Bold claim: a newly uncovered protein-RNA interaction could open doors to treating tissue scarring, or fibrosis.
Researchers from Florida State University’s Institute of Molecular Biophysics and Department of Chemistry and Biochemistry have uncovered how a human protein engages with RNA in a way that might guide future anti-fibrosis therapies.
The focus is on LARP6, a La-related protein that helps control the production of type I collagen—the primary structural protein in connective tissues such as skin and bone. When collagen production goes awry, conditions like fibrosis can arise, making LARP6 a meaningful therapeutic target.
The team identified a novel region in LARP6 that enables precise RNA recognition, akin to two puzzle pieces snapping neatly into place. This finding clarifies how LARP6 could be manipulated to curb excess collagen synthesis.
The study appears in Nucleic Acids Research.
We’re essentially studying how two molecular pieces—like LEGO bricks—fit together. As lead researcher Robert Silvers, an assistant professor in the Department of Chemistry and Biochemistry, puts it, the task is more complex than simply fitting shapes: it also involves understanding how different parts move and how those dynamics influence function.
LARP proteins are a broad family found across plants and animals. They bind RNA, the blueprint for building proteins, and help regulate DNA activity. Among the five major human LARPs, LARP6 stands out for its role in collagen production. Compared with its relatives, LARP6 has received less molecular-level scrutiny, especially regarding how it interacts with RNA.
According to Silvers, this study reveals that LARP6 utilizes a distinct interaction mode with RNA and engages a separate RNA-binding site than other LARPs.
The discovery came with the collaboration of Branco Stefanovic from FSU’s College of Medicine, a fibrosis researcher who helped the team approach the problem with multiple observation techniques before settling on NMR spectroscopy.
NMR spectroscopy lets scientists observe molecular complexes in a solution that closely resembles a living organism’s environment, and it captures both structure and dynamic behavior. This approach was particularly important because LARP6 is unstable until it binds RNA, a challenge that NMR is well suited to overcome.
By applying NMR, the researchers demonstrated that the LARP6–RNA interaction directly influences the biosynthesis of type I collagen. In practical terms, this means scientists now have a tangible drug-target—an interface that could be exploited to slow, halt, or modulate fibrosis in the future.
As Silvers notes, the LARP6–RNA complex represents a promising candidate for therapeutic development aimed at fibrosis, a condition that currently lacks a proven drug to effectively slow or stop its progression.
Funding for this work came from the National Institutes of Health.
If you’re curious about what comes next, the key question is whether a small molecule or biologic could selectively disrupt or modulate the LARP6–RNA interaction without harming normal tissue function. Some readers might wonder: should we pursue strategies to broadly suppress collagen synthesis, or target this pathway with precision to treat only fibrotic tissue? Share your thoughts in the comments: would you favor a broad anti-fibrosis approach or a highly targeted intervention that minimizes side effects?
