Mutations in the highly similar genes B-cell translocation gene 1 () and are identified in approximately 10-15% of non-Hodgkin lymphoma cases, which may suggest a direct involvement of and in malignant transformation. However, it is unclear whether or how disease-associated mutations impair the function of these genes. Therefore, we selected 16 BTG1 variants based on analysis. We then evaluated (i) the ability of these variants to interact with the known protein-binding partners CNOT7 and CNOT8, which encode the Caf1 catalytic subunit of the Ccr4-Not deadenylase complex; (ii) the activity of the variant proteins in cell cycle progression; (iii) translational repression; and (iv) mRNA degradation. Based on these analyses, we conclude that mutations in may contribute to malignant transformation and tumor cell proliferation by interfering with its anti-proliferative activity and ability to interact with CNOT7 and CNOT8.
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| http://dx.doi.org/10.1080/10428194.2020.1827243 | DOI Listing |
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Article Synopsis
- Protein factors, specifically the nascent polypeptide-associated complex (NAC), bind to ribosomes to aid in protein trafficking and folding in eukaryotes, particularly in yeast like Saccharomyces cerevisiae.
- The NAC consists of two beta subunits, Nacβ1 and a minor Nacβ2, with Nacβ2 playing a crucial role in regulating the messenger RNA (mRNA) of ribosomal protein Rpl4 during translation by interacting with the CCR4-Not complex.
- Research indicates that specific Nacβ2 residues are crucial for its interaction with Caf130, and modifying these residues can significantly impact cell growth, suggesting that the positioning of Nacβ2 is vital for effective mRNA degradation
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