AI Article Synopsis
- CLEC12A is a receptor involved in immune balance that recognizes MSU crystals released from dying cells, though how it does this was previously unclear.
- Researchers determined the crystal structure of CLEC12A's C-type lectin-like domain and identified a specific area crucial for MSU crystal binding.
- The study also found that CLEC12A clusters at the cell membrane and acts as a receptor that internalizes MSU crystals, offering new insights into their interaction.
Article Abstract
CLEC12A, a member of the C-type lectin receptor family involved in immune homeostasis, recognizes MSU crystals released from dying cells. However, the molecular mechanism underlying the CLEC12A-mediated recognition of MSU crystals remains unclear. Herein, we reported the crystal structure of the human CLEC12A-C-type lectin-like domain (CTLD) and identified a unique "basic patch" site on CLEC12A-CTLD that is necessary for the binding of MSU crystals. Meanwhile, we determined the interaction strength between CLEC12A-CTLD and MSU crystals using single-molecule force spectroscopy. Furthermore, we found that CLEC12A clusters at the cell membrane and seems to serve as an internalizing receptor of MSU crystals. Altogether, these findings provide mechanistic insights for understanding the molecular mechanisms underlying the interplay between CLEC12A and MSU crystals.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10959670 | PMC |
| http://dx.doi.org/10.1016/j.jbc.2024.105765 | DOI Listing |
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