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Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
Published on: October 7, 2021
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CacyBP/SIP - RPL6 interaction: potential influence on ribosome function
Ewelina Jurewicz1, Małgorzata Maksymowicz-Trivedi1, Omid Saberi-Khomami1
1Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Street, Warsaw, 02-093, Poland.
Amino Acids
|July 21, 2025
Summary
CacyBP/SIP directly interacts with ribosomal protein RPL6, impacting ribosome function and protein synthesis. Silencing CacyBP/SIP reduced nascent polypeptide synthesis and altered stress response in neuroblastoma cells.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- CacyBP/SIP (also known as CacyBP) has a previously identified interaction with NPM1, a key player in ribosome biogenesis.
- This study investigates the role of CacyBP/SIP in the broader context of ribosome biogenesis and function.
Purpose of the Study:
- To determine the impact of CacyBP/SIP on ribosome biogenesis and function.
- To identify potential ribosomal protein targets of CacyBP/SIP.
- To elucidate the functional consequences of CacyBP/SIP-ribosome interactions on protein synthesis.
Main Methods:
- Mass spectrometry to identify CacyBP/SIP interacting partners.
- Biochemical assays to confirm direct interaction between CacyBP/SIP and RPL6.
- In silico analysis to map protein-binding domains.
- O-propargyl-puromycin (OPP) labeling to assess nascent polypeptide synthesis.
- Heat shock experiments to evaluate stress-induced protein production (Hsp70) in CacyBP/SIP-silenced cells.
Main Results:
- Mass spectrometry identified several ribosomal proteins (RPs) as potential CacyBP/SIP targets, with RPL6 showing high-quality scores.
- Biochemical and in silico methods confirmed a direct interaction between CacyBP/SIP and RPL6, identifying involved protein domains.
- CacyBP/SIP silencing in neuroblastoma cells led to a significant decrease in cells exhibiting perinuclear staining for nascent polypeptides.
- CacyBP/SIP-silenced cells showed markedly higher Hsp70 production under heat shock compared to control cells, suggesting impaired protein synthesis regulation.
Conclusions:
- CacyBP/SIP directly interacts with RPL6 and potentially other RPs.
- CacyBP/SIP appears to play a role in ribosome function and the efficiency of protein synthesis.
- The findings suggest CacyBP/SIP's involvement in cellular protein synthesis regulation, possibly via its interaction with ribosomal components.
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