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. 2019 Feb 18;47(8):4211–4225. doi: 10.1093/nar/gkz108

Figure 3.

Figure 3.

Bioinformatic identification and biochemical characterization of PCAT1-associated proteins. (A) Commonly upregulated (fold change > 2.0-fold, P < 0.01) lncRNAs (n = 245) in our Arraystar Human LncRNA Microarray V3.0 data (details in Supplementary Table S5) and possible lncRNAs (n = 92) interacted with FKBP51 protein predicted by the catRAPID omics module. (B) CatRAPID signature module prediction of the RNA-binding propensity for FKBP51 protein followed by prediction of RNA-binding regions. Overall interaction scores above 50% indicate propensity to bind. (C) CatRAPID fragments module prediction of the interaction profile and matrix between FKBP51 protein and PCAT1. (D) IB detection of proteins retrieved by in vitro-transcribed desthiobiotinylated PCAT1 from LNCaP-AI cell lysates. (E) RIP detection of the interaction between FKBP51 and PCAT1 by FKBP51 antibody in LNCaP-AI cells. The level of PCAT1 was determined by qRT-PCR and normalized by the input levels. A P-value of <0.05 was considered significant. *represents P < 0.05, **represents P < 0.01 and ***represents P < 0.001. (F) RT-PCR detection of PCAT1 in LNCaP-AI cell line after PCAT1 knockdown and IB detection of FKBP51, IKKα and PHLPP proteins expression after transfection with lentiviruses carrying PCAT1 shRNA in LNCaP-AI cells.