Functional characterization of the ribonucleoprotein, PTB-binding 1/Raver1 promoter region

Lorenzi, Pamela; Avesani, Francesca; Morandi, Carlo

doi:10.1016/j.gene.2007.09.004

Cited by 9 publications

(6 citation statements)

References 43 publications

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“…3, panel B) shows that human Raver2 gene is strictly related to its ortholog in chimpanzee, forming one clade that diverged most recently in the phylogeny. In previously published results, we have shown that in comparing the 5′ upstream sequences of Raver1 ortholog genes, several conserved sequences were shared not only between human and chimpanzee but with other species as well (Romanelli et al, 2007). These results indicate that although Raver1 and Raver2 may play similar functions as co-factors of the alternative splicing regulator PTB, their roles can be distinguished during divergent evolution in primates on the basis of tissue-specific requirements and development.…”

Section: Raver2 Mrna Expression In Human and Mouse Tissuessupporting

confidence: 51%

Transcriptional regulation of the human Raver2 ribonucleoprotein gene

Romanelli

Lorenzi

Diani

et al. 2012

Gene

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Section: Raver2 Mrna Expression In Human and Mouse Tissuessupporting

confidence: 51%

Transcriptional regulation of the human Raver2 ribonucleoprotein gene

Romanelli

Lorenzi

Diani

et al. 2012

Gene

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“…A cooperative action in regulating adjacent exons has been confirmed by the structural model of PTB RRM2 bound to the Raver1 peptide [43]. The human Raver 1 gene is ubiquitously expressed in tissues at different levels and encodes a 748 amino acid protein containing three RRMs, two nuclear localization signals (NLSs), one nuclear export sequence and a proline-rich region at its C -terminal region [58,62,63]. Similarly to PTB, Raver1 is a shuttle-protein.…”

Section: Ptb Paralogs and Co-factorsmentioning

confidence: 99%

“…Raver2 expression is restricted to differentiated neurons and glia cells. We have recently contributed to the characterization of Raver1 and Raver2 promoters and to the identification of cis -acting signals [62,67]. In contrast to Raver1, which binds to cytosolic proteins, so far there is no evidence of a Raver2 interaction with cytoplasmic proteins.…”

Section: Ptb Paralogs and Co-factorsmentioning

confidence: 99%

New Insights into Functional Roles of the Polypyrimidine Tract-Binding Protein

Romanelli

Diani

Lievens

2013

IJMS

114

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Polypyrimidine Tract Binding Protein (PTB) is an intensely studied RNA binding protein involved in several post-transcriptional regulatory events of gene expression. Initially described as a pre-mRNA splicing regulator, PTB is now widely accepted as a multifunctional protein shuttling between nucleus and cytoplasm. Accordingly, PTB can interact with selected RNA targets, structural elements and proteins. There is increasing evidence that PTB and its paralog PTBP2 play a major role as repressors of alternatively spliced exons, whose transcription is tissue-regulated. In addition to alternative splicing, PTB is involved in almost all steps of mRNA metabolism, including polyadenylation, mRNA stability and initiation of protein translation. Furthermore, it is well established that PTB recruitment in internal ribosome entry site (IRES) activates the translation of picornaviral and cellular proteins. Detailed studies of the structural properties of PTB have contributed to our understanding of the mechanism of RNA binding by RNA Recognition Motif (RRM) domains. In the present review, we will describe the structural properties of PTB, its paralogs and co-factors, the role in post-transcriptional regulation and actions in cell differentiation and pathogenesis. Defining the multifunctional roles of PTB will contribute to the understanding of key regulatory events in gene expression.

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“…One of the most investigated repressors of exon recognition is the polypyrimidine tract‐binding protein (PTB) [3]. We have previously characterized the regulatory region required for PTB gene expression and for its cofactors Raver1 and Raver2 [4–6]. Both SR and hnRNPs proteins are structurally organized in modular domains represented by one or more RNA recognition motifs (RRMs), plus additional protein motifs required for nucleic acids or protein–protein interactions and subcellular localization [7,8].…”

Section: Introductionmentioning

confidence: 99%

Identification of nuclear retention domains in the RBM20 protein

Filippello¹,

Lorenzi²,

Bergamo³

et al. 2013

FEBS Letters

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Edited by Ulrike KutayKeywords: RBM20 DCM Alternative splicing Nuclear localization Ribonucleoprotein SR a b s t r a c t RBM20 is a nuclear protein which regulates alternative splicing of expressed genes that have a key role in cardiac function. By cloning the human and mouse RBM20 cDNA, producing expressing vectors for truncated proteins, and comparing their sub-cellular distribution in transfected cells, we have identified the sequences necessary for RBM20 full nuclear retention. The region overlaps an RNA binding motif and a serine-arginine domain. The sequence is conserved in many species but belongs only to RBM20 orthologs. The RMB20 tissue specificity, together with the properties of its nuclear localization determinant, demonstrates a specific evolutionary selection of post-transcriptional regulation factors.

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Functional characterization of the ribonucleoprotein, PTB-binding 1/Raver1 promoter region

Cited by 9 publications

References 43 publications

Transcriptional regulation of the human Raver2 ribonucleoprotein gene

Transcriptional regulation of the human Raver2 ribonucleoprotein gene

New Insights into Functional Roles of the Polypyrimidine Tract-Binding Protein

Identification of nuclear retention domains in the RBM20 protein

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