PSF and p54<sup>nrb</sup>/NonO – multi‐functional nuclear proteins

Shav‐Tal, Yaron; Zipori, Dov

doi:10.1016/s0014-5793(02)03447-6

Cited by 310 publications

(332 citation statements)

References 57 publications

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“…These two accessory splicing factors also bind RNAPII and other transcription factors (Shav-Tal and Zipori, 2002) as well as N-WASP (Wu et al, 2006), whose down-regulation prevents HoxB induction by RA (Figure 2). Although in a different cell model (HeLa cells), we show that Prep1 and Pbx1 bind p54Nrb and that the resulting complex still binds DNA ( Figure 5B), which indicates that these proteins can be recruited to the same DNA target sequence.…”

Section: Discussionmentioning

confidence: 99%

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Induction of HoxB Transcription by Retinoic Acid Requires Actin Polymerization

Ferrai

Naum-Onganía

Longobardi

et al. 2009

MBoC

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We have analyzed the role of actin polymerization in retinoic acid (RA)-induced HoxB transcription, which is mediated by the HoxB regulator Prep1. RA induction of the HoxB genes can be prevented by the inhibition of actin polymerization. Importantly, inhibition of actin polymerization specifically affects the transcription of inducible Hox genes, but not that of their transcriptional regulators, the RARs, nor of constitutively expressed, nor of actively transcribed Hox genes. RA treatment induces the recruitment to the HoxB2 gene enhancer of a complex composed of "elongating" RNAPII, Prep1, ␤-actin, and N-WASP as well as the accessory splicing components p54Nrb and PSF. We show that inhibition of actin polymerization prevents such recruitment. We conclude that inducible Hox genes are selectively sensitive to the inhibition of actin polymerization and that actin polymerization is required for the assembly of a transcription complex on the regulatory region of the Hox genes.

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Section: Discussionmentioning

confidence: 99%

“…In the nucleus, N-WASP is associated with p54Nrb-PSF (Wu et al, 2006), a protein complex that interacts with both RNAPII and the splicing machinery (Shav-Tal and Zipori, 2002). We therefore tested the association of Prep1 with p54Nrb-PSF.…”

Section: N-wasp Down-regulation Inhibits the Expression Of The Hoxb Cmentioning

confidence: 99%

Induction of HoxB Transcription by Retinoic Acid Requires Actin Polymerization

Ferrai

Naum-Onganía

Longobardi

et al. 2009

MBoC

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“…Like many other proteins, such as polypyrimidine tract-binding protein-associated splicing factor (PSF/p100) (40) and heterogeneous nuclear ribonucleoprotein units/SAF-A (41-45), SAFB1 is involved in transcription, mRNA stability and/or processing, and chromatin regulation. SAFB1 has been shown previously to bind DNA (2), and here we show that it is also able to bind RNA.…”

Section: Discussionmentioning

confidence: 99%

Structure-Function Analysis of the Estrogen Receptor α Corepressor Scaffold Attachment Factor-B1

Townson

Kang

Lee

et al. 2004

Journal of Biological Chemistry

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Scaffold attachment factor-B1 (SAFB1) is a nuclear matrix protein that has been proposed to couple chromatin structure, transcription, and RNA processing. We have previously shown that SAFB1 can repress estrogen receptor (ER␣)-mediated transactivation. Here we present a structure-function study showing that transactivation is mediated via an intrinsic and transferable Cterminal repression domain (RD). A similar C-terminal RD was found in the family member SAFB2. Removal of the RD from SAFB1 resulted in a dominant-negative SAFB1 protein that increased ligand-dependent and -independent ER␣ activity. SAFB1RD-mediated repression was partly blocked by histone deacetylase inhibitors; however, no histone deacetylase inhibitors were identified in a yeast two-hybrid screen using the RD as bait. Instead, SAFB1RD was found to interact with TAFII68, a member of the basal transcription machinery. We propose a model in which SAFB1 represses ER␣ activity via indirect association with histone deacetylation and interaction with the basal transcription machinery.SAFB1 1 belongs to a family of nuclear proteins that are localized in the nuclear matrix. The matrix is a proteinaceous structure consisting of a network of ribonucleoproteins and non-histone proteins, such as transcription factors, that serve as a scaffold for the higher organization of chromatin into loop structures (1). A characteristic of SAFB family members is the presence of an N-terminal SAF box (2-4) that binds to DNA regulatory regions termed scaffold/matrix attachment regions (S/MARs). S/MARs are bound to the nuclear matrix, define the loop structure of higher order chromatin (5-8), divide the genome into structural and functional domains, and are implicated in the regulation of gene expression (1).SAFB proteins contain a central RNA recognition motive (RRM), which suggests a role in mRNA processing. Because SAFB1 also has been shown to interact with members of the RNA processing machinery and with RNA polymerase II, it has been suggested that this protein is part of a "transcriptosome" complex, coupling chromatin structure to transcription and RNA processing (9 -12).We have previously reported that SAFB1 plays an important role in breast cancer because its overexpression results in growth inhibition (13). SAFB1 maps to a chromosomal locus that displays unusually high rates of loss of heterozygosity (14), and mutations have been identified in breast tumors (14). We have also shown that SAFB1 can bind to and repress transcriptional activity of the estrogen receptor ␣ (ER␣), thereby functioning as an ER␣ corepressor (15).ER␣ is a steroid receptor that regulates transcription of genes involved in proliferation, apoptosis, migration, and other cellular processes (16). ER␣ corepressors and coactivators are components of large protein complexes that tightly control the activity of ER␣ (17,18). Although the role of coactivators in the activity of ER␣ is well established, the role of ER␣ corepressors is less clear. Based on recent studies, it is believed that ER␣ corepr...

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“…The interactions of these proteins thus allow the Apaf-1 IRES RNA to attain the correct structural conformation for ribosome recruitment by creating a single-stranded region, which allows the ribosome-landing site to become accessible metvinculin, and also interacts with PTB to regulate splicing; 57,58 hnRNP-L, a PTB homologue that was found to bind PTB in a yeast two-hybrid screen; 59 PSF (PTB-associated splicing factor) and p54 nrb /NonO are related multifunctional nuclear factors that contain both RNA-binding and DNAbinding functions. 60 Other ITAFs that help to regulate IRES-mediated expression of proteins that function during apoptosis include PCBP2 and hnRNPK. In combination with PCBP1, these interact specifically with regions of the c-myc IRES, and increase internal translation initiation.…”

Section: Analysis Of Mrnas That Remain Polysomally Associated During mentioning

confidence: 99%

Internal ribosome entry segment-mediated translation during apoptosis: the role of IRES-trans-acting factors

et al. 2005

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During apoptosis, there is a reduction in translation initiation caused by caspase cleavage of several of the factors required for the cap-dependent scanning mechanism. Under these circumstances, many proteins that are required for apoptosis are instead translated by the alternative method of internal ribosome entry. This mechanism requires the formation of a complex RNA structural element and in the presence of internal ribosome entry segment (IRES)-trans-acting factors (ITAFs), the ribosome is recruited to the RNA. The interactions of several ITAFs with IRESs have been investigated in detail, and several mechanisms of action have been noted, including acting as chaperones, stabilising and remodelling the RNA structure. Structural remodelling by PTB in particular will be discussed, and how this protein is able to facilitate recruitment of the ribosome to several IRESs by causing previously occluded sites to become more accessible.

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PSF and p54^nrb/NonO – multi‐functional nuclear proteins

Cited by 310 publications

References 57 publications

Induction of HoxB Transcription by Retinoic Acid Requires Actin Polymerization

Induction of HoxB Transcription by Retinoic Acid Requires Actin Polymerization

Structure-Function Analysis of the Estrogen Receptor α Corepressor Scaffold Attachment Factor-B1

Internal ribosome entry segment-mediated translation during apoptosis: the role of IRES-trans-acting factors

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PSF and p54nrb/NonO – multi‐functional nuclear proteins

Cited by 310 publications

References 57 publications

Induction of HoxB Transcription by Retinoic Acid Requires Actin Polymerization

Induction of HoxB Transcription by Retinoic Acid Requires Actin Polymerization

Structure-Function Analysis of the Estrogen Receptor α Corepressor Scaffold Attachment Factor-B1

Internal ribosome entry segment-mediated translation during apoptosis: the role of IRES-trans-acting factors

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PSF and p54^nrb/NonO – multi‐functional nuclear proteins