A new protein–RNA connection uncovered, with potential to combat fibrosis
Researchers from Florida State University’s Institute of Molecular Biophysics and the Department of Chemistry and Biochemistry have identified a novel way a human protein interacts with RNA that could open doors to treatments for tissue scarring, known as fibrosis.
The focus is on a protein called LARP6, which influences how the body makes type I collagen—the primary component of connective tissues such as skin and bone. Because excessive collagen production is linked to fibrotic diseases, understanding LARP6’s behavior is particularly important.
The team pinpointed a previously unrecognized segment of LARP6 that enables precise recognition and binding to RNA, functioning like two puzzle pieces that fit together perfectly. This discovery provides a clearer blueprint for designing strategies that target LARP6 in conditions driven by collagen overproduction.
The findings were published in Nucleic Acids Research.
In the words of lead investigator Robert Silvers, an assistant professor in the Chemistry and Biochemistry Department, the team is essentially asking, “How do two molecules, much like LEGO bricks, lock together?” He adds that the reality is more intricate because scientists must account not only for the shapes of the molecules but also for how their different parts move and interact, which ultimately governs their function.
LARPs, or La-related proteins, constitute a broad family present across plants and animals. They bind RNA, influence how genetic information is used to build proteins, and regulate DNA activity. Among the human LARPs, LARP6 stands out for its role in managing collagen production. Until now, there has been relatively little research detailing how LARP6 engages with RNA at the molecular level.
“Our latest finding shows that this ‘LEGO piece’ operates via a distinct mode of interaction with RNA,” Silvers notes. “It follows its own rules and uses a binding site on RNA that’s different from other LARPs.”
Bringing this unusual LARP into view was Branco Stefanovic, a professor at the FSU College of Medicine, whose fibrosis research has spanned many years. Before converging on a method suitable for studying the protein, the researchers attempted several techniques, including X-ray crystallography, and ultimately turned to nuclear magnetic resonance (NMR) spectroscopy.
With NMR, they could examine the protein–RNA complex in solution, in an environment close to physiological conditions, which helps reveal both structural details and dynamic behavior. This approach was particularly valuable because LARP6 is unstable on its own and stabilizes upon RNA binding.
The NMR results demonstrated that the LARP6–RNA interaction plays a direct role in the synthesis of type I collagen, linking the new molecular insight to a pathway involved in fibrosis. This connection points to the possibility of developing fibrosis therapies that target this specific complex in the future.
Silvers emphasizes that, given its function, the LARP6–RNA complex represents a promising drug target for antifibrotic strategies. He notes that at present there is no known medication capable of slowing or halting fibrosis progression.
Funding for this work came from the National Institutes of Health.
Public release note: This material reflects information available at the time of the original report and has been edited for clarity, style, and length. Mirage.News does not endorse any positions or conclusions beyond those of the original authors.
