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The Protein Interaction Network of the Human Transcription Machinery Reveals a Role for the Conserved GTPase RPAP4/GPN1 and Microtubule Assembly in Nuclear Import and Biogenesis of RNA Polymerase II*
RPAP4/GPN1 is a member of a newly discovered GTPase family that contains a unique and highly conserved GPN loop motif that is essential, in conjunction with its GTP-binding motifs, for nuclear localization of POLR2A/RPB1 in a process that also requires microtubule assembly.
A Newly Uncovered Group of Distantly Related Lysine Methyltransferases Preferentially Interact with Molecular Chaperones to Regulate Their Activity
- Philippe Cloutier, M. Lavallée-Adam, D. Faubert, M. Blanchette, B. Coulombe
- BiologyPLoS genetics
- 1 January 2013
A new role for protein methylation as a regulatory pathway for molecular chaperones is uncovered and a novel regulatory mechanism for the chaperone VCP, whose deregulation is causative of degenerative neuromuscular diseases is defined.
hnRNP proteins and splicing control.
- Rebeca D Martínez-Contreras, Philippe Cloutier, L. Shkreta, Jean-François Fisette, T. Revil, B. Chabot
- BiologyAdvances in experimental medicine and biology
Recent advances supporting a role for heterogeneous nuclear RNP proteins in precursor-messenger RNA (pre-mRNA) splicing are discussed.
R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2 to regulate assembly of U5 small nuclear ribonucleoprotein
The use of multiple target affinity purification coupled to mass spectrometry is reported on to identify two additional complexes that interact with R2TP/PFDL: the TSC1–TSC2 complex and the U5 small nuclear ribonucleoprotein (snRNP).
High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes.
Nuclear import of RNA polymerase II is coupled with nucleocytoplasmic shuttling of the RNA polymerase II-associated protein 2
- D. Forget, Andrée-Anne Lacombe, Philippe Cloutier, M. Lavallée-Adam, M. Blanchette, B. Coulombe
- BiologyNucleic acids research
- 30 May 2013
The results have important implications, as they indicate that RPAP2 controls gene expression by two distinct mechanisms, one that targetsRNAP II activity during transcription and the other that controls availability of RNAP II in the nucleus.
Protein Kinase C-Dependent Control of Bcl-x Alternative Splicing
- T. Revil, Johanne Toutant, L. Shkreta, D. Garneau, Philippe Cloutier, B. Chabot
- BiologyMolecular and Cellular Biology
- 8 October 2007
It is reported that the protein kinase C (PKC) inhibitor and apoptotic inducer staurosporine switches the production of Bcl-x towards the xS mRNA isoform in 293 cells, suggesting the existence of factors that couple splicing decisions with PKC signaling.
Transcription Factor IIS Cooperates with the E3 Ligase UBR5 to Ubiquitinate the CDK9 Subunit of the Positive Transcription Elongation Factor B*
- Marilena Cojocaru, A. Bouchard, B. Coulombe
- BiologyThe Journal of Biological Chemistry
- 2 December 2010
UBR5 is identified as a novel E3 ligase that regulates transcription and an additional function of TFIIS in the regulation of CDK9 is defined, indicating that a ternary complex involving these factors participates in the transcriptional regulation of this gene.
New insights into the biogenesis of nuclear RNA polymerases?
Using protein affinity purification coupled to mass spectrometry (AP-MS), a high-density interaction network formed by nuclear RNAP subunits from the soluble fraction of human cell extracts was unraveled and novel interactors that regulate the RNAP II transcription machinery were uncovered, including a set of proteins named the RN AP II-associated proteins (RPAPs).
hnRNP I/PTB can antagonize the splicing repressor activity of SRp30c.
- Caroline Paradis, Philippe Cloutier, L. Shkreta, Johanne Toutant, K. Klarskov, B. Chabot
- 1 August 2007
In vivo results are consistent with the notion that increasing PTB levels alleviates the repression imposed by CE9 to a downstream 3' splice site, and can function as an anti-repressor molecule to counteract the splicing inhibitory activity of SRp30c.