RNA-binding protein PCBP2 modulates glioma growth by regulating FHL3

Han, Wei; Xin, Zhongshuai; Zhao, Zhiqiang; Wen, Bo; Lin, Xihua; Yin, Bin; Zhao, Jizong; Yuan, Jing; Qiang, Boqin; Peng, Xiaozhong

doi:10.1172/jci61820

Cited by 90 publications

(84 citation statements)

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“…3D), compatible with the RNAbinding properties of PCBP2 (Du et al 2005). Based upon its noncoding binding topology, PCBP2 appears to have broad regulatory scope through interaction with 18S rRNA as well as serving as a translational regulator in both cancer (Eiring et al 2010;Han et al 2013) and infectious disease (Gamarnik and Andino 2000;Herold and Andino 2001;Shetty et al 2013).…”

Section: Resultsmentioning

confidence: 82%

“…We applied this Fully Automated and Standardized iCLIP (FAST-iCLIP) pipeline to a published iCLIP data set of the RBP hnRNP-C, recapitulating the published biology of this protein. We then applied FAST-iCLIP to the human and viral interactomes of Poly-C binding protein 2 (PCBP2), a KH domain (hnRNP-K homology) (Lunde et al 2007) containing RBP that has a preference for C/Urich motifs (Choi et al 2009) as well as pathological associations in cancer (Eiring et al 2010;Han et al 2013) and infectious disease (Gamarnik and Andino 2000;Herold and Andino 2001;Shetty et al 2013). The unbiased characterization of the PCBP2 protein revealed novel RNAprotein interactions and provided supporting evidence for previously known cellular and viral roles for PCBP2.…”

Section: Introductionmentioning

confidence: 78%

“…PCBP2 has a preference for C-rich motifs (Choi et al 2009) and notable association with infectious disease (Han et al 2013). PCBP2 was a favorable target, as features of its biology are well understood, but no CLIP-seq study has been reported to date (Waggoner and Liebhaber 2003;Han et al 2013). We performed FAST-iCLIP in the human Huh-7 (human hepatoma) cells and processed the data, revealing that the majority (2116) of targets were mRNAs with 68% of reads found within 3 ′ UTRs ( Fig.…”

Section: Resultsmentioning

confidence: 99%

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Dissecting noncoding and pathogen RNA–protein interactomes

Flynn

Martin

Spitale

et al. 2014

RNA

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RNA-protein interactions are central to biological regulation. Cross-linking immunoprecipitation (CLIP)-seq is a powerful tool for genome-wide interrogation of RNA-protein interactomes, but current CLIP methods are limited by challenging biochemical steps and fail to detect many classes of noncoding and nonhuman RNAs. Here we present FAST-iCLIP, an integrated pipeline with improved CLIP biochemistry and an automated informatic pipeline for comprehensive analysis across protein coding, noncoding, repetitive, retroviral, and nonhuman transcriptomes. FAST-iCLIP of Poly-C binding protein 2 (PCBP2) showed that PCBP2-bound CU-rich motifs in different topologies to recognize mRNAs and noncoding RNAs with distinct biological functions. FAST-iCLIP of PCBP2 in hepatitis C virus-infected cells enabled a joint analysis of the PCBP2 interactome with host and viral RNAs and their interplay. These results show that FAST-iCLIP can be used to rapidly discover and decipher mechanisms of RNA-protein recognition across the diversity of human and pathogen RNAs.

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Section: Resultsmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 78%

Section: Resultsmentioning

confidence: 99%

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Dissecting noncoding and pathogen RNA–protein interactomes

Flynn

Martin

Spitale

et al. 2014

RNA

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“…Many RNA-binding proteins have important roles in the initiation and progression of glioblastoma, including LIN28 (7), PCBP2 (8), HuR (9-11), Quaking (12), and Musashi1 (MSI1) (13)(14)(15)(16)(17)(18)(19)(20)(21). Among these, MSI1 stands out due to its evolutionary conservation, connection to neural stem cells, and role in balancing self-renewal and differentiation (18,(22)(23)(24)(25)(26).…”

mentioning

confidence: 99%

RNA-Binding Protein Musashi1 Is a Central Regulator of Adhesion Pathways in Glioblastoma

Uren

Araújo

et al. 2015

Molecular and Cellular Biology

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The conserved RNA-binding protein Musashi1 (MSI1) has emerged as a key oncogenic factor in numerous solid tumors, including glioblastoma. However, its mechanism of action has not yet been established comprehensively. To identify its target genes comprehensively and determine the main routes by which it influences glioblastoma phenotypes, we conducted individualnucleotide resolution cross-linking and immunoprecipitation (iCLIP) experiments. We confirmed that MSI1 has a preference for UAG sequences contained in a particular structural context, especially in 3= untranslated regions. Although numerous binding sites were also identified in intronic sequences, our RNA transcriptome sequencing analysis does not favor the idea that MSI1 is a major regulator of splicing in glioblastoma cells. MSI1 target mRNAs encode proteins that function in multiple pathways of cell proliferation and cell adhesion. Since these associations indicate potentially new roles for MSI1, we investigated its impact on glioblastoma cell adhesion, morphology, migration, and invasion. These processes are known to underpin the spread and relapse of glioblastoma, in contrast to other tumors where metastasis is the main driver of recurrence and progression.

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“…PCBP2 could also function indirectly by inhibiting the expression or activation of proteases that might cleave Mst1. PCBP2 depletion by siRNA is associated with activation of apoptotic markers in HeLa and glioma cells (36,37); thus, both mechanisms may be at work.…”

Section: Discussionmentioning

confidence: 99%