scholarly journals An Essential Nuclear Protein in Trypanosomes Is a Component of mRNA Transcription/Export Pathway

PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e20730 ◽  
Author(s):  
Mariana Serpeloni ◽  
Carolina Borsoi Moraes ◽  
João Renato Carvalho Muniz ◽  
Maria Cristina Machado Motta ◽  
Augusto Savio Peixoto Ramos ◽  
...  
Keyword(s):  
Nuclear Protein ◽  
Mrna Transcription ◽  
Export Pathway

scholarly journals Adenovirus E4orf6 targets pp32/LANP to control the fate of ARE-containing mRNAs by perturbing the CRM1-dependent mechanism

2005 ◽  
Vol 170 (1) ◽  
pp. 15-20 ◽  
Author(s):  
Fumihiro Higashino ◽  
Mariko Aoyagi ◽  
Akiko Takahashi ◽  
Masaho Ishino ◽  
Masato Taoka ◽  
...  
Keyword(s):  
Nuclear Protein ◽  
Cyclooxygenase 2 ◽  
Viral Mrnas ◽  
Binding Partner ◽  
Export Pathway ◽  
Cytokine Mrnas ◽  
Dependent Mechanism

E4orf6 plays an important role in the transportation of cellular and viral mRNAs and is known as an oncogene product of adenovirus. Here, we show that E4orf6 interacts with pp32/leucine-rich acidic nuclear protein (LANP). E4orf6 exports pp32/LANP from the nucleus to the cytoplasm with its binding partner, HuR, which binds to an AU-rich element (ARE) present within many protooncogene and cytokine mRNAs. We found that ARE-mRNAs, such as c-fos, c-myc, and cyclooxygenase-2, were also exported to and stabilized in the cytoplasm of E4orf6-expressing cells. The oncodomain of E4orf6 was necessary for both binding to pp32/LANP and effect for ARE-mRNA. C-fos mRNA was exported together with E4orf6, E1B-55kD, pp32/LANP, and HuR proteins. Moreover, inhibition of the CRM1-dependent export pathway failed to block the export of ARE-mRNAs mediated by E4orf6. Thus, E4orf6 interacts with pp32/LANP to modulate the fate of ARE-mRNAs by altering the CRM1-dependent export pathway.

scholarly journals Chromatin association of XRCC5/6 in the absence of DNA damage depends on the XPE gene product DDB2

2017 ◽  
Vol 28 (1) ◽  
pp. 192-200 ◽  
Author(s):  
Damiano Fantini ◽  
Shuo Huang ◽  
John M. Asara ◽  
Srilata Bagchi ◽  
Pradip Raychaudhuri
Keyword(s):  
Colon Cancer ◽  
Dna Damage ◽  
Nuclear Protein ◽  
Excision Repair ◽  
Regulatory Function ◽  
Colon Cancer Cells ◽  
Mrna Transcription ◽  
Protein Partners ◽  
Transcriptional Regulatory ◽  
Nucleotide Excision

Damaged DNA-binding protein 2 (DDB2), a nuclear protein, participates in both nucleotide excision repair and mRNA transcription. The transcriptional regulatory function of DDB2 is significant in colon cancer, as it regulates metastasis. To characterize the mechanism by which DDB2 participates in transcription, we investigated the protein partners in colon cancer cells. Here we show that DDB2 abundantly associates with XRCC5/6, not involving CUL4 and DNA-PKcs. A DNA-damaging agent that induces DNA double-stranded breaks (DSBs) does not affect the interaction between DDB2 and XRCC5. In addition, DSB-induced nuclear enrichment or chromatin association of XRCC5 does not involve DDB2, suggesting that the DDB2/XRCC5/6 complex represents a distinct pool of XRCC5/6 that is not directly involved in DNA break repair (NHEJ). In the absence of DNA damage, on the other hand, chromatin association of XRCC5 requires DDB2. We show that DDB2 recruits XRCC5 onto the promoter of SEMA3A, a DDB2-stimulated gene. Moreover, depletion of XRCC5 inhibits SEMA3A expression without affecting expression of VEGFA, a repression target of DDB2. Together our results show that DDB2 is critical for chromatin association of XRCC5/6 in the absence of DNA damage and provide evidence that XRCC5/6 are functional partners of DDB2 in its transcriptional stimulatory activity.

scholarly journals Nuclear protein export pathway in aging therapeutics

Aging ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 4682-4684
Author(s):  
Bulmaro Cisneros ◽  
Ian García-Aguirre
Keyword(s):  
Nuclear Protein ◽  
Protein Export ◽  
Export Pathway
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