogenously expressed HA-SMCR8 protein is not observed in SGs of U2OS cells stressed with NaAsO2. d WDR41-FL protein does not colocalize with SG marker protein TIA1 in U2OS cells stressed with NaAsO2. e Endogenous C9orf72 protein detercted by the α-SMCR8-SC antibody does not colocalize with SGs in NaAsO2-stressed U2OS cells (see also Fig. S4E). f Endogenous C9orf72 protein detected by the C9-L antibody [54] does not colocalize with SGs in DTT-stressed U2OS cells. g,h Endogenous SMCR8 detected by the α-SMCR8-ab202283 antibody localizes to SGs of stressed (h), but not unstressed (g) U2OS cells (see also Fig. S4G-I). i The α-WDR41-SC antibody does not detect endogenous protein in SGs of NaAsO2-stressed 2102Ep cells. NT: no treatment. Cell nuclei were stained with Hoechst 33342 (right-most panels). Size bars are 10 μm

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