Cells are incredibly busy places! They constantly receive, use, and recycle proteins. One key player in this vital process is the Retriever complex, a protein trio that helps cells efficiently recycle proteins that is cellular recycling of proteins from the plasma membrane (PM).
How Retriever Recycles Proteins
Think of the plasma membrane as a cell’s outer shell. Proteins embedded within it perform many important tasks. However, these proteins don’t last forever. They frequently get internalized into the endosomal compartment, where they are either recycled back to the PM or sent off for degradation.
The Role of Retriever
The Retriever complex—composed of VPS35L, VPS26C, and VPS29—acts as a crucial traffic controller. It specifically identifies proteins destined for recycling, preventing their premature breakdown.
Retriever vs. Retromer
Interestingly, Retriever is related to another recycling complex, Retromer. However, they work with different sets of proteins. Retriever handles a broader range, including integrins, tyrosine receptor kinases, and G-protein coupled receptors (GPCRs), while Retromer focuses on a distinct group of cargoes. Both complexes, however, work alongside the WASH regulatory complex to ensure efficient sorting.
The SNX17 Connection and Beyond
Scientists recently uncovered more about Retriever’s workings. A protein called SNX17 plays a critical role in connecting Retriever to specific proteins for recycling. Studies revealed that SNX17’s C-terminal tail is essential for this interaction. Furthermore, research using cryo-electron microscopy (cryo-EM) has revealed the structure of the Retriever-SNX17 complex, offering a detailed look at how they interact.
Cargo Binding and Regulation
Interestingly, scientists found that SNX17’s interaction with Retriever is regulated by its own FERM domain and cargo binding. It appears that cargo binding influences whether the SNX17 tail is available to interact with Retriever. This regulatory mechanism adds another layer of complexity to cellular protein recycling.
More Ligands Discovered
Moreover, the study unveiled additional proteins that interact with Retriever, suggesting that this complex might play an even broader role in cellular processes than previously anticipated. This adds to the understanding of the complex interplay within cellular systems. This discovery opens up new avenues for research into cell biology and has potential implications for understanding and treating various diseases.
Reference
Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., Juneja, P., Billadeau, D. D., Bai, X., Chen, Z., Turer, E. E., Burstein, E., & Chen, B. (2024). Structural basis for Retriever-SNX17 assembly and endosomal sorting. Nature Communications, 15(1). https://doi.org/10.1038/s41467-024-54583-6
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