FSU researchers discover new protein-RNA interaction with potential to treat fibrosis

脡abha Phelan, Bill Wellock

Tue, 12/16/25
Robert Silvers is an assistant professor in the Department of Chemistry and Biochemistry.
Robert Silvers is an assistant professor in the Department of Chemistry and Biochemistry.

A research team at 糖心vlog鈥檚  and  has discovered how a protein found in the human body interacts with RNA in a way that could lead to new treatments for tissue scarring also known as fibrosis.

The researchers studied a special protein called LARP6, which plays a role in how our bodies produce type I collagen, a key building block in tissues like skin and bones. This protein is important because it鈥檚 linked to diseases where too much collagen is made, such as fibrosis.

They discovered a new part of the protein that helps it recognize and stick to the RNA very precisely, like two puzzle pieces fitting perfectly. The study gives scientists a clearer picture of how LARP6 might be targeted in treatments for diseases involving collagen overproduction.

The work was published in .

鈥淚n the simplest terms, we鈥檙e trying to figure out how two molecules, just like LEGO pieces, fit together,鈥 said principal investigator Robert Silvers, an assistant professor in the Department of Chemistry and Biochemistry. 鈥淏ut it鈥檚 obviously much more complicated than that, because we鈥檙e not just considering the structure of the LEGO pieces and how they fit together, but also how different parts of the LEGO pieces move around, and that all ties directly into functionality.鈥

A diagram showing two versions of the Human LARP6 protein. The unbound version is not attached to RNA. The bound version is attached to an RNA, forming a tight, water-repelling core, which makes the protein more rigid and stable.
A diagram showing two versions of the Human LARP6 protein. The unbound version is not attached to RNA. The bound version is attached to an RNA, forming a tight, water-repelling core, which makes the protein more rigid and stable.

LARPs, or La-related proteins, are a superfamily of proteins common in all plants and animals. They bind RNA, the molecule that carries genetic information, helps build proteins and regulates the function of DNA. LARP6 is one of five main human LARP proteins and is involved in the regulation and biosynthesis of collagen. Compared to other LARPs, there has been very little research into how LARP6 interacts with RNA on a molecular level.

鈥淥ur new 鈥楲EGO piece鈥 uses a different kind of interaction with its RNA,鈥 said Silvers. 鈥淚t utilizes a different set of rules and the protein uses a different RNA binding site altogether.鈥

The team was introduced to this unusual LARP by Branco Stefanovic, a professor in the , who has spent much of his career researching fibrosis. They attempted multiple methods of observing the protein, such as X-ray crystallography, before landing on NMR spectroscopy.

鈥淚n NMR spectroscopy, we can look at the complex in solution close to its natural environment under physiological conditions,鈥 said Silvers. 鈥淣MR spectroscopy is ideal as we can study the dynamics of a molecule as well as its structure.鈥

NMR spectroscopy is a method that uses the magnetic properties of certain nuclei to reveal a molecule鈥檚 detailed structure and properties. It proved especially useful because LARP6 is unstable until it binds with RNA.

Using NMR spectroscopy, the researchers found that the way LARP6 binds to RNA is directly involved in the biosynthesis of type I collagen, the protein involved in fibrosis. This discovery could help scientists develop a treatment for fibrosis in the future.

鈥淏ecause of its function, the complex between LARP6 and RNA is something that we potentially can develop a drug for, to work against fibrosis,鈥 said Silvers. 鈥淭here is currently no drug, to my knowledge, that can slow down or stop the progression of fibrosis.鈥

This research was funded by the National Institutes of Health.

La-related proteins diagram

Most La-related proteins bind to a single strand of RNA in a particular location on the protein, as known as the 鈥渃anonical鈥 binding site. In contrast, the LARP6 protein found in humans binds to a more complex RNA using a previously unknown and unique location, known as the 鈥渘oncanonical鈥 binding site. This affects how certain cells synthesize type I collagen, a protein involved in fibrosis. Understanding the unique characteristics of LARP6 could help scientists develop a treatment for fibrosis in the future.

FSU Health is a transformational initiative to improve health in Florida by leveraging 糖心vlog鈥檚 cutting-edge research capabilities and academic offerings to forge new collaborations with clinical partners.

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